Pubmed abstracts for Protein-Protein Interaction search result :

Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.65713304
In pea ( Pisum sativum ) , chloroplast cpn 10 was identified by its ability to ( 1 ) assist bacterial chaperonin 60 ( cpn 60 ; also known as groEL ) in the ATP dependent refolding of chemically denatured ribulose 1 , 5 bisphosphate carboxylase and ( 2 ) form a stable complex with bacterial cpn 60 in the presence of Mg . 0.65713304^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.52135287
These data indicate that mAb 54G8 appears to bind at or near the end of the B . pertussis cpn 60 molecule and that binding of mAb 54G8 at this location affects the ability of cpn 10 to productively interact with cpn 60 , most likely either by sterically blocking the binding of cpn 10 , by affecting the conformation of cpn 60 in such a way that it no longer binds cpn 10 , or by inhibiting proper transduction of the effects of cpn 10 binding . . 0.52135287^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.82310117
Chaperone hsp 10 also interacted with hsp 60 and ALDH 2 ( 1 ) and ALDH 2 ( 2 ) , but again the interactions were weak ones . . 0.82310117^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :1.1513243
In contrast , a symmetrical complex formed between one GroEL and two GroES oligomers , with substrate protein binding to the outer surface of GroEL , was recently proposed to be the functional chaperonin unit . 1.1513243^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.55325687
In the absence of groES and MgATP , the two isozymes interact differently with groEL , groEL arrests the refolding of mAspAT throughout the temperature range of 0 45 degrees C . 0.55325687^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.58552351
In the presence of nucleotide , GroES forms a 1 : 1 complex with GroEL which binds unfolded protein in its central cavity and releases it to allow folding upon ATP hydrolysis . 0.58552351^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.72921445
After a single cycle of ATP hydrolysis by the adenosine triphosphatase ( ATPase ) activity of GroEL , the bi toroidal GroEL formed a stable asymmetric ternary complex with GroES and nucleotide ( bulletlike structures ) . 0.72921445^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.67517247
The specific mechanism of GroE facilitated folding involves numerous interactions between GroEL , GroES , the refolding protein , and ATP . 0.67517247^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.65192282
The chaperonin GroEL can assist protein folding and normally acts with the co chaperonin GroES . 0.65192282^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.64987436
It has been believed that when GroEL binds to GroES its apical domain moves upward and outward . 0.64987436^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.55393953
We find that GroEL bound substrate polypeptide can induce GroES cycling on and off GroEL in the presence of ADP . 0.55393953^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.71855115
The interaction of GroEL with GroES in the presence of Mg2+ ADP eliminates the destabilizing effect of ADP on the GroEL molecule against the action of temperature and Ellman ' s reagent but does not change its hydrophobicity and accessibility to trypsin . . 0.71855115^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.6004498
The three dimensional structure of the GroES monomer and its interaction with GroEL has been predicted using a combination of prediction tools and experimental data obtained by biophysical [ electron microscope ( EM ) , Fourier transform infrared ( FTIR ) , and nuclear magnetic resonance ( NMR ) ] and biochemical techniques . 0.6004498^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.61086427
In Escherichia coli , asymmetric intermediates of GroEL are formed with the co chaperonin GroES and nucleotides bound only to one of the seven subunit rings ( the cis ring ) and not to the opposing ring ( the trans ring ) . 0.61086427^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.54605562
In the presence of ATP , GroES binds to GroEL , forming a large chamber that encapsulates substrate proteins for folding . 0.54605562^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.6505896
Structural models of the complex between GroEL and its co chaperonin GroES , and of the isolated apical domain of GroEL ( minichaperone ; residues 191 376 ) with a 17 residue N terminal tag show that a linear sequential sequence ( extended beta strand ) can be bound . 0.6505896^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.77934647
This loop is responsible for the interaction between GroES and GroEL , and it undergoes a folding transition upon binding to GroEL . 0.77934647^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.56529876
GroES interacts with GroEL through selective hydrophobic residues present on its mobile loop region , and we have considered the group of residues on the GroES mobile loop as the key element in choosing a substrate for GroEL . 0.56529876^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The two proteins , one a GroEL homologue ( cpn 60 : M . glycogenes 60 kDa chaperonin ) and the other a GroES homologue ( cpn 10 : M . glycogenes 10 kDa chaperonin ) , composed a heteropolymeric complex in the presence of ATP . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Oligomeric cpn 10 on top of two layers of cpn 60 rings with two stripes each . ^^^ A structural model of holo chaperonin , known as a protein folding control protein comprising 60 kDa ( cpn 60 ) and 10 kDa polypeptides ( cpn 10 ) , is proposed based on the electron microscopic images of holo chaperonin from Thermus thermophilus and cpn 60 from Paracoccus denitrificans . ^^^ We conclude that a single cpn 60 heptamer ring with two stripes stacks into two layers , and a cpn 10 oligomer binds to one side of the layers . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
We conclude that Hsp 10 is a eukaryotic Cpn 10 homologue and , therefore , together with Cpn 60 essential for mitochondrial protein biogenesis . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
GroEL 140 retained its ability to bind non native ribulose bisphosphate carboxylase / oxygenase ( Rbu P 2 carboxylase ) , but released bound proteins upon addition of ATP and GroES ( cpn 10 ) 6 7 fold less efficiently compared to GroEL . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Rhodanese that had been inactivated by incubation at 48 degrees C , in the presence of cpn 60 can be reactivated at 25 degrees C , upon addition of cpn 10 , K+ , and MgATP . ^^^ However , optimal chaperonin assisted refolding of rhodanese observed at 25 degrees C , which is achieved upon addition of cpn 10 and ATP to the cpn 60 rhodanese complex , is independent of the temperature of preincubation of the complex , that was formed previously at low temperature . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
A stable complex of the chaperonins , cpn 60 and cpn 10 ( Escherichia coli GroEL and GroES homologues ) , from the extremely thermophilic bacterium Thermus thermophilus has been isolated and crystallized . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Implications with respect to dependence of chloroplast cpn 60 function on cpn 10 are discussed . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The cpn 60 that had been covalently modified with NEM or IAANS , was not able to support the chaperonin assisted refolding of the mitochondrial enzyme rhodanese , which also requires cpn 10 and ATP hydrolysis . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
X . , & Kiefhaber , T . , 1991 , Biochemistry 30 , 1586 1591 ) that refolding of CS is facilitated by the GroE system ( an Escherichia coli chaperonin [ cpn ] that is composed of GroEL [ cpn 60 ] and GroES [ cpn 10 ] ) has been confirmed . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
In vitro refolding of the urea unfolded , monomeric , mitochondrial enzyme rhodanese ( thiosulfate sulfur transferase ; EC 2 . 8 . 1 . 1 ) is facilitated by the chaperonin proteins cpn 60 and cpn 10 from Escherichia coli at 37 degrees C , but the refolding is strongly inhibited at 10 degrees C . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Instrumental to its identification , mitochondrial cpn 10 and bacterial cpn 60 form a stable complex in the presence of Mg . ^^^ Bacterial and mitochondrial cpn 10 compete for a common saturable site on bacterial cpn 60 . ^^^ As a result of complex formation , with either mitochondrial or bacterial cpn 10 , the `` uncoupled ATPase ' ' activity of bacterial cpn 60 is virtually abolished . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
In addition to their presence in the cellular compartments of the secretory pathway , the chaperonins cpn 10 and cpn 60 were found to also be concentrated in the RER intracisternal crystals . ^^^ These labeling patterns suggest a participation of the chaperonins cpn 10 and cpn 60 but not of the hsp 70 in the aberrant aggregation of secretory proteins leading to RER crystal formation . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Utilizing the ability of bacterial chaperonin 60 ( GroEL ) to functionally interact with chaperonin 10 ( Cpn 10 ) homologues in an ATP dependent fashion , we have purified substantial amounts of mammalian , chloroplast , and thermophilic Cpn 10 homologues from their natural host . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Holo chaperonin molecule from Thermus thermophilus is a bullet shaped particle whose cylinder part and round top are composed of two stacked rings of the cpn 60 heptamer and a single ring of the cpn 10 heptamer , respectively . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The ability of the two proteins to refold from 8 M urea to enzymatically active species was similar both for unassisted refolding , and when folding was assisted either by the detergent , lauryl maltoside or by the E . coli chaperonin system composed of cpn 60 and cpn 10 . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The binding of nucleotides and chaperonin 10 ( cpn 10 ) to the Escherichia coli chaperonin 60 ( cpn 60 ) and their effect upon the molecular symmetry has been examined both kinetically and at equilibrium . ^^^ ATP binds tightly and is hydrolysed on only one heptameric ring of the cpn 60 tetradecamer at a time , thus inducing asymmetry in the cpn 60 oligomer even in the absence of cpn 10 . ^^^ In the absence of cpn 10 these seven ATP molecules hydrolyse to form a cpn 60 : ADP 7 complex in which ADP is tightly bound ( Kd = 2 7 microM ) ; further ADP binding to form a cpn 60 : ADP 14 complex is weak ( K1 / 2 = 2 . 3 mM ) . ^^^ When cpn 60 is mixed with cpn 10 and ATP the resultant cpn 60 : ATP 7 : cpn 10 complex is formed rapidly ( the rate constant for cpn 10 association is > 4 10 10 ( 7 ) M 1 s 1 ) and before ATP is hydrolysed ( k = 0 . 12 s 1 per active subunit ) to produce an extremely stable cpn 60 : ADP 7 : cpn 10 complex . ^^^ In `` trapping ' ' experiments , where the cpn 60 : ADP 7 : cpn 10 is challenged with ATP , cpn 10 was observed to dissociate at a rate identical to that of steady state ATP hydrolysis in the presence of cpn 10 ( k = 0 . 042 s 1 per active subunit ) . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The deduced amino acid sequence of each ORF has strong homologies to the heat shock proteins / chaperonins Cpn 60 and Cpn 10 . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Cochaperonins ( cpn 10 ) assist chaperonins ( cpn 60 ) in mediating folding of polypeptide substrates in an ATP dependent reaction . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Productive binding of several precursors with a positively charged amino terminal matrix targeting sequence , such as SU 9 DHFR , hsp 60 , and mitochondrial cpn 10 , was strongly inhibited by salt , by low concentrations of a mitochondrial presequence peptide , and by a deletion of Mas20p , but was independent of Mas37p / Mas70p . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Chaperonin 60 ( cpn 60 ) and chaperonin 10 ( cpn 10 ) constitute the chaperonin system in prokaryotes , mitochondria , and chloroplasts . ^^^ When dimeric ribulose 1 , 5 bisphosphate carboxylase ( Rubisco ) is denatured and allowed to bind to yeast cpn 60 , subsequent refolding of Rubisco is strictly dependent upon yeast cpn 10 . ^^^ The heterologous combination of cpn 60 from E . coli plus yeast cpn 10 is also functional . ^^^ In contrast , yeast cpn 60 plus E . coli cpn 10 do not support refolding of Rubisco . ^^^ In the presence of MgATP , yeast cpn 60 and yeast cpn 10 form a stable complex that can be isolated by gel filtration and that facilitates refolding of denatured Rubisco . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
This antibody , previously shown to affect the ability of chaperonin 10 ( cpn 10 ) to inhibit the ATPase activity of cpn 60 , is attached at the ends of the cpn 60 and links the molecules into long chains . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Chaperonin mediated , in vitro folding of rhodanese by the intact protein cpn 60 has previously been shown to require cpn 10 and ATP hydrolysis ( Martin , J . , Langer , T . , Boteva , R . , Schramel , A . , Horwich , A . ^^^ The present work demonstrates that the rhodanese cpn 60 complex can be dissociated by urea to allow folding to proceed , thus removing the obligatory requirement for cpn 10 and ATP . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Two further hybridizing clones were analysed and found to consist of two additional cpn 60 sequences plus upstream regions containing putative cpn 10 genes . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The hydrophilic and stable cMDH is bound by cpn 60 but released by Mg ATP alone , while the hydrophobic and unstable mMDH requires both Mg ATP and cpn 10 . ^^^ The yield and rate of folding of cMDH is unaffected while that of mMDH is markedly increased by the presence of cpn 60 , cpn 10 and Mg ATP . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The incubation of chaperonins cpn 60 ( GroEL ) and cpn 10 ( GroES ) from E . coli in the presence of Mg ATP and KCl generates the formation , as revealed by electron microscopy , of GroEL GroES complexes with a symmetrical shape in which one toroidal GroES oligomer is bound to each end of the tetradecameric GroEL aggregate ( 1 : 2 GroEL : GroES oligomer molar ratio ) . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Molecular chaperones in pancreatic tissue : the presence of cpn 10 , cpn 60 and hsp 70 in distinct compartments along the secretory pathway of the acinar cells . ^^^ Three chaperones , the chaperonins cpn 10 and cpn 60 , and the hsp 70 protein , were revealed by immunochemistry and cytochemistry in pancreatic rat acinar cells . ^^^ Western immunoblotting analysis of rat pancreas homogenates has shown that antibodies against cpn 10 , cpn 60 and hsp 70 protein recognize single protein bands of 25 kDa , 60 kDa and 70 kDa , respectively . ^^^ Single bands for the cpn 10 and cpn 60 were also detected in pancreatic juice . ^^^ Immunofluorescence studies on rat pancreatic tissue revealed a strong positive signal in the apical region of the acinar cells for cpn 10 and cpn 60 , while an immunoreaction was detected at the juxtanuclear Golgi region with the anti hsp 70 antibody . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
This was performed in the presence of the following chaperonin complexes in the refolding medium : chaperonin 60 ( cpn 60 ) , cpn 60 MgATP , cpn 60 Mgp [ NH ] ppA , cpn 60 MgADP in both the presence and absence of chaperonin 10 ( cpn 10 ) . ^^^ Dissociation constants for the different complexes were found to be in the order : cpn 60 < cpn 60 MgADP cpn 10 ( formed at low [ MgADP ] ) < cpn 60 MgADP < cpn 60 MgADP cpn 10 < cpn 60 Mgp [ NH ] ppA < cpn 60 Mgp [ NH ] ppA cpn 10 < cpn 60 MgATP < cpn 60 MgATP cpn 10 ; i . e . the tightest complex is with cpn 60 and the weakest with cpn 60 MgATP cpn 10 . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Cpn 60 was labeled with pyrene maleimide in order to follow structural rearrangements in the protein triggered by the binding of nucleotides and cpn 10 . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Escherichia coli chaperonins cpn 60 ( groEL ) and cpn 10 ( groES ) do not catalyse the refolding of mitochondrial malate dehydrogenase . ^^^ In vitro refolding of pig mitochondrial malate dehydrogenase is investigated in the presence and absence of Escherichia coli chaperonins cpn 60 ( groEL ) and cpn 10 ( groES ) . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Unlike Escherichia coli chaperonins , a chaperonin ( cpn ) from a thermophilic bacterium , Thermus thermophilus , consisting of homologues to GroEL ( cpn 60 ) and GroES ( cpn 10 ) is co purified as a large complex . ^^^ We conclude that a single cpn 60 heptamer ring with two stripes stacks into two layers and a cpn 10 oligomer binds to one side of the layers . ^^^ The purified Thermus chaperonin contains endogenously bound ADP , and incubation with ATP causes a partial dissociation of chaperonin into cpn 60 monomers and a cpn 10 heptamer . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Experiments reported recently show that for one molecular chaperone ( Cpn 60 , typified by the E . coli protein GroEL ) , the folding reaction is driven by cycles of binding and release of the co chaperone Cpn 10 ( known as GroES in E . coli ) . ^^^ These cycles come about because of the opposite effects of Cpn 10 and unfolded protein on the Cpn 60 complex : the former stabilises the ADP bound state of Cpn 60 , whereas the latter stimulates ADP ATP exchange . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Refolding and recognition of mitochondrial malate dehydrogenase by Escherichia coli chaperonins cpn 60 ( groEL ) and cpn 10 ( groES ) . ^^^ In vitro refolding of pig mitochondrial malate dehydrogenase is investigated in the presence of Escherichia coli chaperonins cpn 60 ( groEL ) and cpn 10 ( groES ) . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Identification of a GroES ( CPN 10 ) related sequence motif in the GroEL ( CPN 60 ) chaperonins . ^^^ Significant sequence similarity has been noted between a segment of the 60 kDa heat shock family of proteins ( designated as GroEL , cpn 60 or hsp 60 ) and its functional partner , the 10 12 kDa GroES ( or cpn 10 ) family of proteins . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The crystallographically averaged images correlate well with those obtained by other authors from single particle analysis of GroEL and our own previous crystallographic analysis . 2 D crystallization of the smaller chaperone GroES ( cpn 10 ) 7 mer has also been achieved using the NS CF technique . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The results are interpreted in terms of an essential role of the exchanged amino acid residues for the interaction between co chaperonin and cpn 60 partner and in terms of a functional coupling of both cpn 10 domains . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The members of the 10 kDa and 60 kDa heat shock chaperonin proteins ( Hsp 10 and Hsp 60 or Cpn 10 and Cpn 60 ) , which form an operon in bacteria , are present in all eubacteria and eukaryotic cell organelles such as mitochondria and chloroplasts . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Using antisera against chaperonin 60 ( cpn 60 ) , chaperonin 10 ( cpn 10 ) and the heat shock cognate protein of 70 kDa ( hsc 70 ) we are able to demonstrate , that the thylakoid lumen contains a separate set of molecular chaperones , which is distinct from the stromal one . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Chaperonin 60 ( Cpn 60 , symbionin ) and chaperonin 10 ( Cpn 10 ) , which are high and low molecular weight heatshock proteins , were sought in tissues of more than 60 aphid species . ^^^ It was demonstrated that ( 1 ) there are two types of aphids in terms of the endosymbiotic system : some with only primary symbionts and others with , in addition , secondary symbionts ; ( 2 ) the primary symbionts of various aphids are quite similar in morphology whereas the secondary symbionts vary ; and ( 3 ) irrespective of the aphid species , Cpn 60 is abundant in both the primary and secondary symbionts , while Cpn 10 is abundant in the secondary symbionts but present in small amounts in the primary ones . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
With the structure of a cpn 10 heptamer now revealed and the structure of the E . coli GroEL previously known , models of cpn 10 : cpn 60 and GroEL : GroES complexes are proposed . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The cloned genes of chaperonin subunits , chaperonin 10 ( T . th cpn 10 ) and chaperonin 60 ( T . th cpn 60 ) , were separately expressed in Escherichia coli cells . ^^^ Since chaperonin from T . thermophilus HB 8 is purified as a holochaperonin , a complex of tetradecameric T . th cpn 60 and heptameric T . th cpn 10 , a tetradecamer of T . th cpn 60 without T . th cpn 10 has not been obtained before . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Homologues of the chaperonins Cpn 60 and Cpn 10 have been purified from the Gram positive cellulolytic thermophile Clostridium thermocellum . ^^^ The Cpn 60 protein was purified by ATP affinity chromatography and the Cpn 10 protein was purified by gel filtration , ion exchange and hydrophobic interaction chromatographies . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Chaperonin cpn 60 and heat shock protein hsp 70 couple their ATPase cycles to the binding and dissociation of non native proteins . cpn 60 is a cylindrical tetradecamer that uses a co protein ( cpn 10 ) and both positive and negative cooperativity to alter the properties of its two voluminous protein binding chambers in an alternating , asymmetric cycle . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Two open reading frames ( 285 and 1 , 635 bp ) were found ; they encode Cpn 10 and Cpn 60 , with corresponding deduced molecular masses of 10 . 6 and 57 . 6 kDa . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Using the loss of mitochondrial DNA as a means of producing a specific mitochondrial stress , we show by Western blot analysis that mtDNA less ( rho 0 ) rat hepatoma cells show an increase in the steady state levels of chaperonin 60 ( cpn 60 ) and chaperonin 10 ( cpn 10 ) . ^^^ Heat stress was able to provide an additional induction of cpn 60 and cpn 10 above that obtained for the rho 0 state alone , indicating that these genes have separate regulatory elements for the specific mitochondrial and general stress responses . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
In the present study we report the occurrence of chaperonins , cpn 10 and cpn 60 , in Chromatium vinosum and rat hepatocytes , using specific polyclonal antibodies in conjunction with the protein A gold immunocytochemical technique . ^^^ As demonstrated by quantitative evaluations , the immunolabeling for cpn 10 and cpn 60 in C vinosum cells was associated primarily with the bacterial cell envelope . ^^^ On the other hand , using the post embedding immunoelectron microscopy technique cpn 10 and cpn 60 were localized specifically in liver mitochondria and peroxisomes . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Cochaperonins ( cpn 10 ) assist chaperonins ( cpn 60 ) in promoting folding and assembly of other proteins . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The deduced amino acid sequences of GroEL 1 ( cpn 60 ) and GroES 1 ( cpn 10 ) were in agreement with N terminal sequences previously obtained for the isolated proteins ( K . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Cpn 10 is a co factor of Cpn 60 , which regulates Cpn 60 mediated protein folding . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Identification of amino acid residues at nucleotide binding sites of chaperonin GroEL / GroES and cpn 10 by photoaffinity labeling with 2 azido adenosine 5 ' triphosphate . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The groE operon of Francisella tularensis LVS , encoding the heat shock proteins chaperone 10 ( Cpn 10 ) and Cpn 60 , was sequenced and characterized , and the T cell response of LVS vaccinated individuals to the two proteins and the third major chaperone , Ft DnaK , was assayed . ^^^ The cpn 10 and cpn 60 genes were amplified by PCR with degenerate oligonucleotides derived from the N terminal sequence of the two proteins . ^^^ The deduced amino acid sequences closely resembled Cpn 10 and Cpn 60 proteins of other prokaryotes . ^^^ The genes constituted a bicistronic operon , the cpn 10 gene preceding the cpn 60 gene . ^^^ After separation of lysates of the F . tularensis LVS organism by two dimensional gel electrophoresis , DnaK , Cpn 60 , and Cpn 10 were extracted and used as antigens in T cell tests . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Chaperonin 10 protein from Rattus norvegicus ( Rat cpn 10 ) has been reported to bind chaperonin 60 from Escherichia coli ( GroEL ) in an ATP dependent manner . ^^^ The biotinylated Rat cpn 10 avidin affinity matrix was then used to isolate GroEL from a crude cell lysate . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The heptameric cpn 10 ( Method B ) bound correctly to GroEL from E . coli , demonstrating that N terminal acetylation is not necessary for its folding and binding to bacterial cpn60 . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Monomeric yeast cpn 10 does not bind to GroEL in the presence of nucleotides , whereas under identical conditions E . coli cpn 10 ( GroES ) , having a strong sequence homology to the yeast form but a pI of 5 . 2 , shows no pH dependent dissociation and is able to complex with GroEL at both pH 7 . 5 and 4 . 5 . ^^^ However , refolding of yeast cpn 10 to a complex that can be recognised by GroEL depends on the presence of a lipid water interface with a specificity for negatively charged lipids . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The TRt groES and groEL encode subunits of chaperonin 10 ( Cpn 10 ) and chaperonin 60 ( Cpn 60 ) of 94 and 541 amino acids , respectively , and are arranged in that order forming the open reading frames ( ORFs ) of a bicistronic operon . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
By using biochemistry and immunocytochemistry , we have shown that Grp 94 , Cpn 10 , Cpn 60 , and protein disulfide isomerase ( PDI ) are present all along the rough endoplasmic reticulum Golgi granule secretory pathway of the pancreatic acinar cells and are secreted into the acinar lumen . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
It is believed that CPN 60 and CPN 10 are involved in the assembly of Rubisco , a key enzyme involved in the photosynthetic pathway . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
PROBLEM : The aim of this study was to investigate the expression of chaperonin ( cpn ) 10 and cpn 60 mRNA in oocytes or embryos , and to further explore the possibility that early pregnancy factor ( EPF ) is identical with cpn 10 . ^^^ METHOD OF STUDY : The expressions of cpn 10 and cpn 60 mRNA in oocytes and embryos at the different stages ( 1 cell , 2 cell , 8 cell , and morula ) were examined by polymerase chain reaction techniques . ^^^ RESULTS : Similar levels of mRNA of cpn 10 and cpn 60 were detected in oocytes and embryos at every stage . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Chaperonin 60 ( cpn 60 ) and chaperonin 10 ( cpn 10 ) are essential proteins involved in ATP dependent folding of several intracellular proteins in the bacterial cell . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Hsp 10 ( 10 kDa heat shock protein , also known as chaperonin 10 or Cpn 10 ) is a co chaperone for Hsp 60 in the protein folding process . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Hydrolysable ATP is a requirement for the correct interaction of molecular chaperonins cpn 60 and cpn 10 . ^^^ Over recent years the binding ability of the molecular chaperone cpn 60 ( GroEL 14 ) and its co chaperone cpn 10 ( GroES 7 ) has been reported to occur under an assortment of specific conditions from the use of non hydrolysable ATP analogues ( namely adenosine 5 ' [ gamma thio ] triphosphate ) to requiring hydrolysable ATP for any interaction to occur . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Intramitochondrial components ( mtHSP 70 ) pull the precursor into the matrix , cleave off the targeting sequence ( mitochondrial processing peptidase ) , and refold the protein ( HSP 60 , cpn 10 ) into its mature conformation . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Chaperonins Cpn 10 and Cpn 60 are present in pancreatic juice , but Hsp 70 is not . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
BACKGROUND : The co chaperonin protein 10 ( cpn 10 ) assists cpn 60 in the folding of nonnative polypeptides in a wide range of organisms . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The cpn 60 and cpn 10 genes from psychrophilic bacterium , Oleispira antarctica RB 8 , showed a positive effect in Escherichia coli growth at low temperature , shifting its theoretical minimal growth temperature from +7 . 5 degrees C to 13 . 7 degrees C [ Ferrer , M . , Chernikova , T . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The identity of the molecule ( s ) on the cell surface that is targeted by EPF is unknown , but as EPF is an extracellular homologue of the intracellular protein chaperonin 10 ( Cpn 10 ) , we examined the possibility that the EPF receptor is a membrane associated form of chaperonin 60 ( Cpn 60 ) , the functional associate of Cpn 10 within the cell . ^^^ The EPF target molecule on lymphocytes was visualized by chemical cross linking of exogenous iodinated Cpn 10 to cells and probed with anti Cpn 60 . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
This principle was based on simultaneous expression of the target protein with chaperones ( Cpn 60 and Cpn 10 ) from a psychrophilic bacterium , Oleispira antarctica RB 8 ( T ) , that allow E . coli to grow at high rates at 4 degrees C ( maximum growth rate , 0 . 28 h ( 1 ) ) . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Cpn 10 binds to only one end of the cpn 60 structure and is visible as an additional layer of density forming a cap on one end of the cpn 60 cylinder . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
In this study , a gene encoding molecular chaperonin Cpn 10 the functional partner of Cpn 60 was cloned , and its structure and expression were characterized , as well as the cellular localization of its encoded protein . ^^^ The amoebic Cpn 10 , like Cpn 60 , is not significantly upregulated upon heat shock treatment . ^^^ Computer assisted protein modelling , and specific antibodies against Cpn 10 and Cpn 60 , suggest that both proteins interact with each other , and that they function in the same intracellular compartment . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
T . halophila chaperonin composed of a core moiety of chaperonin 60 ( cpn 60 ) and a lid moiety of chaperonin 10 ( cpn 10 ) , is thought to contribute to host halotolerant capability . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Chaperonins in all bacteria are encoded by the essential groEL and groES genes , also called cpn 60 and cpn 10 arranged on the bicistronic groESL operon . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The growth of Escherichia coli cells is impaired at temperatures below 21 degrees C and stops at 7 . 5 degrees C ; however , growth of a transgenic strain producing the cold adapted chaperones Cpn 60 and Cpn 10 from the psychrophilic bacterium Oleispira antarctica is good at low temperatures . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The complete sequence of the resulting reading frames showed high homology to those of the genes encoding GroEL ( hsp 60 ) and GroES ( hsp 10 ) of E . coli , and hsp60s and hsp10s of several other species . ^^^ Heat shock proteins 60 ( hsp 60 ) and 10 ( hsp 10 ) are essential for the formation and restoration of many supramolecular structures . ^^^ For reconstitution of these structures , we isolated stable hsps of 61kDa and 12kDa , which are similar to hsp 60 and hsp 10 , respectively , from the supernatant fraction of thermophilic bacterium PS 3 by ATP Agarose chromatography . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
In amino acid sequence comparison studies the sequences of these proteins , which were designated GroES and GroEL , exhibited up to 78 % homology with known prokaryotic sequences of 10 and 60 kDa heat shock proteins ( hsp 10 and hsp 60 ) . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Comparisons of deduced amino acid sequences disclosed a high degree of homology between the R . tsutsugamushi proteins Stp 11 and Sta 58 and the E . coli proteins GroES and GroEL , respectively , and the family of primordial heat shock proteins designated Hsp 10 Hsp60 . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
All 11 antigenic molecules tested ( including M . leprae hsp 10 , hsp 18 , hsp 65 and several novel M . leprae antigens ) were shown to be recognized by T cells , but clear quantitative differences existed between reactivities induced by individual antigens . ^^^ Similar quantitative differences were observed when antibody responses to hsp 10 and hsp 65 antigens were determined . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
This proliferation was markedly augmented by hsp 65 ( 3 fold ) and hsp 70 ( 5 fold ) , whereas hsp 10 and the protein control ovalbumin had no effect . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Our results identify Hsp 10 as an essential component of the mitochondrial protein folding apparatus , participating in various aspects of Hsp 60 function . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The resulting sequence revealed two reading frames and showed high homology to those of hsp 60 ( groEL ) and hsp 10 ( groES ) of bacteria ( E . coli ) and several other species . ^^^ Molecular characterization of the gene operon of heat shock proteins HSP 60 and HSP 10 in methicillin resistant Staphylococcus aureus . ^^^ Two of these proteins were HSP 60 and HSP 10 . ^^^ The genes of HSP 60 and HSP 10 in S . aureus comprised an operon as in E . coli . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Hsp 10 and GroES are members of the chaperonin 10 family of molecular chaperones , and GroEs is necessary for the optimal activity of GroEL , a member of the chaperonin 60 family and the E . coli homologue of mycobacterial hsp 65 . ^^^ Since hsp 65 has been implicated in both experimental and human rheumatoid arthritis , we aimed to assess the immunomodulatory effects of its co chaperonin , hsp 10 , in experimental arthritis . ^^^ Assessment of circulating antibody levels to mycobacterial hsp 10 and hsp 65 indicated that all arthritic rats had increased titres to both hsp 10 and hsp 65 : hsp 10 treated rats showed further elevation of this humoral response not only to hsp 10 but also to hsp 65 when compared with the untreated arthritic control . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
As in any other bacterium , Helicobacter pylori synthesizes two heat shock proteins , the HspA ( GroES or Hsp 10 homologue ) and the HspB ( GroEL or Hsp 60 homologue ) . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
We show here that hydrogenosomes contain heat shock proteins , Hsp 70 , Hsp 60 , and Hsp 10 , with signature sequences that are conserved only in mitochondrial and alpha Gram negative purple bacterial Hsps . ^^^ Moreover , phylogenetic analyses of hydrogenosomal Hsp 70 , Hsp 60 , and Hsp 10 show that these proteins branch within a monophyletic group composed exclusively of mitochondrial homologues . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Furthermore , members of the GrpE family exhibit a much lower degree of sequence identity than do the well studied members of the Hsp 70 , Hsp 60 and Hsp 10 families . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The affinity of hsp 10 ( P36H ) to hsp 60 as well as to Escherichia coli GroEL is reduced . ^^^ However , this decrease in affinity does not correlate with the functional defect , because hsp 10 ( P36H ) fully assists the GroEL mediated refolding of malate dehydrogenase at 30 degrees C . ^^^ Refolding activity , rather , correlates with the ability of hsp 10 ( P36H ) to inhibit the ATPase of GroEL but not that of hsp 60 . ^^^ We have functionally characterized the yeast mitochondrial chaperonins hsp 60 and hsp 10 . ^^^ In the presence of ADP , one molecule of hsp 10 binds to hsp 60 with an apparent Kd of 0 . 9 nM and a second molecule of hsp 10 binds with a Kd of 24 nM . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
A highly flexible , yet conserved polypeptide loop of Hsp 10 mediates binding to Hsp 60 in the course of chaperonin dependent protein folding . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Two other heat shock proteins ( HSP 60 and HSP 10 ) are known to form , within the mitochondria , a chaperonin complex that is important for mitochondrial protein folding and function . ^^^ METHODS AND RESULTS : We generated recombinant adenoviral vectors containing HSP 60 , HSP 10 , or a combination of the two genes . ^^^ Cells infected with an adenoviral construct overexpressing both HSP 60 and HSP 10 were found to be protected against simulated ischemia , whereas cells infected with adenoviral constructs overexpressing only HSP 60 or HSP 10 alone were not rendered tolerant to simulated ischemic injury . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Identification of in vivo substrates of the yeast mitochondrial chaperonins reveals overlapping but non identical requirement for hsp 60 and hsp 10 . ^^^ In order to understand the relative importance of hsp 60 and hsp 10 in the living cell , homologous substrate proteins need to be identified and analyzed . ^^^ We have devised a novel screen to test the folding of a large variety of homologous substrates in the mitochondrial matrix in the absence or presence of functional hsp 60 or hsp 10 . ^^^ The identified substrates have an Mr of 15 90 kDa and fall into three groups : ( 1 ) proteins that require both hsp 60 and hsp 10 for correct folding ; ( 2 ) proteins that completely fail to fold after inactivation of hsp 60 but are unaffected by the inactivation of hsp 10 ; and ( 3 ) newly imported hsp 60 itself , which is more severely affected by inactivation of hsp 10 than by inactivation of pre existing hsp 60 . ^^^ For these , the lack of hsp 60 function has a more pronounced effect than inactivation of hsp 10 . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Since HSP 10 ( GroES ) and HSP 60 ( GroEL ) exhibited no activity for neurite outgrowth in the same culture , this activity was specific to HSP 90 among the heat shock proteins . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The hsp 70 operon is comprised of five genes , hrc 37 , hsp 20 , hsp 70 , hsp 40 and orf 35 , and the hsp 60 is comprised of two genes , hsp 10 and hsp 60 . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Presence of a pre apoptotic complex of pro caspase 3 , Hsp 60 and Hsp 10 in the mitochondrial fraction of jurkat cells . ^^^ In the present study , we demonstrate that pro caspase 3 is present in the mitochondrial fraction of Jurkat T cells in a complex with the chaperone proteins Hsp 60 and Hsp 10 . ^^^ In in vitro systems , recombinant Hsp 60 and Hsp 10 accelerated the activation of pro caspase 3 by cytochrome c and dATP in an ATP dependent manner , consistent with their function as chaperones . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Inducible hsp 70 , hsp 60 and hsp 10 when coexpressed , and hsp 27 and alphaB crystallin have an overall protective effect against ischemic injury as determined by the release of enzymes like creatine kinase and LDH . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
A prime candidate , however , is the chlamydial GroES homolog Hsp 10 , which is genetically and physiologically linked to Hsp 60 . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
HSP 60 and HSP 10 as diagnostic and prognostic tools in the management of exocervical carcinoma . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Using chimeric chaperonin molecules assembled by fusing equatorial and apical domains derived from GroEL and its mammalian mitochondrial homolog , Hsp 60 , we show that productive folding by Hsp 60 and its cognate cochaperonin , Hsp 10 , proceeds in vitro and in vivo without the formation of a two ring structure . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The alignment of DNA inferred amino acid sequences of the Hsp 10 and Hsp 60 heat shock proteins with bacterial and mitochondrial homologues revealed the presence within Hsp 60 of signatures shared by mitochondria and rickettsiae . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Hsp 60 is found in eubacteria , mitochondria , and chloroplasts , where , in cooperation with Hsp 10 , it participates in protein folding and translocation of proteins to the organelles . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The human serologic response to chlamydial Hsp 10 , Hsp 60 , and major outer membrane protein ( MOMP ) was measured by enzyme linked immunosorbent assay . ^^^ Thus , among women with similar exposure to chlamydiae , the serologic response to Hsp 10 exhibited a stronger correlation with TFI than did the response to Hsp 60 or MOMP . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Molecular analysis of the hydrogenosomal heat shock proteins Hsp 70 , Hsp 60 and Hsp 10 in Trichomonas vaginalis , one of the deepest branching eukaryotes known to date , has revealed that these group exclusively with mitochondrial heat shock proteins . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
While bacterial GroEL is functionally promiscuous with various co chaperonin partners , its human homologue , Hsp 60 functions specifically with its co chaperonin partner , Hsp 10 , and not with other co chaperonins , such as the bacterial GroES or bacteriophage T 4 encoded Gp 31 . ^^^ Here , we show that the ability of Hsp 10 , but not GroES , to interact specifically with Hsp 60 lies within the mobile loop sequence . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
In situ hybridization analysis revealed that the induction pattern of HSP 60 mRNA was identical to that of HSP 10 mRNA throughout the entire ischemic course . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Combined and individual mitochondrial HSP 60 and HSP 10 expression in cardiac myocytes protects mitochondrial function and prevents apoptotic cell deaths induced by simulated ischemia reoxygenation . ^^^ BACKGROUND : The mitochondrial heat shock proteins HSP 60 and HSP 10 form a mitochondrial chaperonin complex , and previous studies have shown that their increased expression exerts a protective effect against ischemic injury when cardiac myocytes are submitted to simulated ischemia . ^^^ We wanted to determine whether HSP 60 and HSP 10 could exert a protection against simulated ischemia and reoxygenation ( SI / RO ) induced apoptotic cell death and whether such protection results from decreased mitochondrial cytochrome c release and caspase 3 activation and from the preservation of ATP levels by preservation of the electron transport chain complexes . ^^^ In addition , we explored whether increased expression of HSP 60 or HSP 10 by itself exerts a protective effect . ^^^ METHODS AND RESULTS : We overexpressed HSP 60 and HSP 10 together or separately in rat neonatal cardiac myocytes using an adenoviral vector and then subjected the myocytes to SI / RO . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Hsp 60 , Hsp 10 , Cytochrome c , TRAP 1 and P 32 ( gC1q R ) ) in recent studies , within both mitochondria and at various specific extramitochondrial sites raises fundamental questions about the role of mitochondria in cell structure and function , and about the mechanisms that exist in normal cells for protein translocation from mitochondria to other compartments . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
However , the other analyzed hsps ( hsp 70 , hsp 27 , hsp 60 , hsp 10 , and CyP A ) did not display any significant induction after incubation with SNAP . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The HSP 60 and HSP 10 protein levels were determined by SDS PAGE , Western blot , and quantified by optical densitometry according to the immunoreactive bands of actin . ^^^ HSP 60 expression was more than 2 . 3 fold and HSP 10 expression was more than 2 . 4 fold increased in atrial myocardium of patients with chronic atrial fibrillation . ^^^ CONCLUSIONS : These results indicate functional upregulation of mitochondrial HSP 60 and HSP 10 in response to chronic atrial fibrillation . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Serum immunoglobulin G reactivity to Hsp 10 and Hsp 60 antigens ( chlamydial , Escherichia coli , and human ) , and C pneumoniae whole organisms were measured by ELISA . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The topographical and chronological patterns of HSP 60 and HSP 10 messenger ribonucleic acid ( mRNA ) expression and induction were investigated in the rat focal cerebral ischemia model . ^^^ RT PCR analysis showed that both HSP 60 and HSP 10 mRNA levels increased significantly in the ischemic cortex from 4 to 24 h of reperfusion after 30 min of occlusion . ^^^ Expression patterns and the timing of the induction of both HSP 60 and HSP 10 mRNAs were identical throughout the experiments . ^^^ Simultaneous induction of the mRNAs for the mitochondrial chaperonins , HSP 60 and HSP 10 , in various regions in focal cerebral ischemia demonstrates that mitochondrial stress conditions persist concomitantly with cytosolic stress conditions in focal cerebral ischemia . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
HSP 10 , HSP 60 , and HSP 73 did not differ between groups . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
To improve the reliability of the serodiagnosis of Chlamydia trachomatis infections , an immunoblot analysis , a microimmunofluorescence titration , and different immunoassays using synthetic peptides derived from species specific epitopes in variable domain 4 of the major outer membrane protein or recombinant antigens ( heat shock protein 70 [ hsp 70 ] , hsp 60 , hsp 10 , polypeptide encoded by open reading frame 3 of the plasmid [ pgp 3 ] , macrophage infectivity potentiator , and a fragment of the total lipopolysaccharide ) were evaluated . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Chaperone proteins Hsp 10 and Hsp 60 were readily decreased by half in mitochondria at both doses , most likely by leaking into cytoplasm . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
A complementation assay showed that wild type HSP 60 ( also known as `` HSPD 1 ' ' ) , but not HSP 60 ( V72I ) , together with the co chaperonin HSP 10 ( also known as `` HSPE 1 ' ' ) , can support growth of Escherichia coli cells in which the homologous chromosomal groESgroEL chaperonin genes have been deleted . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
This system recognizes polypeptide chains in an extended conformation . ( 3 ) The Hsp 60 system , consisting of GroEL ( Hsp 60 ) and its cofactor GroES ( Hsp 10 ) , which assists in the folding of compact folding intermediates that expose hydrophobic surfaces . ( 4 ) The Clp ATPases which are typically members of the Hsp 100 family of heat shock proteins . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The interaction of CaNB and Hsp 60 was not disrupted by the incubation with Hsp 10 , ATP and Mg++ , suggesting that CaNB was not associated with Hsp 60 as a misfolded substrate , and may serve as a regulatory protein . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Genomic structure of the human mitochondrial chaperonin genes : HSP 60 and HSP 10 are localised head to head on chromosome 2 separated by a bidirectional promoter . ^^^ Although the mitochondrial chaperonin Hsp 60 and its co chaperonin Hsp 10 have received great attention in the last decade , and it has been proposed that mutations and variations in these genes may be implicated in genetic diseases , the genome structure of the human HSP 60 and HSP 10 genes ( also known as HSPD 1 and HSPE 1 , respectively ) has not been firmly established . ^^^ The picture has been confused by the presence of many pseudogenes of both HSP 60 and HSP 10 and the long surviving assumption that the HSP 60 gene is intron less . ^^^ We present the full sequence of the human HSP 60 and HSP 10 genes . ^^^ The first exon of the human HSP 60 gene is non coding and the first exon of the human HSP 10 gene ends with the start codon . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Western blot analysis showed that mitochondrial Hsp 25 increased , whereas Hsp 10 , Hsp 60 , Hsp 70 , Hsp 75 , cyclophilin D , and voltage dependent anion channel did not change after heat shock . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Immunohistochemical evaluation of PCNA , p 53 , HSP 60 , HSP 10 and MUC 2 presence and expression in prostate carcinogenesis . ^^^ MATERIALS AND METHODS : In the present work we evaluated , by immunohistochemistry , the presence and the expression of PCNA , p 53 , HSP 60 , HSP 10 and MUC 2 in a series of nodular hyperplasia , low and high grade prostatic intraepithelial lesions and adenocarcinomas . ^^^ CONCLUSION : We suggest the further examination , by molecular and genetic studies , of the role of HSP 60 and HSP 10 during carcinogenesis of the prostate as well as of other organs . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
This report correlates the overexpression of HSP 10 with that of HSP 60 during carcinogenesis in vivo . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Hsp 10 and Hsp 60 modulate Bcl 2 family and mitochondria apoptosis signaling induced by doxorubicin in cardiac muscle cells . ^^^ This study was carried out to define the roles of two heat shock proteins , Hsp 10 and Hsp 60 , on doxorubicin induced apoptosis in primary cardiomyocytes . ^^^ Transducing cardiomyocytes with Hsp 10 or Hsp 60 with adenoviral vector suppressed the occurrence of apoptosis in the doxorubicin treated cardiomyocytes . ^^^ Overexpression of Hsp 10 and Hsp 60 increased the abundance of the anti apoptotic Bcl xl and Bcl 2 , and reduced the protein content of the pro apoptotic Bax . ^^^ Hsp 60 overexpression also significantly reduced doxorubicin induction of Bad , whereas overexpression of Hsp 10 did not alter the expression of Bad in the doxorubicin treated cells . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Hsp 10 and Hsp 60 suppress ubiquitination of insulin like growth factor 1 receptor and augment insulin like growth factor 1 receptor signaling in cardiac muscle : implications on decreased myocardial protection in diabetic cardiomyopathy . ^^^ We have investigated the effects of two heat shock proteins , Hsp 10 and Hsp 60 , on insulin like growth factor 1 receptor ( IGF 1R ) signaling in cardiac muscle cells . ^^^ Neonatal cardiomyocytes were transduced with Hsp 10 or Hsp 60 via adenoviral vector . ^^^ Compared with the cells transduced with a control vector , overexpression of Hsp 10 or Hsp 60 increased the abundance of IGF 1R and IGF 1 stimulated receptor autophosphorylation . ^^^ Thus , Hsp 10 and Hsp 60 overexpression increased the number of functioning receptors and amplified activation of IGF 1R signaling . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
They included four upregulated HSPs : HSP90alpha , HSP 60 , HSP 27 , and HSP 10 . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Heat shock proteins ( hsp ) , hsp 60 and hsp 10 , are involved in the folding of imported mitochondrial proteins and the refolding of denatured proteins after stress . ^^^ We generated an adenoviral vector coding for a temperature sensitive mutant hsp 10 protein ( P34H ) , incapable of cooperatively refolding denatured malate dehydrogenase with hsp 60 . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
BACKGROUND : In myocardium of patients with chronic atrial fibrillation ( AF ) the expression of the mitochondrial heat shock proteins HSP 60 and HSP 10 is increased . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Heat shock protein 10 ( Hsp 10 ) and heat shock protein 60 ( Hsp 60 ) were originally described as essential mitochondrial proteins involved in protein folding . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
It also affects HSP 60 and HSP 10 mRNAs that encode essential mitochondrial chaperones . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The expression of HSP 60 and HSP 10 in large bowel carcinomas with lymph node metastase . ^^^ The objective of the present study was to evaluate the presence and expression of HSP 60 and HSP 10 in a series of large bowel carcinomas and locoregional lymph nodes with and without metastases . ^^^ An immunohistochemical research for HSP 60 and HSP 10 was performed and the semiquantitative results were analysed by statistical analysis to determine the correlation between HSPs expression and 1 ) tumour grading ; 2 ) degree of inflammation ; 3 ) number of lymph nodes involved ; 4 ) lymph node compartment hyperplasia . ^^^ RESULTS : Our data show that the expression of HSP 60 , in both primary tumour and lymph node metastasis , is correlated with the tumoral grade , while the HSP 10 expression is not . ^^^ Nevertheless , the levels of HSP 10 are commonly higher than the levels of HSP 60 . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The cloning and sequencing of the Brucella abortus groES and groEL genes are reported . ^^^ The groES gene exhibits 60 % , and the groEl gene 69 % , sequence identity with the corresponding Escherichia coli genes . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Antibodies to Chlamydia trachomatis heat shock proteins Hsp 60 and Hsp 10 and subfertility in general population at age 31 . ^^^ PROBLEM : To assess the association between antibodies to Chlamydia trachomatis heat shock proteins 60 and 10 ( Hsp 60 and Hsp 10 ) and subfertility in a general population sample . ^^^ Serum immunoglobulin ( Ig ) G and IgA antibodies against C . trachomatis Hsp 60 and Hsp 10 , explanatory factors , were measured by enzyme immunoassay , using recombinant proteins as antigens . ^^^ RESULTS : The prevalence and medians of serum IgA antibodies to Hsp 60 and Hsp 10 were significantly higher in the female partners of subfertile couple than in their fertile controls . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
We investigated the presence and the expression of HSP 60 and HSP 10 in a series of 20 normal human bone marrow specimens ( NHBM ) by the means of immunohistochemistry . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Association of uterine and salpingeal fibrosis with chlamydial hsp 60 and hsp 10 antigen specific antibodies in Chlamydia infected koalas . ^^^ Studies of humans have associated titers of serum immunoglobulin G ( IgG ) against chlamydial hsp 60 and hsp 10 antigens with chronic infection , salpingeal fibrosis , and tubal infertility . ^^^ To determine whether a similar relationship exists in Chlamydia infected koalas , samples were collected opportunistically from 34 wild female koalas and examined by gross pathology and histopathology , PCR , and immunohistochemistry for Chlamydia spp . and enzyme linked immunosorbent assay for serological responses to chlamydial hsp 10 and hsp 60 antigens . ^^^ Greater anti hsp titers occurred in Chlamydia infected koalas with fibrous occlusion of the uterus or uterine tube than in other Chlamydia infected koalas ( for hsp 10 IgG , P = 0 . 005 ; for hsp 60 IgG , P = 0 . 001 ; for hsp 10 IgA , P = 0 . 04 ; for hsp 60 IgA , P = 0 . 09 ) . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
In the presence of its partner , GroES , the tetradecameric molecular chaperone GroEL binds 14 ATP molecules , half of which are hydrolyzed in a cooperative manner . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Two complete open reading frames ( 288 and 1632 bp ) were found and identified as the groES and groEL homologous genes of C . acetobutylicum , respectively . ^^^ The length of the groESL specific mRNA ( 2 . 2 kb ) , a transcription terminator downstream of groEL , and a transcription start site upstream of groES , identified by primer extension analysis , indicated that groES and groEL of C . acetobutylicum are organized in a bicistronic operon . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Thus during heat shock some groEL is reversibly phosphorylated , which allows its ATP dependent release from protein substrates in the absence of its usual cofactor ( groES ) , and probably promotes the repair of damaged polypeptides . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The clone contained two open reading frames homologous to the GroES and GroEL ( or HSP 60 ) family of bacterial and eukaryotic proteins as well as other upstream and downstream sequences . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Complementation experiments with E . coli groE mutants showed that the chaperonin 10 and chaperonin 60 genes from the endosymbiont are expressed in E . coli and that they can function as molecular chaperones together with endogenous GroEL and GroES , respectively . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
A 2 . 1 kb groESL mRNA from B . subtilis was detected independently by Northern ( RNA ) blot analyses with a groES and a groEL specific probe . ^^^ This demonstrated that groES and groEL are in an operon . ^^^ With this strain , it was possible to show that both groES and groEL are essential genes under both normal and heat shock conditions . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Sequencing of 2 , 525 bp revealed two open reading frames in the order groES groEL . ^^^ Alignment of the GroES and GroEL proteins with those of eight other eubacteria revealed 50 to 65 % and 72 to 84 % sequence similarity , respectively . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Chaperonins groEL and groES promote assembly of heterotetramers ( alpha 2 beta 2 ) of mammalian mitochondrial branched chain alpha keto acid decarboxylase in Escherichia coli . ^^^ We have investigated the possible role of chaperonins groEL and groES in the folding and assembly of heterotetramers ( alpha 2 beta 2 ) of mammalian mitochondrial branched chain alpha keto acid decarboxylase ( E 1 ) in Escherichia coli . ^^^ Cotransformation of the ES mutant host with a second vector overexpressing groEL and groES resulted in a greater than 500 fold increase in E 1 specific activity . ^^^ The time course studies showed that the increase in E 1 specific activity and subunit levels correlated with the increase in groEL and groES until the concentration of the chaperonins reached a saturating level in the cell . ^^^ The present results demonstrate that chaperonins groEL and groES promote folding and assembly of heterotetrameric proteins of mammalian mitochondrial origin . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Functional refolding to the native state is inhibited transiently by GroEL , but there is no complete folding arrest in the absence of Mg ATP and GroES . ^^^ GroES is not essential for functional GroEL mediated refolding of the F ( ab ) fragment but affects the reactivation yield to a small extent . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The GroEL subunit was required for this improvement in refolding yield , whereas the GroES subunit was not . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
These H . ducreyi ORFs and the encoded proteins show significant homology with the groE genes and GroES and GroEL heat shock proteins from several bacterial pathogens and with conserved eukaryotic 60 kDa heat shock proteins . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
When holoenzyme formation from purified apo 6 HDNO was investigated in vitro , addition of GroEL and GroES to the reaction assays increased the yield of holoenzyme formation . ^^^ The refolding of guanidinium hydrochloride unfolded holoenzyme , however , was catalyzed by GroEL and GroES in an ATP dependent reaction . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Cooperation of GroEL / GroES and DnaK / DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli . ^^^ Overproduction of either GroEL and GroES or DnaK and DnaJ prevents aggregation . ^^^ Our data suggest that the GroEL and GroES proteins and the DnaK and DnaJ proteins have complementary functions in the folding and assembly of most proteins . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Chaperonin mediated protein folding : GroES binds to one end of the GroEL cylinder , which accommodates the protein substrate within its central cavity . ^^^ We have analysed structural and functional properties of the interaction between GroEL and the co chaperonin GroES . ^^^ The stoichiometry of the GroEL 14mer and the GroES 7mer in the functional holo chaperonin is 1 : 1 . ^^^ GroES protects half of the GroEL subunits from proteolytic truncation of the approximately 50 C terminal residues . ^^^ Removal of this region results in an inhibition of the GroEL ATPase , mimicking the effect of GroES on full length GroEL . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Mycobacteria contain two groEL genes : the second Mycobacterium leprae groEL gene is arranged in an operon with groES . ^^^ In contrast to other bacterial species , mycobacteria were thus far considered to contain groEL and groES genes that are present on separate loci on their chromosomes , Here , by screening a Mycobacterium leprae lambda gt 11 expression library with serum from an Ethiopian lepromatous leprosy patient , two DNA clones were isolated that contain a groEL gene arranged in an operon with a groES gene . ^^^ The predicted amino acid sequences of the GroES and GroEL proteins encoded by this operon are 85 90 % and 59 61 % homologous to the sequences from previously characterized mycobacterial GroES and GroEL proteins . ^^^ Southern blotting analyses with M . leprae groES and groEL specific probes demonstrate that similar groESL homologous DNA is present in the genomes of other mycobacteria , including Mycobacterium tuberculosis . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Isolation and characterization of the groES and groEL genes of Bacillus subtilis Marburg . ^^^ The complete set of groES and groEL gene homologues from Bacillus subtilis Marburg 168 was identified , cloned , and characterized . ^^^ The nucleotide sequence indicated the presence of two open reading frames corresponding to the groES and groEL genes . ^^^ The presumptive GroES and GroEL proteins were calculated to be polypeptides of 10 , 175 and 57 , 175 Da , respectively , and showed extensive sequence similarities with the known GroES and GroEL proteins of Escherichia coli and Mycobacterium tuberculosis . ^^^ Two proteins of 10 and 60 kDa overproduced in B . subtilis cells carrying a multi copy groES and groEL plasmid were demonstrated to correspond to two out of the six heat shock inducible proteins . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Addition of GroES and ATP hydrolysis is required to release the polypeptide chain bound to GroEL and to allow further folding to its final , active state . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Two open reading frames of 57 , 677 and 10 , 456 Da were identified , corresponding to the heat shock proteins GroEL and GroES , respectively . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Mg ATP and groES then promote the acquisition of ordered tertiary structure at the surface of groEL . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The four components : two proteins from Escherichia coli , chaperonin 60 ( groEL ) and chaperonin 10 ( groES ) , MgATP , and K+ , are necessary for the in vitro folding of rhodanese . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
We have used transferred nuclear Overhauser effects to demonstrate that the Escherichia coli chaperonin GroEL binds to a peptide corresponding to the N terminal alpha helix in rhodanese , a mitochondrial protein whose in vitro refolding is facilitated by addition of GroEL , GroES , and ATP . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
A newly synthesized protein interacts with GroES on the surface of chaperonin GroEL . ^^^ To facilitate folding and assembly of different proteins , chaperonin GroEL requires the presence of its helper protein GroES . ^^^ Using a photochemical cross linking approach , we show that GroES and newly synthesized pre beta lactamase ( pre beta lac ) contact with each other only within the ternary complex with GroEL . ^^^ Possibly owing to this contact GroES is able to directly influence the pre beta lac / GroEL interaction . ^^^ Furthermore , the cross linking of pre beta lac to GroES suggests that the binding of the protein ligands to GroEL occurs near the GroES binding site , known to be in the central hole space of GroEL . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
GroEL alone inhibited reactivation , but in the presence of ATP , GroEL and GroES significantly increased the yield of active protein . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Two heat shock proteins that show high identity with the Escherichia coli chaperonin 60 ( groEL ) and chaperonin 10 ( groES ) chaperonin proteins were purified and characterized from photolithoautotrophically grown Rhodobacter sphaeroides . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
GroES accelerates the MgATP dependent dissociation of the alpha glucosidase GroEL complex . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Inactivation of DnaJ , GrpE , and GroES did not affect the association or dissociation of DnaK or GroEL from CRAG . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The derived amino acid sequences of the GroES and GroEL proteins demonstrated very high levels of amino acid identity with cognate chaperonins from bacteria and chloroplasts . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Most of the mutagenesis that accompanies the SOS repair of ultraviolet light induced lesions in the single stranded DNA of phage S 13 is eliminated when the groES or the groEL gene of Escherichia coli is defective . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The E . coli groES and groEL genes have been shown to form an operon , to be essential for E . coli viability , and to belong to the so called heat shock class of genes whose expression is regulated by the intracellular levels of sigma factor sigma 32 . ^^^ Both groE chaperonin proteins possess a seven fold axis of symmetry , groES being composed of seven identical subunits of 97 amino acids each , and groEL of fourteen identical subunits of 548 amino acids each . ^^^ The proposed role of the groES chaperonin is to displace the polypeptides bound to groEL , thus effectively promoting the recycling of groEL . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
In Escherichia coli this response is characterized by the induction of several proteins , three of which are the 70 kilodalton product of the dnaK gene , the 60 kilodalton product of the groEL ( mopA ) gene and the 15 kilodalton product of the groES ( mopB ) gene . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
HSP mediated lysis resistance was abolished by a mutation in any one of five heat shock genes ( dnaK , dnaJ , grpE , GroES , or groEL ) . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
In addition , we have obtained evidence which indicates that the GroEL and GroES proteins also play a role in UV mutagenesis . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The Escherichia coli heat shock proteins GroEL and GroES modulate the folding of the beta lactamase precursor . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
A temperature increase from 37 to 42 degrees C induced elevated synthesis of three major proteins corresponding to the DnaK , GroEL , and GroES proteins of M . tuberculosis previously identified as prominent antigens . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Cooperativity in ATP hydrolysis by GroEL is increased by GroES . ^^^ The kinetics of ATP hydrolysis by the ' molecular chaperone ' GroEL and the inhibition of this hydrolysis by GroES have been studied in more detail . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Also found in complexes with phoA 61 were the hsps , protease La and grpE ( but no groEL , or groES ) . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
When the cells were UV irradiated , the groE heat shock gene products , GroES and GroEL , were needed for at least 50 % of the Weigle reactivation of the single stranded DNA phage S 13 . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The product of htpR gene is known to be responsible for positive regulation of transcription of at least three genes encoding proteases lon , groEL , and groES . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Assembly of foreign prokaryotic ribulose bisphosphate carboxylases ( Rubiscos ) in Escherichia coli requires both heat shock proteins groEL and groES . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures . ^^^ The products of the groES and groEL genes of Escherichia coli , constituting the groE operon , are known to be required for growth at high temperature ( 42 degrees C ) and are members of the heat shock regulon . ^^^ To do this , we constructed various groES groEL heterodiploid derivative strains . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
At 30 degrees C , mutants in five heat shock genes ( dnaK , dnaJ , groEL , groES , and grpE ) were more sensitive to lysis than were their wild type parents . ^^^ This protective effect was completely abolished by mutations in dnaK , dnaJ , or groES but not by grpE or groEL mutations . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
In contrast , mutations in groES , groEL , and rpoH heat shock genes suppress cold sensitivity regardless of the transcriptional regulation of the umuDC genes . ^^^ We have also found that mutations in groES and groEL genes are defective in umuDC dependent UV mutagenesis . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Effects of mutations in heat shock genes groES and groEL on protein export in Escherichia coli . ^^^ Escherichia coli heat shock proteins GroES and GroEL are essential cytoplasmic proteins , which have been termed ' chaperonins ' because of their ability to assist protein assembly of bacteriophage capsids and multimeric enzymes of foreign origin . ^^^ In this report we show that temperature sensitive mutations in groES and groEL genes cause defective export of the plasmid encoded beta lactamase ( Bla ) in vivo . ^^^ Since efficient translocation of proteins across biological membranes is thought to be supported by cytoplasmic factors that protect presecretory molecules from being misfolded , these results suggest that both GroES and GroEL proteins possess a chaperone function by which they facilitate export of Bla . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Our data indicate a general role for the groE operon products , the GroEL and GroES proteins , in the folding assembly pathways of many proteins . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Subcloning demonstrated that an intact mutant groEL gene was necessary for suppression and that plasmids carrying the 8 . 3 kilobase insert could suppress mutants carrying groES but not groEL genes for phage lambda growth . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Most of them were found to carry a DNA insertion in the groE upstream region , resulting in high level synthesis of major heat shock proteins GroE ( GroES and GroEL ) . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Growth of bacteriophage Mu was severely inhibited at elevated temperature in mutants defective in the heat shock genes dnaK , groEL , and groES and in the rpoH ( htpR ) regulatory mutant , but not in mutants defective in the heat shock genes dnaJ or grpE ; growth of a mutant of Mu deficient in functions encoded in the accessory region of the Mu genome was inhibited in the latter two host mutants . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Suppression of the Escherichia coli dnaA 46 mutation by amplification of the groES and groEL genes . ^^^ Genetic mapping shows that the groES ( mopB ) and groEL ( mopA ) genes are located on the 8 . 1 kb suppressor fragment . ^^^ Further analysis , including in vitro mutagenesis and subcloning , demonstrates that the amplification of the groES and groEL genes is both necessary and sufficient to suppress the temperature sensitive phenotype of the dnaA 46 mutation . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The morphogenesis of lambda proheads is governed by the products of at least four bacteriophage coded genes ( B , C , E and Nu 3 ) and two host coded genes ( groES ( mopB ) and groEL ( mopA ) ) . ^^^ Earlier genetic experiments indicated that the phenotypes of some of the groES mutations could be suppressed by mutations in the groEL gene , suggesting an interaction between the two groE proteins in vivo ( Tilly , K . , and Georgopoulos , C . ^^^ The following results implicate a physical association between the groES and groEL proteins in vitro . ^^^ The groES protein inhibits the weak ATPase activity of the groEL protein , with a maximal effect seen at a 1 : 1 molar ratio ; the two proteins cosediment during glycerol gradient centrifugation in the presence of ATP and Mg2+ ; and the groES protein binds specifically to a groEL affinity column . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Further analysis showed that the groES ( mopA ) and groEL ( mopB ) genes , both located at 94 . 2 min on the standard map , were indeed carried by the cloned suppressor fragment . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The morphogenesis of bacteriophage lambda proheads is under the control of the four phage genes B , C , Nu 3 , and E , as well as the E . coli genes groEL and groES . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The morphogenesis of bacteriophage lambda proheads is under the control of the four phage genes B , C , Nu 3 and E , and the two Escherichia coli genes groEL and groES . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
We have established the existence of a second groE gene , which we call groES , that is different from the previously described groE gene encoding a 65 , 000 Mr polypeptide ( Georgopoulos and Hohn , 1978 ; Hendrix and Tsui , 1978 ) and which is renamed groEL . ^^^ Bacterial groEL or groES mutants exhibit the same growth kinetics and phenotype at high temperature and lambda proheads have the same protein composition in both classes of mutants . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The Escherichia coli groEL and groES gene products are essential for both phage morphogenesis and bacterial growth . ^^^ We have isolated mutations in the groEL gene that suppress defects in the groES gene . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Database searching indicated that the two genes were homologues of groES and groEL , genes encoding a group of heat shock proteins involved in protein processing , export and assembly . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Moreover , Mn2+ increases the affinity of GroES for GroEL , even in the presence of saturating amounts of Mg2+ . ^^^ Chemical cross linking showed that lower concentrations of Mn ATP as compared with Mg ATP are needed to form both asymmetric GroEL14GroES7 and symmetric GroEL 14 ( GroES 7 ) 2 particles . ^^^ The manganese dependent increase in the rate of protein folding concurred with a specific increase in the amount of symmetric GroEL 14 ( GroES 7 ) 2 particles detected in a chaperonin solution . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
GroES and GroEL appear to be required to stabilize UmuC . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
With CRAG and histone as the ligands , some unphosphorylated GroEL also bound , but this species ( unlike the phosphorylated form ) was not released by ATP alone ; its release required the addition of the cofactor GroES together with ATP . ^^^ Thus , the phosphorylation of GroEL during heat shock greatly enhances its ability to bind to certain denatured proteins and stimulates its ATP dependent dissociation in the absence of GroES . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The operon was found to be activated under heat shock conditions and transcribed as a polycistronic mRNA that contains the groES and groEL genes . ^^^ After activation , the polycistronic mRNA appeared to be cleaved between the groES and groEL genes and formed two monocistronic mRNAs . ^^^ The groES cleavage product appeared to be unstable and subjected to degradation , while the groEL cleavage product appeared to be stable and became the major mRNA representing the groESL operon after long periods of growth at a high temperature . ^^^ The polycistronic mRNA containing the groES and groEL genes was the major mRNA representing the groESL operon at a low temperature , and it reappeared when the cells were returned to the lower growth temperature after heat shock induction . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
One groE gene , groEL , has been shown to encode the synthesis of a 65 , 000 Mr polypeptide , whereas the second , groES , codes for the synthesis of a 15 , 000 Mr polypeptide . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The 70 , 58 , 41 and 14 . 5 kDa proteins were immunologically homologous to DnaK , GroEL , DnaJ and GroES heat shock proteins of Escherichia coli , respectively . 5 . harveyi GroES protein had a lower molecular mass ( 14 . 5 kDa ) than E . coli GroES , migrating in SDS PAGE as 15kDa protein . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The cDNA for nNOS was subcloned into the pCW vector under the control of the tac promotor and was coexpressed with the chaperonins groEL and groES in the protease deficient BL 21 strain of E . coli . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The 42 kDa capsid protein of bacteriophage HK 97 requires the GroEL and GroES chaperonin proteins of its Escherichia coli host to facilitate correct folding , both in vivo and in vitro . ^^^ In the absence of GroES and ATP , denatured gp 5 forms a stable complex with the 14 subunit GroEL molecule . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Eco ES 7 complex only bound one unfolded protein , thus GroES binding blocks one GroEL peptide binding site . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Mechanism of GroEL action : productive release of polypeptide from a sequestered position under GroES . ^^^ The chaperonin GroEL is a large , double ring structure that , together with ATP and the cochaperonin GroES , assists protein folding in vivo . ^^^ GroES forms an asymmetric complex with GroEL in which a single GroES ring binds one end of the GroEL cylinder . ^^^ Cross linking studies reveal that polypeptide binding occurs exclusively to the GroEL ring not occupied by GroES ( trans ) . ^^^ During the folding reaction , however , released GroES can rebind to the GroEL ring containing polypeptide ( cis ) . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Like GroEL and GroES of Escherichia coli , the chloroplast chaperonins can physically interact with each other . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
In Streptomyces coelicolor A 3 ( 2 ) , synthesis of the groES , groES groEL 1 and groEL 2 transcripts is induced either by heat shock or by undefined physiological stress signals present at a certain stage of growth . ^^^ Under all conditions tested , transcription of groES and groES groEL 1 originated from a unique start site upstream of groES , whereas transcription of groEL 2 originated from a unique site upstream of groEL 2 . ^^^ RNA polymerase isolated either from heat shocked or control mycelia allowed in vitro transcription from the P 1 promoter of groES / EL1 and the P 2 promoter of groEL 2 . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Each revealed two open reading frames encoding two proteins with a predicted molecular mass of 10 and 57 kDa , corresponding to GroES and GroEL respectively . ^^^ The sequence data confirm the existence of highly conserved structures , which could be functionally important for the concerted action of GroEL and GroES in the folding and assembly of other proteins , and possibly in the initiation of autoimmune diseases . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The role of ATP hydrolysis in the function of the chaperonin GroEL : dynamic complex formation with GroES . ^^^ In order to understand the role of ATP hydrolysis of the chaperonin GroEL during protein folding , we have studied GroEL GroES complex formation in the presence of ATP or ADP by using capillary electrophoresis and surface plasmon resonance . ^^^ Capillary electrophoresis analysis showed that the GroEL 14 mer and GroES 7 mer formed a 1 : 1 complex in the presence of ATP . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Expression was improved by overexpression of chaperonins GroEL and GroES . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The KD value remained almost unchanged when GroES and / or 10 microM ADP was included in the GroEL solution . ^^^ The effect of excess GroES on the preformed GroEL . rLA and GroEL / ES . rLA complexes was also examined . ^^^ With increasing GroES , the dissociation of GroEL and GroEL / ES from rLA was accelerated , and thus the possibility is suggested that the substrate protein and GroES compete for the same site on GroEL . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
In order to investigate in detail the molecular defects of the mutant MCAD proteins we overexpressed them in COS 7 and in an E . coli based expression system with and without co overexpression of the molecular chaperones GroES and GroEL . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
We have found that overproduction of the chaperonins GroES and GroEL from a multicopy plasmid suppresses a wide array of cold sensitive sec mutations in E . coli . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding . ^^^ The chaperonins GroEL and GroES of Escherichia coli facilitate protein folding in an adenosine triphosphate ( ATP ) dependent reaction cycle . ^^^ The kinetic parameters for the formation and dissociation of GroEL GroES complexes were analyzed by surface plasmon resonance . ^^^ Association of GroES and subsequent ATP hydrolysis in the interacting GroEL toroid resulted in the formation of a stable GroEL : ADP : GroES complex . ^^^ The complex dissociated as a result of ATP hydrolysis in the opposite GroEL toroid , without formation of a symmetrical GroEL : ( GroES ) 2 intermediate . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Efficient renaturation of urea denatured rhodanese using the chaperonin GroE system requires GroEL , GroES , and ATP . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
In addition , the DnaK and GroEL chaperone machines were discovered composed of DnaK / DnaJ / GrpE and GroES / GroEL heat shock proteins . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Here we demonstrate that in addition to the above three proteins , GroEL and GroES are necessary for the Cl 857 repressor to acquire full activity at the permissive temperature . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Upon addition of the cochaperonin GroES and Mg ATP to the adrenodoxin GroEL complex , adrenodoxin was released , indicating a specific binding between GroEL and adrenodoxin . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
A stable expression plasmid has been developed to overproduce the Escherichia coli GroES and GroEL molecular chaperones in large scale cultures . ^^^ Induced cells harboring the pT7groE expression plasmid accumulated GroEL to levels of 30 % total cell protein , and GroES to 4 5 % . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
We have developed an efficient histidine tagged bacterial expression system that allows the folding and assembly of E 1 alpha and E 1 beta subunits into the E 1 heterotetramer ( alpha 2 beta 2 ) in the presence of overexpressed chaperonins GroEL and GroES . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
In the presence of MgATP or MgADP the E . coli chaperonin proteins , GroEL and GroES , form a stable asymmetric complex with a stoichiometry of two GroEL 7 : one GroES 7 : seven MgADP . ^^^ On the basis of cross linking experiments with 8 azido ATP and the heterobifunctional reagent , N succinimidyl 3 ( 2 pyridyldithio ) propionate ( SPDP ) , it was suggested that GroES and MgADP are bound to the same GroEL ring which resists proteinase K digestion [ Nature 366 ( 1993 ) 228 233 ] . ^^^ However , we find that the SPDP promoted cross linking of GroES and GroEL occurs in the absence of Mg2+ , ADP or ATP , which are required for the formation of the asymmetric complex . ^^^ Cross linking is shown to occur only when the SPDP modified GroES is co precipitated with GroEL by trichloracetic acid . ^^^ Furthermore , there are structural grounds for questioning whether SPDP can crosslink , in a physiologically relevant manner , an amino group of GroES with any of the cysteinyl groups of GroEL . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The resulting mutant chaperonin protein is still functional and it can : ( a ) arrest the spontaneous folding of rhodanese in the absence of GroES and ATP , ( b ) assist refolding of the enzyme rhodanese in the presence of GroES and ATP / Mg2+ , and ( c ) permit the urea induced release and refolding of rhodanese from its complex with cpn 60 . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Reversal by GroES of the GroEL preference from hydrophobic amino acids toward hydrophilic amino acids . ^^^ GroEL / hsp60 cooperates with GroES / hsp10 , and the productive folding of proteins by GroEL generally requires GroES , which appears to regulate the binding and release of substrate proteins by GroEL . ^^^ In this study , we show that GroES reduces the specificity of GroEL for hydrophobic amino acids and increases its specificity for hydrophilic ones . ^^^ This shift by GroES of the GroEL specificity from hydrophobic amino acids toward hydrophilic ones might be of importance for its function in protein folding . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Purified spinach cpn 21 has a ring like toroidal structure and forms a stable complex with E . coli GroEL in the presence of ADP and is functionally interchangeable with bacterial GroES in the chaperonin facilitated refolding of denatured ribulose 1 , 5 bisphosphate carboxylase . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The chaperonin proteins , GroEL 14 and GroES 7 , inhibit protein aggregation and assist in protein folding in a potassium / ATP dependent manner . ^^^ Guanidinium decreased the ATPase activity of GroEL and attenuated the inhibition of GroEL ATP hydrolysis by GroES . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
In vitro , reactivation of heat inactivated luciferase to 80 % of its initial activity required the combined activity of DnaK , DnaJ and GrpE as well as ATP , but not GroEL and GroES . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Both the Escherichia coli chaperone systems , GroEL / GroES and DnaK / DnaJ / GrpE , can reactivate heat treated RNA polymerase . ^^^ In this protection reaction , the GroES protein is not essential , but its presence reduces the amount of GroEL required . ^^^ GroEL and GroES can also reactivate heat inactivated RNAP in the presence of ATP . ^^^ The mutant GroEL 673 protein , with or without GroES , is incapable of reactivating heat inactivated RNAP . ^^^ GroEL 673 can only protect RNAP , and this protecting ability is not stimulated by GroES . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Recombination frequencies in the groES , groEL and dnaK mutants were decreased 6 to 21 % of those of the isogenic wild type strain , at a sub lethal temperature . ^^^ Thus , the heat shock proteins GroES , GroEL and DnaK apparently participate in homologous recombination in Escherichia coli . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The mitochondrial chaperonin system consists of chaperonin 60 ( also termed hsp 60 ) , which is homologous to E . coli groEL , and chaperonin 10 , which is homologous to E . coli groES . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The single ring chaperonin co factor GroES interacts with the C 40 domain while the ATP binding site of GroEL is probably close to the junction between N 15 and C40 . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The groESL operon codes for the chaperone proteins GroES and GroEL , which are responsible for mediating the folding and assembly of many proteins . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Cosynthesis of GroEL and GroES chaperonins resulted in complete proteolysis of the scFvNC 10 FLAG gIIIp fusion product and did not improve total phage production . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Purification and characterization of recombinant human p50csk protein tyrosine kinase from an Escherichia coli expression system overproducing the bacterial chaperones GroES and GroEL . ^^^ An Escherichia coli expression system overproducing the bacterial chaperones GroES and GroEL was engineered and has been successfully used to produce large quantities of the recombinant human protein tyrosine kinase p50csk . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The E . coli chaperonin proteins , GroEL and GroES , assist in folding newly synthesized proteins . ^^^ GroES is necessary for GroEL assisted folding under conditions where the substrate protein can not spontaneously fold . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Several bacteriophages use the Escherichia coli GroES and GroEL chaperonins for folding and assembly of their morphogenetic structures . ^^^ Like GroES , the bacteriophage Gp 31 protein forms a stable complex with the E . coli GroEL protein in the presence of Mg ATP and inhibits the ATPase activity of GroEL in vitro . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The sequence of the groES and groEL genes from the mouse pneumonitis agent of Chlamydia trachomatis . ^^^ The co transcribed structural genes , groES and groEL , of the groE stress response operon from Chlamydia trachomatis mouse pneumonitis ( MoPn ) , were cloned and sequenced . ^^^ The calculated molecular masses of the encoded heat shock proteins ( Hsp ) , a small Hsp ( GroES ) and Hsp 60 ( GroEL ) , are 11 , 089 and 58 , 367 Da , respectively . ^^^ By comparison with other known chlamydial groES and groEL sequences , there is 89 and 94 % nucleotide ( nt ) identity with C . trachomatis human strains ( serovars A and L 2 ) , 77 and 82 % with C . psittaci strain GPIC , and 75 and 80 % with C . pneumoniae isolate AR 39 . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Truncated GroEL monomer has the ability to promote folding of rhodanese without GroES and ATP . ^^^ However , the peptide fragments of GroEL of molecular size 34 50 kDa , which are produced by limited proteolysis of monomeric GroEL and are unable to assemble into an oligomer , retain the ability to promote folding of rhodanese even though the yield of productive folding is lower than the intact GroEL / GroES / ATP system . ^^^ This promotion by truncated GroEL obeys rapid kinetics and does not require GroES and ATP . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Increased synthesis of DnaK , GroEL , and GroES homologs by Francisella tularensis LVS in response to heat and hydrogen peroxide . ^^^ By N terminal sequence analysis , these three proteins were found to be extensively homologous to the highly conserved chaperone proteins DnaK , GroEL , and GroES of Escherichia coli . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
As in the self assembly of GroEL , that of symbionin was stimulated by the presence of GroES . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Generation of a stable folding intermediate which can be rescued by the chaperonins GroEL and GroES . ^^^ This intermediate is readily refolded by the chaperonins GroEL and GroES and may prove useful in future attempts to describe several aspects of chaperonin action at physiological temperatures . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Under `` non permissive ' ' conditions , where unassisted spontaneous folding could not occur , reactivation to the native state required the complete chaperonin system ( e . g . groEL , groES , and MgATP ) . ^^^ The results suggest that the incompletely folded protein species that are released from groEL , in the absence of groES , are not necessarily committed to the native state . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The GroE heat shock proteins ( GroEL and GroES ) of Escherichia coli represent major molecular chaperones that participate in folding ( and assembly ) of a variety of proteins and are essential for cell growth at all temperatures . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Nucleotide sequence analysis revealed that groEL 1 , but not groEL 2 , was preceded by a groES like gene . ^^^ Northern blots showed that heat shock induced the accumulation of transcripts corresponding to groES ( 0 . 7 kb ) , groES / EL1 ( 2 . 3 kb ) and groEL 2 ( 2 . 1 kb ) . ^^^ Unique transcription start points and promoters were located for groES / EL1 and groEL 2 , having 10 and 35 hexamers similar to eubacterial vegetative promoters . ^^^ Regions located 5 ' to the groES / EL1 or groEL 2 structural genes contain ' GCACTCN9GAGTGC ' motifs conserved upstream from the heat shock genes of other bacteria . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The effect of groES on the groEL dependent assembly of dodecameric glutamine synthetase in the presence of ATP and ADP . ^^^ GS complex ( no groES ) , a groEL . ^^^ These results indicate that groES facilitates GS assembly from groEL by inducing the rapid release of GS from groEL , which in turn increases the concentration of assembly competent GS monomers . ^^^ In addition , groES can initiate renaturation of GS from the groEL . ^^^ Since ATP hydrolysis is not absolutely required , the combined binding energies of groES and ATP ( or ADP ) appear to be sufficient to weaken the binding affinity of groEL for GS subunits and facilitate the release and refolding of assembly competent GS monomers from groEL . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
For both NifA preparations , cochaperonin GroES and ATP promoted release of NifA from GroEL . ^^^ These results provide evidence for the association of NifA with GroEL and for the role of both GroEL and GroES in the solubilization and thereby folding of the nif transcriptional activator . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Like the prokaryotic cochaperonin GroES , which interacts with the prototypical Escherichia coli chaperonin GroEL and regulates its ATPase activity , cofactor A modulates the ATPase activity of its cognate chaperonin . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
In the presence of ADP , the molecular chaperones GroEL and GroES from Escherichia coli not only facilitated the refolding of various proteins , but also prevented their irreversible heat inactivation in vitro . ^^^ The presence of GroE ( GroEL and GroES ) and ADP also protected against heat inactivation of native enzymes at various temperatures . ^^^ These findings suggest that in the presence of GroES , nucleotide binding is an important event in the mechanism of GroEL facilitated protein folding . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
There was no correlation between acute reactive arthritis and antibodies to heat shock proteins GroEL , GroES and DnaK . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Chaperonin 60 and chaperonin 10 ( GroEL and GroES homologues , respectively ) have been isolated from extracts of the anaerobic thermophile Thermoanaerobacter brockii . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Characterization of a functional GroEL 14 ( GroES 7 ) 2 chaperonin hetero oligomer . ^^^ Chaperonins GroEL and GroES form two types of hetero oligomers in vitro that can mediate the folding of proteins . ^^^ Chemical cross linking and electron microscopy showed that in the presence of adenosine triphosphate ( ATP ) , two GroES 7 rings can successively bind a single GroEL 14 core oligomer . ^^^ The symmetric GroEL 14 ( GroES 7 ) 2 chaperonin , whose central cavity appears obstructed by two GroES 7 rings , can nonetheless stably bind and assist the ATP dependent refolding of RuBisCO enzyme . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The interaction of the oligomeric bacterial chaperonin GroEL and its cochaperonin , GroES , in the presence of adenosine diphosphate ( ADP ) forms an asymmetric complex . ^^^ Because complete folding of a nonnative substrate protein in the presence of GroEL and GroES only occurs in the presence of ATP , but not with ADP , the symmetric chaperonin complexes formed during the GroE cycle are proposed to be functionally significant . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Interestingly , overproduced chaperonin ( GroEL and GroES ) partly prevented degradation of TET365 . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
In vitro reconstitution of the 24 meric E 2 inner core of bovine mitochondrial branched chain alpha keto acid dehydrogenase complex : requirement for chaperonins GroEL and GroES . ^^^ The denatured E2c monomers ( apparent M ( r ) = 27 , 000 ) were diluted 100 fold at 25 degrees C into a refolding buffer containing 5 mM Mg ATP and a 4 fold molar excess of chaperonins GroEL and GroES . ^^^ A stable GroEL E2c complex was isolated which , in the presence of GroES and Mg ATP , generated active E2c 24 mers . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
GroEL could be eluted from the fusion protein by incubation with ATP and either GroES or casein , consistent with results of in vitro folding assays . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Strikingly , we find that , upon addition of ATP and the cochaperonin GroES , polypeptide is released rapidly from GroEL in a predominantly nonnative conformation that can be trapped by mutant forms of GroEL that are capable of binding but not releasing substrate . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Location of a folding protein and shape changes in GroEL GroES complexes imaged by cryo electron microscopy . ^^^ Biochemical studies show that GroES improves the efficiency of GroEL function , but the structural basis for this is unknown . ^^^ Addition of GroES to GroEL in the presence of ATP causes a dramatic hinge opening of about 60 degrees . ^^^ GroES binds to the equivalent surface of the GroEL outer domains , but on the opposite end of the GroEL oligomer to the protein substrate . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Tubulin remains bound to the immobilized groEL column after extensive washing and is released upon incubation with groES and ATP . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Rapid degradation of an abnormal protein in Escherichia coli involves the chaperones GroEL and GroES . ^^^ A similar stimulation of proteolysis was observed in cells overproducing GroEL or both GroEL and GroES ; in these cells , more CRAG was associated with GroEL than in the wild type . ^^^ However , in a temperature sensitive groES mutant , CRAG was completely stable at the nonpermissive temperature and accumulated bound to GroEL . ^^^ These findings indicate that the association of CRAG with GroEL is a rate limiting step in CRAG degradation , which also requires a subsequent action of GroES . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
By using a simple strategy which combines the genetic tools of Escherichia coli and Bacillus subtilis , we have cloned genes encoding two of the most abundant stress proteins in Z . mobilis , GroES and GroEL . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
On the basis of N terminal sequence analysis and immunological cross reactivity data , the 64 and 10 kDa proteins were the C . jejuni homologs of Escherichia coli GroEL and GroES proteins , respectively . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
For its function , the Escherichia coli chaperonin GroEL requires the presence of ATP and co chaperonin GroES . ^^^ It is suggested that interaction with ATP induces structural and functional differences between two initially identical rings in GroEL ( inter ring negative cooperativity ) and that the subsequent binding of GroES occurs to the ring that is occupied first by ATP in a positively cooperative manner . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Thus , both the initial rates of protein folding and final yields observed with this heterologous combination are virtually identical to those obtained with groEL and groES . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The GroES and GroEL proteins of Escherichia coli function together as the GroE molecular chaperone machine to ( 1 ) prevent denaturation and aggregation and ( 2 ) assist the folding and oligomerization of other proteins without being part of the final structure . ^^^ Previous genetic and biochemical analyses have determined that this activity requires interactions of the GroES 7 mer with the GroEL 14 mer . ^^^ Recently , we have identified a region of the GroES protein that interacts with the GroEL protein . ^^^ To identify those residues of the GroEL protein that interact with GroES , we have exploited the thermosensitive phenotype of strains bearing mutations at one or the other of two GroEL interacting residues of GroES . ^^^ We have isolated , cloned , and sequenced six suppressor mutations in groEL , three independent isolates for each groES mutant . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The Escherichia coli grpE gene ( along with dnaK , dnaJ , groEL , and groES ) was originally identified as one of the host factors required for phage lambda growth . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
These can be activated and released in the presence of the added chaperones , DnaJ , DnaK , GrpE , GroEL , GroES and ATP . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Increased solubility of trimethoprim resistant type S 1 DHFR from Staphylococcus aureus in Escherichia coli cells overproducing the chaperonins GroEL and GroES . ^^^ The production of the trimethoprim resistant type S 1 dihydrofolate reductase ( DHFR ) from Staphylococcus aureus in Escherichia coli cells overproducing the chaperonins GroEL and GroES is described . ^^^ Thus , the higher concentrations of GroES and GroEL in cells overproducing the chaperonins partially protect DHFR from aggregation , resulting in higher concentrations of soluble and active DHFR in the cell . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Here , we report on the engineering of bacterial strains which overproduce chaperone proteins of the Hsp 70 ( DnaK , DnaJ and GrpE ) and Hsp 60 ( GroEL and GroES ) families . ^^^ The simultaneous overproduction in E . coli of the chaperones DnaK , DnaJ and GrpE on the one hand , or GroEL and GroES on the other hand , and the human non receptor protein tyrosine kinases Csk , Fyn or Lck resulted in increased solubility of the recombinant kinases . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Residue lysine 34 in GroES modulates allosteric transitions in GroEL . ^^^ This residue is near the carboxy terminus of the mobile loop in GroES ( residues 17 32 ) which becomes immobilized upon formation of the GroEL / GroES complex [ Landry et al . ( 1993 ) Nature 364 , 255 258 ] . ^^^ Both charge neutralization ( Lys 34 > Ala ) and charge reversal ( Lys 34 > Glu ) at this position have little effect on the binding constant of GroES to GroEL , but they increase the enhancement by GroES of cooperativity in ATP hydrolysis by GroEL . ^^^ They suggest that Lys 34 in GroES modulates the allosteric transition in GroEL by stabilizing a relaxed ( R ) like state . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The translated amino acid sequence of these ORFs showed a high degree of homology with known sequences for GroES and GroEL from several bacterial species and humans . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The amino acid sequences deduced from the nucleotide sequences of the two open reading frames are identical to those gained from N terminal sequencing of purified groEL and groES proteins . ^^^ This finding demonstrates that these two open reading frames correspond to groEL and groES genes of Synechocystis sp . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
In contrast to other GroE ligands , the tailspike polypeptide was bound by and released from GroE in similar states of folding , and the presence of GroES in addition to GroEL had no effect on reconstitution yields at any temperature . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The groES and groEL genes of Escherichia coli have been shown previously to belong to a single operon under heat shock regulation . ^^^ ATP hydrolysis by GroEL results in the release of the bound polypeptides , a process that often requires the action of GroES . ^^^ In an effort to understand GroEL and GroES structure and function , we have determined the nucleotide changes of nine mutant alleles of groEL . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Substoichiometric amounts of the molecular chaperones GroEL and GroES prevent thermal denaturation and aggregation of mammalian mitochondrial malate dehydrogenase in vitro . ^^^ The molecular chaperones GroEL and GroES were produced at very high levels in Escherichia coli , purified , and shown to protect pig mitochondrial malate dehydrogenase ( MDH ) against thermal inactivation in vitro . ^^^ The apparent rate of MDH inactivation at 37 degrees C was reduced by a factor of at least 5 in a process which required only GroEL , GroES , and ATP . ^^^ Protection could be extended for more than 24 hr at 37 degrees C and was observed at molar ratios of chaperones to MDH as low as 1 : 4 , suggesting that GroEL and GroES perform multiple turnovers in the absence of auxiliary chaperones . ^^^ We speculate that GroEL and GroES perform similar protective roles in vivo and thereby increase the half life of proteins which otherwise might aggregate under physiological conditions . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
GroEL and GroES increase the specific enzymatic activity of newly synthesized rhodanese if present during in vitro transcription / translation . ^^^ The bacterial chaperonins , GroEL and GroES , along with the rhodanese substrate thiosulfate greatly enhance the specific enzymatic activity of the rhodanese polypeptide that is formed . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
GroEL , GroES , and ATP dependent folding and spontaneous assembly of ornithine transcarbamylase . ^^^ Upon addition of the cochaperonin groES and ATP to the isolated OTC groEL complex , OTC monomers were folded , released , and assembled into active trimer . ^^^ Neither groES nor ATP alone was sufficient to release active OTC from groEL . ^^^ A nonhydrolyzable ATP analog could release bound OTC from groEL in the presence of groES , but the OTC monomers were not competent for assembly . ^^^ These data show that recovery of OTC activity in vitro can be efficiently directed by the bacterial chaperonins in the presence of ATP and suggest that the mechanism of reconstitution involves ATP and groES dependent folding and release of OTC monomers from groEL , followed by spontaneous assembly of trimers . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Sequencing of 2 , 309 bp led to the detection of two open reading frames in the order groES groEL . ^^^ The groESL operon of B . stearothermophilus could complement E . coli groES ( Ts ) and groEL ( Ts ) mutants for growth at high temperature and for propagation of phage lambda . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
In the upstream regions of two of the groEL , but not the third , open reading frames corresponding to GroES proteins were also identified . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Over expression of the chaperonins GroEL and GroES significantly suppressed the temperature dependent pattern of expression of Cu , Zn superoxide dismutases in Escherichia coli and increased the yield of active enzyme . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Under optimal conditions and in the presence of ATP , chaperonins ( groEL and groES ) enhanced the renaturation of dodecameric glutamine synthetase ( GS ) with yields of active enzyme between 75 and 85 % of the original activity ( Fisher , M . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The sequences of the 10 . 3 and 58 kDa polypeptides were homologous to those of the Escherichia coli GroES and GroEL heat shock proteins , respectively . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Hydrolysis of adenosine 5 ' triphosphate by Escherichia coli GroEL : effects of GroES and potassium ion . ^^^ In the absence of groES , the K ( + ) dependent hydrolysis of ATP by groEL continues to completion . ^^^ In the presence of groES , the time course for the hydrolysis of ATP by groEL becomes more complex . ^^^ This leads to the formation of an asymmetric binary complex , groEL 14 MgADP7 groES 7 , in which 7 mol of ADP is trapped in a form that does not readily exchange with free ADP . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The addition of exceedingly small quantities of GroES in the presence of excess GroEL and a moderate amount of ATP also has a marked effect on the barnase refolding rate constant , suggesting that GroES may have higher affinity for the barnase : GroEL complex than for GroEL . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The influence of co overexpression of the bacterial chaperonins GroEL and GroES on solubility , tetramer formation and enzyme activity of three variants of heterologously expressed human medium chain acyl CoA dehydrogenase ( MCAD ) was analysed in order to investigate the molecular mechanism underlying MCAD deficiency caused by the prevalent K304E mutation . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Facilitation of protein folding by GroEL usually requires involvement of GroES and ATP . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The ribosome bound protein is enzymatically inactive but can be activated and released from the ribosomes without additional protein synthesis by subsequent incubation in the presence of the added chaperones DnaJ , DnaK , GrpE , GroEL , and GroES plus ATP . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Although genetic and biochemical evidence has established that GroES is required for the full function of the molecular chaperone , GroEL , little is known about the molecular details of their interaction . ^^^ GroES enhances the cooperativity of ATP binding and hydrolysis by GroEL ( refs 4 , 5 ) and is necessary for release and folding of several GroEL substrates . ^^^ Here we report that native GroES has a highly mobile and accessible polypeptide loop whose mobility and accessibility are lost upon formation of the GroES / GroEL complex . ^^^ Flexibility may be required in the mobile loops on the GroES seven mer to allow them to bind simultaneously to sites on seven GroEL subunits , which may themselves be able to adopt different arrangements , and thus to modulate allosterically GroEL / substrate affinity . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
This report is concerned with the structural characterization and genetic regulation of new bacterial groES and groEL chaperonin genes , and presents two novelties . ^^^ As an attractive hypothesis it follows that B . japonicum may modulate its cellular contents of GroES and GroEL like chaperonins in response to specific environmental conditions and physiological needs . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The operon ( groESL ) coding for the Lactococcus lactis subsp . lactis heat shock proteins GroEL and GroES , has been isolated and its complete nucleotide ( nt ) sequence determined . ^^^ A region of this 5 . 0 kb EcoRI fragment was sequenced and revealed that the groES gene was located 5 ' to groEL . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
When these same phytochrome sequences are coexpressed with the chaperonins GroEL and GroES , the truncated phytochrome migrates as a native like dimer in size exclusion chromatography and no higher order aggregates were detected . ^^^ GroEL and GroES inhibition of phytochrome aggregation in E . coli presumably occurs via the suppression of folding pathways leading to incorrectly folded phytochrome . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The isolated genomic fragment was found to contain two open reading frames , the sequences of which were highly homologous to the prokaryotic groES and groEL families of genes . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The Escherichia coli protein GroES is a co chaperonin that is able to assist GroEL in the refolding of proteins . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
However , when this fusion protein was produced in a bacterial strain overexpressing the bacterial chaperonins GroEL and GroES , a fraction of GST was exported into the periplasmic space with the correct N terminal sequence . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The ' mobile loop ' segment , previously identified as a GroEL binding determinant , is disordered in the crystal structure in six subunits ; the single well ordered copy extends from the bottom outer rim of the GroES dome , suggesting that the cavity within the dome is continuous with the polypeptide binding chamber of GroEL in the chaperonin complex . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
In vivo expression kinetics of seven of eight examined new proteins were found to be similar to those of the four most studied heat shock proteins , DnaK , DnaJ , GroEL ( MopA ) , and GroES ( MopB ) . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The mature form of PDPc was coexpressed in Escherichia coli with the chaperonin proteins groEL and groES . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Sequencing of this fragment indicated the presence of two open reading frames encoding polypeptides of 97 and 544 amino acids , respectively , which showed high similarity to the molecular chaperones GroES and GroEL , respectively , from several eubacteria and eukaryotic organelles . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Further , complexes of GroEL with GroES or rhodanese display the same sensitivity to proteolysis , unlike the GroEL GroES rhodanese complex , which is protected from proteolysis . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Biochemical characterization of symmetric GroEL GroES complexes . ^^^ When chaperonins GroEL and GroES are incubated under functional conditions in the presence of ATP ( 5 mM ) and K+ ( 150 mM ) , GroEL GroES complexes appear in the incubation mixture , that are either asymmetric ( 1 : 1 GroEL : GroES oligomer ratio ) or symmetric ( 1 : 2 GroEL : GroES oligomer ratio ) . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Protein folding in the central cavity of the GroEL GroES chaperonin complex . ^^^ GroEL bound dihydrofolate reductase assumes its native conformation when the GroES cofactor caps one end of the GroEL cylinder , thereby discharging the unfolded polypeptide into an enclosed cage . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Although bound ATP induces modest conformational shifts in the equatorial domain , the stereochemistry that functionally coordinates GroEL ' s affinity for nucleotides , polypeptide , and GroES remains uncertain . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
One of the intragenic suppressors has been mapped to a segment that codes for the GroES mobile loop , previously shown to be indispensable for proper GroES / GroEL interaction . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The best studied family of molecular chaperones are called the chaperonins , the archetypal examples being the GroEL and GroES proteins of Escherichia coli . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
In vitro the chaperonin proteins , GroEL and GroES , facilitate the folding of some other proteins under conditions where that process does not occur spontaneously . ^^^ Using values drawn from a number of such in vitro studies , together with the known rates of in vivo protein synthesis by Escherichia coli and the known quantities of GroEL and GroES in E . coli , an assessment of the general role of these proteins in protein folding in vivo has been made . ^^^ However , in general , there appears to be sufficient GroEL and GroES to facilitate the folding of no more than 5 % of all of the proteins within E . coli . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The Bacillus subtilis GroESL chaperonin was isolated by sucrose density gradient centrifugation and the constituent GroES and GroEL moieties were purified by electrophoresis in agarose . ^^^ Electron microscopic images of negatively stained GroEL and GroES oligomers and GroESL complexes were averaged using a reference free alignment method . ^^^ The GroEL and GroES particles had the sevenfold symmetry characteristic of their Escherichia coli counterparts . ^^^ GroESL complexes , reconstituted efficiently in vitro from GroEL and GroES in the absence of added ADP or ATP , had the characteristic bullet and football like shapes in side view . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
We found that sera from these mice contained IgG antibodies that reacted in immunoblots with recombinant heat shock protein 70 ( DmaK from Escherichia coli ) but not with heat shock protein 60 ( GroEL ) or heat shock protein 10 ( GroES ) . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Overproduction , purification and characterization of GroES and GroEL from thermophilic Bacillus stearothermophilus . ^^^ To facilitate purification of the two chaperonins GroES and GroEL encoded by the thermophilic Bacillus stearothermophilus , an Escherichia coli strain was constructed in which the geoESL operon was replaced by that of B . stearothermophilus . ^^^ Both proteins GroES and GroEL , were purified from E . coli using the standard protocol with some modifications . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Characterization of the active intermediate of a GroEL GroES mediated protein folding reaction . ^^^ Recent studies of GroE mediated protein folding indicate that substrate proteins are productively released from a cis ternary complex in which the nonnative substrate is sequestered within the GroEL channel underneath GroES . ^^^ Stopped flow fluorescence anisotropy of a pyrene rhodanese GroEl complex indicates that addition of GroES and ATP ( but not ADP ) leads to a rapid change in substrate flexibility at GroEL . ^^^ Strikingly , when GroES release is blocked by the use of either a nonhydrolyzable ATP analog or a single ring GroEL mutant , substrates complete folding while remaining associated with chaperonin . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The protein folding activity of chaperonins correlates with the symmetric GroEL 14 ( GroES 7 ) 2 heterooligomer . ^^^ Chaperonins GroEL and GroES form , in the presence of ATP , two types of heterooligomers in solution : an asymmetric GroEL14GroES7 `` bullet ' ' shaped particle and a symmetric GroEL 14 ( GroES 7 ) 2 `` football ' ' shaped particle . ^^^ Under limiting concentrations of ATP or GroES , excess ADP , or in the presence of 5 ' adenylyl imidodiphosphate , a correlation is seen between protein folding and the amount of symmetric GroEL 14 ( GroES 7 ) 2 particles in a chaperonin solution , as detected by electron microscopy or by chemical crosslinking . ^^^ Kinetic analysis suggests that protein folding is more efficient when carried out by a chaperonin solution populated with a majority of symmetric GroEL 14 ( GroES 7 ) 2 particles than by a majority of asymmetric GroEL14GroES7 particles . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
While the co overexpression of the DnaK and DnaJ molecular chaperones led to a 3 6 fold increase in the recovery of enzymatically active preS 2 S ' beta galactosidase over a wide range of growth temperatures ( 30 42 degrees C ) , an increase in the concentration of the GroEL and GroES chaperonins had a significant effect at 30 degrees C only . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The chaperonins GroEL and GroES catalyze the folding of ribulose bisphosphate carboxylase at a rate proportional to the GroEL concentration . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
GroEL undergoes an allosteric transition from its tight binding T state to a weaker binding R state on the cooperative binding of nucleotides ( ATP / ADP ) and GroES . ^^^ Binding of GroES and nucleotides to a preformed GroEL . denatured barnase complex forms an intermediately fast folding complex . ^^^ This step causes transient release of GroES and formation of the GroEL . denatured protein complexes with higher annealing potential . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Bovine endothelial constitutive nitric oxide synthase ( eNOS ) was expressed in E . coli as a soluble , catalytically active enzyme using the pCW expression vector coexpressed with a plasmid , pGroELS , encoding the chaperonins groEL and groES . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Protein folding by the double ring chaperonin GroEL is initiated in cis ternary complexes , in which polypeptide is sequestered in the central channel of a GroEL ring , capped by the co chaperonin GroES . ^^^ Here we address this question using a ' cis only ' mixed ring GroEL complex that binds polypeptide and GroES on only one of its two rings . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
This chaperone network is proposed to be of particular importance for the assisted refolding of proteins that are unfolded by stress treatment such as heat shock and whose size is too large to allow folding inside the substrate binding cavity of the GroEL ring underneath GroES . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Maximal expression was obtained in nirB E . coli cells grown anaerobically at 22 + / 1 degrees C , in conjunction with co expression of a plasmid borne cysG gene ( encoding the rate limiting enzyme in siroheme synthesis ) and co transformation with plasmid pGroESL ( encoding bacterial chaperonins GroES and GroEL ) . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The co chaperonin GroES is an essential partner in protein folding mediated by the chaperonin , GroEL . ^^^ Two recent crystal structures of GroES provide a structural basis to understand how GroES forms the lid on the folding active cis ternary complex , and how the GroEL GroES complex enhances folding . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Co expression of the bacterial chaperones , GroES and GroEL , resulted in a proportional twofold increase in soluble PMI while causing an overall decrease in the PMI expression level . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
It was found that GroEL could not bind to the adsorbed GroES in the presence of AMP PNP and Mg2+ , suggesting that the side of GroES with the central protrusion faces away from the GroEL lumen , because only one side of GroES was observed under these conditions . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Cloning , characterization and functional analysis of groEL like gene from thermophilic cyanobacterium Synechococcus vulcanus , which does not form an operon with groES . ^^^ A gene encoding 57 102 Da polypeptide homologous to groEL of Escherichia coli but accompanying no groES , has been cloned and sequenced from a thermophilic cyanobacterium , Synechococcus vulcanus . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
They contain only the groES and groEL genes and always in the same order . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The Escherichia coli chaperonins GroEL and GroES facilitate the refolding of polypeptide chains in an ATP hydrolysis dependent reaction . ^^^ The addition of GroES resulted in a marked increase in the rate of nonnative polypeptide release from GroEL , indicating that the cochaperonin binds more rapidly than the dissociation of polypeptides . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
We analyzed the involvement of chaperonins GroES and GroEL in the biosynthesis of the three hydrogenase isoenzymes , HYD 1 , HYD 2 , and HYD 3 , of Escherichia coli . ^^^ Total hydrogenase activity was found to be reduced by up to 60 % in groES and groEL thermosensitive mutant strains . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The use of the complete chaperonin system ( GroEL , GroES , and ATP ) eliminated the GroEL mediated increase in recovery and folding proceeded less efficiently than in buffer alone . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Binding of the Escherichia coli cochaperonin GroES to chaperonin GroEL is mediated , at least in part , by a mobile polypeptide loop in GroES that becomes immobilized in the GroEL / GroES / nucleotide complex . ^^^ When bound to GroEL , a synthetic peptide representing the mobile loop of either GroES or Gp 31 adopts a characteristic bulged hairpin conformation as determined by transferred nuclear Overhauser effects in NMR spectra . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Chaperonins GroEL and GroES : views from atomic force microscopy . ^^^ The Escherichia coli chaperonins , GroEL and GroES , as well as their complexes in the presence of a nonhydrolyzable nucleotide AMP PNP , have been imaged with the atomic force microscope ( AFM ) . ^^^ We demonstrate that both GroEL and GroES that have been adsorbed to a mica surface can be resolved directly by the AFM in aqueous solution at room temperature . ^^^ However , with glutaraldehyde fixation of already adsorbed molecules , the resolution of both GroEL and GroES was further improved , as all seven subunits were well resolved without any image processing . ^^^ GroEL with GroES bound can be clearly distinguished from those without . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The Caulobacter crescentus groESL operon was cloned , sequenced and found to be homologous to previously described groES and groEL genes and proteins . ^^^ The size of the groESL specific transcript ( 2 . 3 kb ) suggested that groES and groEL of C . crescentus are organized in a bicistronic operon . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The extractive cultivation of recombinant Escherichia coli cells to produce , release , and separate heat shock proteins ( HSPs ; GroEL and GroES ) using poly ( ethylene glycol ) ( PEG ) / dextran ( Dex ) aqueous two phase systems was developed . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Co expression of this plasmid with a second plasmid vector over expressing the E . coli chaperonin proteins , groES and groEL , resulted in a several hundred fold increase in PCC specific activity , to a level comparable with that found in crude human liver extracts . ^^^ Our findings indicated that the groES and groEL chaperonin proteins were essential for folding and assembly of the human PCC heteromeric subunits . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Interaction between the two back to back seven membered rings of GroEL plays an important role in regulating binding and release of folding substrates and of the small chaperonin GroES . ^^^ Using cryo electron microscopy , we have obtained three dimensional reconstructions to 30 A resolution for GroEL and GroEL GroES complexes in the presence of ADP , ATP , and the nonhydrolyzable ATP analog , AMP PNP . ^^^ Nucleotide binding to the equatorial domains of GroEL causes large rotations of the apical domains , containing the GroES and substrate protein binding sites . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The groEL gene encoded a polypeptide of 544 amino acids and was preceded by the incomplete groES gene , lacking its 5 ' end . ^^^ The addition of E . coli GroES increased recovery of the enzyme activity , indicating that C 125 GroEL could function in coordination with E . coli GroES . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The chaperonin GroEL is a large complex composed of 14 identical 57 kDa subunits that requires ATP and GroES for some of its activities . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The interaction of GroEL with urea unfolded dihydrofolate reductase ( DHFR ) has been studied in the presence of DHFR substrates by investigating the ability of GroES to release enzyme under conditions where a stable GroES GroEL DHFR ternary complex can be formed . ^^^ These results are in contrast to those observed with the GroEL DHFR complex formed by thermal inactivation of DHFR at 45 degrees C in which GroES addition leads to partial protection of bound DHFR . ^^^ It is suggested that the ability of GroES to bind on the same side of the GroEL double toroid as the target protein and displace it into the central cavity depends on the way the protein substrate is presented to the GroEL molecule . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
These data suggest that GDH is bound weakly to GroEL and that GroES is not required for release of the protein . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The fusion protein with MBP is soluble , binds calmodulin and is enzymically active whereas the non fusion protein is insoluble and does not bind calmodulin unless co expressed with bacterial chaperone proteins ( either GroES and GroEL , or DnaK , DnaJ and GrpE ) . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Differential induction of the chaperonin GroEL and the Co chaperonin GroES by heat , acid , and UV irradiation in Lactococcus lactis subsp . lactis . ^^^ Contrasting to the relative induction of the groEL gene product , the second protein encoded by the groESL operon , GroES shows significantly higher induction under all stress situations . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Further , GroES partially suppresses the GroEL ATPase activity in the same temperature range . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
A His 10 peptide attached to the amino terminus produced a high yield of soluble protein when coexpressed with GroEL and GroES . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Abortus ssb , uvrA , GroES , and GroEL genes into the prokaryotic expression vector pMAL c 2 using PCR . ^^^ Escherichia coli DH 5 alpha was transformed with the pMAL ssb , pMAL uvrA , pMAL GroES , and pMAL GroEL constructs separately , and gene expression was induced by isopropyl beta D thiogalactopyranoside . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
When cell extracts were applied onto a fetuin column , both TF and GroEL bound but not GroES . ^^^ Upon ATP addition , TF and GroEL were eluted together and remained tightly associated ( even in presence of GroES ) in complexes containing one TF per GroEL 14 mer . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Digestions of the GroES oligomer with trypsin , chymotrypsin and Glu C protease from Staphylococcus aureus V 8 ( V 8 ) have helped to locate three regions in the GroES sequence that are sensitive to limited proteolysis and have provided information of the GroES domains involved in monomer monomer and GroEL interaction . ^^^ The removal of the first 20 or 27 amino acids of the N terminal region of each GroES monomer by trypsin or chymotrypsin respectively , abolish the oligomerization of the GroES complex and its binding to GroEL . ^^^ The V 8 treatment of GroES promotes the breakage of the peptide bond between Glu 18 and Thr 19 but not the liberation of the N terminal fragment from the GroES oligomer , which is capable of forming with GroEL a complex active in protein folding . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Assembly of membrane containing bacteriophage PRD 1 is dependent on GroEL and GroES . ^^^ The formation of PRD 1 particles is , in addition to the virus encoded assembly factors P 10 and P 17 , dependent on GroEL / GroES chaperonins . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Bacterial heat shock proteins ( HSPs ) from Escherichia coli ( GroES , GroEL , and DNAk ) were tested for their ability to induce by themselves the expression and release of interleukin 6 ( IL 6 ) , tumor necrosis factor alpha ( TNF alpha ) , and granulocyte monocyte colony stimulating factor ( GM CSF ) by human monocytes and GM CSF , IL 6 , E selectin , intercellular adhesion molecule 1 ( ICAM 1 ) , and vascular cell adhesion molecule 1 ( VCAM 1 ) by human umbilical vein endothelial cells ( HUVEC ) . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Bacterial heat shock proteins ( HSPs ) from Escherichia coli ( GroES , GroEL and DnaK ) were studied for their ability to induce by themselves the expression and release of tumour necrosis factor alpha ( TNF alpha ) , interleukin 1 alpha ( IL 1 alpha ) , interleukin 6 ( IL 6 ) and intercellular adhesion molecule 1 ( ICAM 1 ) by cultured human keratinocytes . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The chaperonin GroEL binds nonnative proteins in its central channel through hydrophobic interactions and initiates productive folding in this space underneath bound co chaperone , GroES , in the presence of ATP . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Interestingly , catalysis of the folding reaction requires the formation of symmetrical football shaped GroEL 10 GroES 2 particles and the intermediate release of the nonnative protein from the chaperone complex . ^^^ Our results show that , in the presence of GroES , the complex architecture of the GroEL toroids allows maintenance of two highly interregulated rings simultaneously active in protein folding . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The cylindrical chaperonin GroEL and its cofactor GroES mediate ATP dependent protein folding in Escherichia coli . ^^^ Recent studies in vitro demonstrated that GroES binding to GroEL causes the displacement of unfolded polypeptide into the central volume of the GroEL cavity for folding in a sequestrated environment . ^^^ Resulting native protein leaves GroEL upon GroES release , whereas incompletely folded polypeptide can be recaptured for structural rearrangement followed by another folding trial . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
A 4 . 4 kb DNA fragment was cloned from Actinobacillus pleuropneumoniae ( strain 4074 , serotype 1 ) by genetic complementation with Escherichia coli groES groEL mutant strains . ^^^ Sequence analysis of this fragment revealed a purine nucleoside phosphorylase ( DeoD ) encoding gene homolog ( deoD ) , heat shock response encoding genes for the small ( groES ) and large subunits ( groEL ) and a partial open reading frame encoding an alcohol dehydrogenase homolog ( adhE ) . ^^^ The predicted amino acid sequence of groES and groEL genes showed extensive sequence identity ( 80 95 % ) with other Pasteurellaceae . ^^^ When expressed in E . coli , groES groEL genes were capable of complementing the growth of a lambda lytic phage , indicating a structural as well as functional conservation . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Sequence and transcriptional analysis of groES and groEL genes from the thermophilic bacterium Clostridium thermocellum . ^^^ The first ORF encoded a 94 aa 10 . 6 kDa GroES homologue ; the second encoded a 541 aa polypeptide of 57 . 6 kDa , that exhibited 61 % and 77 % sequence identity with GroEL from Escherichia coli ( Ec ) and Clostridium acetobutylicum ( Ca ) , respectively . ^^^ The first nt of the groES translational start codon was preceded ( 7 nt ) by a putative RBS ( AGGAGG ) ; a second RBS sequence was located 8 nt upstream of the groEL start . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Some spots were identified by N terminal microsequencing as proteins whose sequences had been reported previously from Brucella , such as three heat shock proteins , namely DnaK , GroEL and GroES ; bacterioferritin ; Cu Zn superoxide dismutase ; and the 50S ribosomal protein L7 / L12 . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
We have analyzed the folding of barnase in the presence of GroEL , GroES and various nucleotides to probe the importance of footballs . ^^^ Higher concentrations of GroES in the presence of ATP or AMP PNP , but not ADP , produce a proportion of a fast folding state , rising to 50 % at a GroES 7 : GroEL 14 stoichiometry of > or = 2 : 1 . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The conformational changes that the GroEL oligomer undergoes upon nucleotide and cochaperonin GroES binding have been studied using electron microscopy and image processing techniques . ^^^ Average side views of the three allosteric states ( TT , TR , and RR , which correspond to none , one , or both of the two heptameric rings of the GroEL oligomer occupied by nucleotide , respectively ) of GroEL and GroEL GroES complexes for ADP , ATP , and two nonhydrolyzable analogs ( AMP PNP and ATP gamma S ) have been obtained at 20 25 A resolution . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Symmetric GroEL GroES complexes can contain substrate simultaneously in both GroEL rings . ^^^ Incubation of rhodanese with hche aperonins GroEL and GroES ( 1 : 2 GroEL 14 : GroES 7 molar ratio ) under functional and steady state conditions for ATP leads to the formation of a high proportion of rhodanese bound symmetric complexes ( GroEL 14 ( GroES 7 ) 2 ) , as revealed by native electrophoresis . ^^^ These results also suggest that symmetric GroEL GroES complexes can use both rings simultaneously for folding , probably increasing the efficiency of the reaction . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Interaction with GroES and ATP hydrolysis are required for the release of the polypeptide chain from GroEL and further acquisition of the completely folded , native conformation . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
In contrast to the temperature sensitive for folding coat protein mutants which can be rescued at nonpermissive temperatures in vivo by the overproduction of molecular chaperones GroEL and GroES [ Gordon , C . ^^^ Chem . 269 , 27941 27951 ] , the folding defects associated with the cold sensitive amino acid substitutions were not recognized by GroEL and GroES . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
In addition , we have identified groES and groEL genes next to the thdF gene . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Architecture of GroEL and GroES and the reaction pathway A . ^^^ Reaction pathway of GroEL GroES mediated folding 2 . ^^^ GroEL GroES polypeptide ternary complexes the folding active cis complex A . ^^^ Release of nonnative polypeptides during the GroEL GroES reaction G . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Mitochondrial malate dehydrogenase ( mMDH ) folds more rapidly in the presence of GroEL , GroES and ATP than it does unassisted . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Nucleotide dependent complex formation between the Escherichia coli chaperonins GroEL and GroES studied under equilibrium conditions . ^^^ Binding of heptameric GroES to the tetradecameric chaperonin GroEL in the absence or presence of nucleotides was investigated by analytical ultracentrifugation . ^^^ In the absence of nucleotides , the association constant for the binding of GroES to GroEL , K 1 , was found to be approximately equal to 3 10 10 ( 5 ) M ( 1 ) . ^^^ The binding of a second GroES heptamer with only one fourth the affinity of the first one can be neglected at subequimolecular concentrations relative to GroEL . ^^^ With increasing GroES : GroEL ratios in the presence of 1 mM ATP analogue , up to two GroES oligomers were bound to one GroEL oligomer , forming the symmetrical `` American football ' ' shaped complex with apparently high affinity for the first GroES ring and considerably lower for the second one . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Upstream of groEL is a homolog of groES and the divergently transcribed frpB gene . ^^^ Northern hybridization demonstrated that synthesis of a full length groES groEL transcript was induced in heat stressed cells . ^^^ These experiments also revealed the presence of a shorter groES specific transcript , apparently the result of the premature termination of transcription at an IR situated between the groES and groEL genes . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
How GroES regulates binding of nonnative protein to GroEL . ^^^ In addition to this , binding of nucleotide to one GroEL ring is strongly favored by GroES binding to the other ring . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
GroES binding regulates GroEL chaperonin activity under heat shock . ^^^ Chaperonins GroEL 14 and GroES 7 are heat shock proteins implicated in the molecular response to stress . ^^^ After heat shock , GroES 7 rebinding to GroEL 14 and GroEL14GroES7 particles correlated with the restoration of optimal protein folding / release activity . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
These deduced amino acid sequences were homologous to those of the GroES and GroEL heat shock proteins ( HSP ) of other bacteria , respectively . ^^^ Phylogenetic trees based on GroES and GroEL homologs of several bacteria including E . sennetsu showed a relationship similar to that based on 16S rRNA gene sequences . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
When folding was resumed by 10 microM ATP ( 1 . 4 mol / mol GroEL subunit ) , about 60 % of GFP recovered native structure , and one half of them ( 30 % ) was found to be still bound to GroEL / ES , indicating the occurrence of folding in the central cavity of the GroEL ring underneath GroES ( cis folding ) . ^^^ The GroEL / ES bound native GFP was observed only when both GroES and ATP ( but not ADP ) were present in the folding mixture . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Induction of heat shock proteins DnaK , GroEL , and GroES by salt stress in Lactococcus lactis . ^^^ After two dimensional separation of proteins , the DnaK , GroEL , and GroES heat shock proteins , the HrcA ( Orf 1 ) heat shock repressor , and the glycolytic enzymes pyruvate kinase , glyceral dehyde 3 phosphate dehydrogenase , and phosphoglycerate kinase were identified by a combination of Western blotting and direct N terminal amino acid sequencing of proteins from the gels . ^^^ GroEL and GroES , which also belong to this group , maintained a high rate of synthesis after 15 min . ^^^ DnaK , GroEL , and GroES showed similar temporal patterns of induction during salt stress , resembling the timing during heat stress although at a lower induction level . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
These data show that productive folding of GroEL bound proteins can occur in the absence of nucleotides or the co chaperonin GroES and suggest that transient complex formation may be the functional role of GroEL under normal conditions . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
A new model of the GroEL / GroES complex architecture . ^^^ A new model of the GroEL / GroES complex architecture is proposed using structural data on the GroEL and GroES chaperonins . ^^^ The known models of the chaperonin complex structure suggest that it is formed by binding of a dome like GroES oligomer to the end orifice of the GroEL cylinder via long mobile loops of its base . ^^^ According to the new model , to form the complex two GroES oligomers one by one enter with their roofing , i . e . , in an inverted way , into the GroEL cylinder and orifices and lock them . ^^^ An active GroEL / GroES complex resembles a hollow cylinder with end orifices . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
GroES promotes the T to R transition of the GroEL ring distal to GroES in the GroEL GroES complex . ^^^ Curves of initial rates of ATP hydrolysis by GroEL as a function of ATP concentration , in the presence of fixed concentrations of GroES , were found to deviate from sigmoidal kinetics . ^^^ The data were fitted to a fractional saturation equation for ATP binding to GroEL based on a partition function that includes both GroES and ATP liganded states of GroEL . ^^^ Using this equation , it was possible to estimate in a reliable manner the value of the allosteric constant , L 2 ' , for the transition of the ring distal to GroES in the GroEL GroES complex from the low ( T ) to the high ( R ) affinity state for ATP . ^^^ Comparison of these values shows that GroES promotes the T to R transition of the ring distal to GroES in the GroEL GroES complex . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Stable expression and rapid purification of Escherichia coli GroEL and GroES chaperonins . ^^^ McKenney , 1989 , Nucleic Acids Res . 17 , 10473 10488 ) , originally developed for the cloning and expression of lethal genes , was used for cloning and hyperexpression of GroEL and GroES genes . ^^^ GroES was found to be a heat stable protein while GroEL was not . ^^^ Both GroE chaperonins were purified in a single chromatographic step with a yield of about 100 mg GroEL and 25 mg GroES per liter of E . coli culture . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
This mutant is able to inhibit the ATPase activity of GroEL to levels comparable to wild type GroES . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Stable expression of the alphaG116R ETF required coexpression of the chaperonins , GroEL and GroES . alphaG116R ETF folds into a conformation different from the wild type , and is catalytically inactive in crude extracts . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The kinetics of the chaperonin system of Escherichia coli GroEL and GroES were analyzed as a model using this system and found to be very similar to those obtained with covalently immobilized ligands . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
La cage aux fold : asymmetry in the crystal structure of GroEL GroES ( ADP ) 7 . ^^^ The structure of the molecular chaperone GroEL from Escherichia coli in complex with GroES and seven ADP molecules has recently been reported to 3 A resolution . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The groE like operon , encoding the two chaperonins groES and GroEL like proteins of the endocytobiotes , was sequenced . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The chaperonin GroEL consists of a double ring structure that assists protein folding in the presence of GroES and ATP . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Soluble secreted proteins ( MPB 64 and proteins of the antigen 85 complex ) and three heat shock proteins ( DnaK , GroEL , and GroES ) were recovered in a single peak after gel filtration , indicating their occurrence as a free monomer in the culture fluid and cytosol , respectively . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Genes encoding 10914 Da and 58267 Da polypeptides homologous to groES and groEL of Escherichia coli were cloned and sequenced from a thermophilic cyanobacterium , Synechococcus vulcanus . ^^^ The deduced amino acid sequence of the GroEL protein was much more homologous to GroELs of other cyanobacteria which accompany GroES than another GroEL homolog of S . vulcanus ( GroEL 2 ) reported previously ( M . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Interaction requires Mg ions , whereas MgATP inhibits , and inhibition is stronger in the presence of co chaperonin GroES . `` Heat shock ' ' of the membrane at 45 degrees C destroys irreversibly its ability to bind GroEL . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
By using a new method based on interactions of GroEL with octyl Sepharose , it was demonstrated that Zn2+ binding strengthens GroEL hydrophobic binding interactions and increases the efficiency of substrate release upon the addition of MgATP and GroES . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
We investigated whether Helicobacter pylori cells actively secrete proteins such as the urease subunits UreA and UreB and the GroES and GroEL homologs HspA and HspB or whether these proteins were present in the extracellular compartment as a consequence of autolysis . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Conditions for nucleotide dependent GroES GroEL interactions . ^^^ GroEL 14 ( groES 7 ) 2 is favored by an asymmetric distribution of nucleotides . ^^^ A still unresolved question regarding the mechanism of chaperonin assisted protein folding involves the stoichiometry of the GroEL GroES complex . ^^^ This is important , because the activities of the Escherichia coli chaperonin GroEL are modulated by the cochaperonin GroES . ^^^ In this report , the binding of GroES to highly purified GroEL in the presence of ATP , ADP , and the nonhydrolyzable ATP analogue , 5 ' adenylyl beta , gamma imidodiphosphate ( AMP PNP ) , was investigated by using the fluorescence anisotropy of succinimidyl 1 pyrenebutyrate labeled GroES . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
At 37 degrees C , GroES binding is restored to normal levels , and the modified GroEL regains its chaperone activity to some extent . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The chaperonin GroEL and its cofactor GroES facilitate protein folding in an ATP regulated manner . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
In this chapter , we have shown how chemical cross linking with a bifunctional reagent , GA , can be used to investigate the structure of large oligomeric complexes such as GroEL14GroES7 and GroEL 14 ( GroES 7 ) 2 . ^^^ Cross linking , followed by denaturing electrophoresis , confirmed the number and arrangement of GroEL and GroES subunits within each individual oligomer , which was previously known from EM analysis . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Recently , we found that bacterial chaperonins GroEL and GroES promote folding and assembly of E 1 decarboxylase component of the BCKD complex in Escherichia coli . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The chaperones GroEL and GroES from Escherichia coli are known to improve in vitro protein refolding yields . ^^^ We show that , for the molecular chaperone assisted refolding of hen egg white lysozyme , GroES is not an essential requirement and that activity is recovered with GroEL and ATP alone . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Protein folding assisted by the GroEL / GroES chaperonin system . ^^^ The chaperonin system GroEL / GroES assists in the folding of proteins in the bacterial cytosol . ^^^ Recent applications of biophysical techniques for the structural analysis of GroEL , GroES , and chaperonin bound protein folding intermediates have provided the basis for understanding the molecular mechanism of GroEL / GroES action . ^^^ Premature release of unfolded protein into external solution is prevented by binding of the cofactor GroES on top of the GroEL cylinder , resulting in an enclosed cage . ^^^ Upon ATP dependent dissociation of GroES , substrate protein is eventually released from GroEL in a native or native like conformation . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
In the absence of GroES , GroEL captured IFN gamma in a folding competent complex . ^^^ Only in the presence of GroES , did ATP induce complete discharge of IFN gamma from GroEL , with the released protein refolded into a conformation that is ( a ) immunoreactive / bio active , ( b ) resistant to precipitation and ( c ) in a dimeric configuration . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Cloning and sequencing of a gene coding for the GroEL homolog suggested that the protein is 55 . 2 % identical to GroEL of E . coli at the amino acid sequence level , and that the gene is preceded by an open reading frame which encodes a protein 39 . 6 % identical to GroES of E . coli . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Assembly of both the head and tail of bacteriophage Mu is blocked in Escherichia coli groEL and groES mutants . ^^^ GroEL and GroES are thus essential for the correct assembly of both Mu heads and Mu tails . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The folding and assembly of Escherichia coli dodecameric glutamine synthetase is facilitated by the E . coli GroE chaperonins , GroEL and GroES . ^^^ Although nucleotide binding is sufficient to dissociate assembly competent glutamine synthetase monomers from GroEL , the addition of GroES substantially accelerates the dissociation , assembly , and reactivation . ^^^ Interestingly , the more physiologically relevant `` low affinity ' ' nucleotide bound ( ( ATP / ADP ) GroEL GroES ) complex is not as efficient at capturing the initial folding intermediates of glutamine synthetase . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Protein encoded by gene 31 completely substitutes co chaperonin GroES of the host cell in folding of the major capsid protein , gp 23 , aided by chaperonin GroEL . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
When GroES is bound to the GroEL : ATP complex and the system is quenched in the same way , approximately half of the bound ATP undergoes hydrolysis on the chaperonin complex showing that the co protein increases the degree of commitment . ^^^ Thus , non competitive inhibition of ATP hydrolysis , combined with the ability of the co protein to block ligand exchange between rings has the effect of imposing a reciprocating cycle of reactions with ATP hydrolysing , and GroES binding , on each of the GroEL rings in turn . ^^^ Taken together , these data imply that the dominant , productive steady state reaction in vivo is : GroEL : ATP : GroES > GroEL : ADP : GroES > ATP : GroEL : ADP : GroES > ATP : GroEL : ADP > GroES : ATP : GroEL : ADP > GroES : ATP : GroEL for a hemi cycle , and that significant inhibi tion of hydrolysis may arise through the formation of a dead end ADP : GroEL : ATP : GroES complex . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Chaperone coexpression plasmids : differential and synergistic roles of DnaK DnaJ GrpE and GroEL GroES in assisting folding of an allergen of Japanese cedar pollen , Cryj 2 , in Escherichia coli . ^^^ Plasmids that can be used for controlled expression of the DnaK DnaJ GrpE and / or GroEL GroES chaperone team were constructed in order to facilitate assessment of the effects of these chaperone teams on folding or assembly or recombinant proteins in Escherichia coli . ^^^ A typical pACYC 184 based plasmid which was obtained could express the major DnaK DnaJ GrpE and GroEL GroES chaperone teams from separate promoters when L arabinose and tetracycline , respectively , were added in a dose dependent fashion . ^^^ Coexpression of the DnaK DnaJ GrpE and / or GroEL GroES chaperone team at appropriate levels resulted in marked stabilization and accumulation of Cryj 2 without extensive aggregation . ^^^ Experiments performed with mutants that lack each of the chaperone proteins ( DnaK , DnaJ , GrpE , GroEL , and GroES ) or heat shock transcription factor sigma 32 revealed that both chaperone teams are critically involved in Cryj 2 folding but that they are involved in distinct ways . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The ampicillin resistance of the low resistance FecR ' BlaM hybrids was increased 2 to 10 fold by cosynthesis of plasmid encoded GroEL GroES and SecB chaperones and in degP and ompT protease mutants , which suggested that the decreased ampicillin resistance level of these hybrids was caused by the formation of inclusion bodies and proteolytic degradation . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Here we demonstrate that an increase in the cellular concentration of GroEL and GroES proteins is not in itself sufficient to cause RC disassembly . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Structural changes of the Escherichia coli GroEL GroES chaperonins upon complex formation in solution : a neutron small angle scattering study . ^^^ We applied neutron scattering in conjunction with deuterium ( D ) labeling in order to obtain information about the domain structure of GroEL and GroES isolated and in the complex . ^^^ Neutron scattering shows that both regions change their conformation upon GroEL / GroES complex formation . ^^^ Upon complex formation the apical domains of GroEL move outwards , which facilitates binding of GroES at a Gro EL GroES center to center distance of ( 87 + / 8 ) A . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
To study the effect of human E1alpha missense mutations on E 1 subunit assembly , we have developed a pulse chase labeling protocol based on efficient expression and assembly of human ( His ) 6 E1alpha and untagged E1beta subunits in Escherichia coli in the presence of overexpressed chaperonins GroEL and GroES . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Genetic and biochemical work has highlighted the biological importance of the GroEL / GroES ( Hsp60 / Hsp10 ; cpn60 / cpn10 ) chaperone machine in protein folding . ^^^ The recent determination of the GroES and GroEL / GroES structures provides a glimpse of their plasticity , revealing dramatic conformational changes that point to an elaborate mechanism , coupling ATP hydrolysis to substrate release by GroEL . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Homology searches indicated that the 55 kDa antigen and the 10 kDa protein were homologues of E . coli GroEL and GroES proteins , respectively . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Northern hybridization and S 1 nuclease mapping demonstrated that the groES and groEL genes in Pseudomonas aeruginosa were transcribed as a bicistronic mRNA of 2 . 2 kb . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The thermally inactivated protein can be released from GroEL in an active form by the addition of chaperonin 10 from E . coli ( GroES ) / ATP , showing that inactivation is not the result of irreversible chemical changes . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Cloning of the groE operon of the marine bacterium Vibrio harveyi using a lambda vector . groES and groEL genes encode two co operating proteins GroES and GroEL , belonging to a class of chaperone proteins highly conserved during evolution . ^^^ In order to clone the groEL and groES genes of the marine bacterium Vibrio harveyi , we constructed the 5 . harveyi genomic library in the lambdaEMBL 1 vector , and selected clones which were able to complement mutations in both groE genes of E . coli for bacteriophage lambda growth . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Fragments encompassing the apical domain of GroEL , called minichaperones , facilitate the refolding of several proteins in vitro without requiring GroES , ATP , or the cage like structure of multimeric GroEL . ^^^ The complex quaternary structure of GroEL , its central cavity , and the structural allosteric changes that take place on the binding of nucleotides and GroES are not essential for all of its functions in vivo . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
In contrast to trimethoprim , sulfamethoxazole triggered the increased synthesis of the heat shock proteins DnaK , GroEL , and GroES . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Major , asymmetric conformational changes in the GroEL double toroid accompany binding of ATP and the cochaperonin GroES . ^^^ When a nonnative polypeptide , bound to one of the GroEL rings , is encapsulated by GroES to form a cis ternary complex , these changes drive the polypeptide into the sequestered cavity and initiate its folding . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
GroEL and GroES control of substrate flux in the in vivo folding pathway of phage P 22 coat protein . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Protein homology searches showed that the first two ORFs encoded homologs to the universally conserved heat shock proteins GroES and GroEL . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Chaperonins GroEL and GroES were also able to prevent aggregation but only in the presence of ATP . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
GroEL GroES mediated protein folding requires an intact central cavity . ^^^ The chaperonin GroEL is an oligomeric double ring structure that , together with the cochaperonin GroES , assists protein folding . ^^^ Biochemical analyses indicate that folding occurs in a cis ternary complex in which substrate is sequestered within the GroEL central cavity underneath GroES . ^^^ Recently , however , studies of GroEL `` minichaperones ' ' containing only the apical substrate binding subdomain have questioned the functional importance of substrate encapsulation within GroEL GroES complexes . ^^^ Here we compare directly the folding activity of minichaperones with that of the full GroEL GroES system . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The activity of GroEL bound rhodanese can be completely recovered upon addition of GroES and ATP . ^^^ However , when rhodanese was allowed to inactivate spontaneously in the absence of GroEL , no recovery of activity was observed upon addition of GroEL , GroES , and ATP . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Increased solubility of glutathione S transferase P 16 ( GST p 16 ) fusion protein by co expression of chaperones groes and groel in Escherichia coli . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The compiled data from PBMC and T cell lines tested for antigen induced proliferation and IFN gamma secretion showed that the most frequently recognized antigen was ESAT 6 , followed by MPT 59 , GroES , MPB 70 , MPT 64 , DnaK , GroEL and PstS . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Chaperonin GroEL from Escherichia coli , together with its cochaperonin GroES , are proteins involved in assisting the folding of polypeptides . ^^^ GroEL is a tetradecamer composed of two heptameric rings , which enclose a cavity where folding takes place through multiple cycles of substrate and GroES binding and release . ^^^ GroEL and GroES are also heat shock proteins , their synthesis being increased during heat shock conditions to help the cell coping with the thermal stress . ^^^ Our results suggest that , as the temperature increases , GroEL decreases its protein folding activity and starts acting as a `` protein store . ' ' The molecular basis of this behavior is the loss of inter ring signaling , which slows down GroES liberation from GroEL and therefore the release of the unfolded protein from the GroEL cavity . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Taken together our results suggest that for protection of cells against heat stress both the ability of GroEL to interact with a large variety of nonnative conformations of proteins and the active , GroES dependent refolding of highly unfolded species are important . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Purification and characterization of Chromatium vinosum GroEL and GroES proteins overexpressed in Escherichia coli cells lacking the endogenous groESL operon . ^^^ Using an Escherichia coli strain ( RF 101 ) in which the endogenous chromosomal groESL operon was removed , we overexpressed the GroEL and GroES chaperonins cloned from the photosynthetic bacterium Chromatium vinosum . ^^^ The native molecular masses of GroEL and GroES , as determined by size exclusion chromatography , were 830 and 74 kDa , respectively . ^^^ This suggests a tetradecameric structure for GroEL and a heptameric structure for GroES . ^^^ GroEL ATPase was inhibited by GroES , reaching about 50 % inhibition at a ratio GroES 7mer / GroEL 14mer of 1 in the presence of 10 mM KCl . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Phosphofructokinase interacts with molecular chaperonins GroEL and GroES . ^^^ For studying the possible interaction between the chaperonins and phosphofructokinase ( PFK ) , bacterial chaperonins GroEL , GroES , and the PFK were co purified from chaperonin over expressing , heat treated E . coli strains . ^^^ This type of GroEL PFK interaction was overcame by the GroES . ^^^ Contrary to this , in a complete refolding system containing GroEL , GroES , ATP and Mg2+ , activity of heat treated bacterial PFK gradually increased showing , that GroEL and GroES together play a role in the folding and / or assembly of PFK . ^^^ The data show that PFK can interact with GroEL , which results in binding of the enzyme ; by contrast , GroEL and GroES together has a folding effect leading ultimately to increase of the activity of the enzyme . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The bacteriophage T 4 GroES homologue , gp 31 , in conjunction with the Escherichia coli chaperonin GroEL , is both necessary and sufficient to fold the T 4 major capsid protein , gp 23 , to a state competent for capsid assembly as shown by in vivo expression studies . ^^^ Although the presence of functional GroEL gp 31 enhances folding of the mutated gp 23 in vivo , GroEL GroES has no such effect . ^^^ Given our finding that gp 31 is not required for the binding of the major capsid protein to GroEL and that active GroES is incapable of folding the gp 23 polypeptide chain to native conformation , our results suggest co chaperonin specificity in the folding of certain substrates . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Chaperone protein GrpE and the GroEL / GroES complex promote the correct folding of tobacco mosaic virus coat protein for ribonucleocapsid assembly in vivo . ^^^ Overproduction of GroEL or GroES alone had little effect . ^^^ However , co overexpression of GroEL and GroES resulted in a two fold increase in soluble TMV CP and a four fold rise in assembled TMV like ( pseudovirus ) particles in vivo . ^^^ Together , these results suggest that GrpE and the GroEL / GroES chaperone complex promote the correct folding and assembly of TMV CP into ribonucleocapsids in vivo . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
In the absence of GroES and nucleotides , the rate of GroEL mediated refolding of heat and DTT denatured mitochondrial malate dehydrogenase was extremely low , but some three times higher than the spontaneous rate . ^^^ This GroEL mediated rate was increased 17 fold by saturating concentrations of ATP , 11 fold by ADP and GroES , and 465 fold by ATP and GroES . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Previous work has shown that the GroEL GroES interaction is primarily mediated by the GroES mobile loop . ^^^ The observed patterns of genetic and biochemical interaction between GroES or Gp 31 and GroEL point to a mechanism of genetic allele specificity based on compensatory changes in affinity of the protein protein interaction . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
GroEl and GroES are two proteins ( chaperones ) which facilitate protein folding in the cell in an ATP dependent manner [ Hemmingson , Woolford , van der Vies , Tilly , Dennis , Georgopoulos , Henfrix and Ellis ( 1988 ) Nature ( London ) 333 , 330 334 ] . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
All the Escherichia coli molecular chaperones ( groEL , groES , and dnaK ) were active . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The results indicate a possible direct form of inter ring communication associated with internal fluctuations in the nucleotide binding domains upon nucleotide and GroES binding that are involved in the allosteric mechanism of GroEL . ^^^ At the level of conformational transitions in entire GroEL rings , nucleotide induced structural changes were found to be distinct and in principle uncoupled from changes occurring upon GroES binding . ^^^ However , a coupling is found between nucleotide induced conformational changes and GroES mediated transitions , but only in simulations of GroEL double rings , and not in simulations of single rings . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
GroEL / GroES : structure and function of a two stroke folding machine . ^^^ The asymmetric binding of ATP and cochaperonin GroES to GroEL triggers a major conformational change in the cis ring , creating an enlarged chamber into which the bound nonnative polypeptide is released . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The chaperonin system , GroEL and GroES of Escherichia coli enable certain proteins to fold under conditions when spontaneous folding is prohibitively slow as to compete with other non productive channels such as aggregation . ^^^ It is known that upon addition of ATP and GroES the interior cavity of GroEL offers a hydrophilic like environment to the substrate protein . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The TXAS cDNA was modified by replacing the sequence encoding the first 28 amino acid residues with a CYP 17 amino terminal sequence and by adding a polyhistidine tag sequence prior to the stop codon ; the cDNA was inserted into the pCW vector and co expressed with chaperonins groES and groEL in Escherichia coli . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Here we report a method of immobilising the chaperonins GroEL and GroES to a glass matrix . ^^^ The enzyme citrate synthetase from porcine heart demonstrates a three fold increase in activity when refolded in the presence of immobilised GroEL , ATP and free GroES . ^^^ Similar results are obtained in the presence of free GroEL , immobilised GroES and ATP . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The function of GroEL is often , though not invariably , dependent on the co chaperone , GroES , and ATP . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
GroEL GroES cycling : ATP and nonnative polypeptide direct alternation of folding active rings . ^^^ The double ring chaperonin GroEL mediates protein folding in the central cavity of a ring bound by ATP and GroES , but it is unclear how GroEL cycles from one folding active complex to the next . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Coexpression of the bacterial chaperone GroES and GroEL genes together did not help solubilize the K 11 RNA polymerase . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
GroEL / GroES dependent reconstitution of alpha 2 beta2 tetramers of humanmitochondrial branched chain alpha ketoacid decarboxylase . ^^^ In the present study , His 6 tagged E 1 alpha2 beta 2 tetramers ( 171 kDa ) denatured in 8 M urea were competently reconstituted in vitro at 23 degrees C with an absolute requirement for chaperonins GroEL / GroES and Mg ATP . ^^^ The alpha subunit was released as soluble monomers from the GroEL alpha complex alone in the presence of GroES and Mg ATP . ^^^ Dimers were regenerated from the GroEL alpha beta complex , but they needed to interact with GroEL / GroES again , thereby perpetuating the cycle until the conversion from dimers to tetramers was complete . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Mechanisms for GroEL / GroES mediated folding of a large 86 kDa fusion polypeptide in vitro . ^^^ Our understanding of mechanisms for GroEL / GroES assisted protein folding to date has been derived mostly from studies with small proteins . ^^^ Reactivation of MBP E 1 denatured in 8 M urea was absolutely dependent on GroEL / GroES and Mg2+ ATP , and exhibited strikingly slow kinetics with a rate constant of 376 M 1 s 1 , analogous to denatured untagged E 1 . ^^^ GroEL complex ( molar ratio 1 : 1 ) was incubated with GroES , the latter was capable of capping either the very ring that harbored the 48 kDa ( His ) 6 alpha polypeptide ( in cis ) or the opposite unoccupied cavity ( in trans ) . ^^^ GroEL ( 1 : 1 ) complex was capped by GroES exclusively in the trans configuration . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Two D glyceraldehyde 3 phosphate dehydrogenase ( GAPDH ) folding intermediate subunits bind with chaperonin 60 ( GroEL ) to form a stable complex , which can no longer bind with additional GAPDH intermediate subunits , but does bind with one more lysozyme folding intermediate or one chaperonin 10 ( GroES ) molecule , suggesting that the two GAPDH subunits bind at one end of the GroEL molecule displaying a `` half of the sites ' ' binding profile . ^^^ GAPDH2 bind with one GroES molecule only at the other end of the GroEL molecule forming a trans ternary complex . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
It consists of two ORFs encoding proteins with molecular masses of 9 . 5 and 57 . 9 kDa , which showed a high degree of homology to other bacterial GroES and GroEL proteins . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Under native conditions , truncated rhodanese bound to GroEL and was released and reactivated by adding ATP and GroES , suggesting equilibrium between native and non native conformers . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The molecular chaperones GroEL and GroES facilitate protein folding in an ATP dependent manner under conditions where no spontaneous folding occurs . ^^^ GroES complexes , a folding reaction takes place , generating association competent monomeric intermediates that are no longer recognized by GroEL . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
To achieve this , the cooperation of GroEL and GroES , the two protein components of the chaperone system , is an essential requirement . ^^^ In both cases , the complete GroE system ( GroEL , GroES and ATP ) compensates the deceleration of MBP Y283D folding . ^^^ Combining kinetic folding experiments and electron microscopy of GroE particles , we demonstrate that at elevated temperatures , symmetrical GroE particles with GroES bound to both ends of the GroEL cylinder play an important role in the efficient catalysis of MBP Y283D refolding . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
In the case of mature Adx , the activity was increased in the presence of either GroEL , GroES , or bovine serum albumin and the refolding of mature Adx is a nonspecific process . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The cylindrical chaperonin GroEL of E . coli and its ring shaped cofactor GroES cooperate in mediating the ATP dependent folding of a wide range of polypeptides in vivo and in vitro . ^^^ By binding to the ends of the GroEL cylinder , GroES displaces GroEL bound polypeptide into an enclosed folding cage , thereby preventing protein aggregation during folding . ^^^ The dynamic interaction of GroEL and GroES is regulated by the GroEL ATPase and involves the formation of asymmetrical GroEL : GroES 1 and symmetrical GroEL : GroES 2 complexes . ^^^ It has also been suggested that the formation of GroEL : GroES 2 complexes allows the folding of two polypeptide molecules per GroEL reaction cycle , one in each ring of GroEL . ^^^ By making use of a procedure to stabilize chaperonin complexes by rapid crosslinking for subsequent analysis by native PAGE , we have quantified the occurrence of GroEL : GroES 1 and GroEL : GroES 2 complexes in active refolding reactions under a variety of conditions using mitochondrial malate dehydrogenase ( mMDH ) as a substrate . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The 2 , 253 bp groESL fragment contained three putative open reading frames , two of which encoded the ubiquitous GroES and GroEL chaperone proteins . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The observed variations in sulfhydryl accessibility are consistent with mechanisms that suggest binding of GroES to GroEL differs from the binding of substrate protein to GroEL , and that the binding of Mg2+ or Mg adenine nucleotides results in conformational changes in GroEL . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
This conformational change then leads to the discharge of GroES from GroEL , enabling polypeptide release . ^^^ Single ring forms of GroEL are thus predicted to be unable to chaperone the folding of GroES dependent substrates efficiently , since they are unable to discharge the bound GroES and unable to release folded protein . ^^^ We demonstrate that whereas the double ring form of the GroEL chimera functions effectively in refolding of a GroES dependent substrate , the single ring form does not . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
On the maximum size of proteins to stay and fold in the cavity of GroEL underneath GroES . ^^^ GroEL encapsulates non native protein in a folding cage underneath GroES ( cis cavity ) . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Eighteen amino acid substitutions have been identified in bacteriophage P 22 coat protein that are defective in folding and cause their folding intermediates to be substrates for GroEL and GroES . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The heptameric Gp 31 cochaperonin , like the E . coli GroES cochaperonin , interacts with GroEL primarily through its unstructured mobile loop segment . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The refolding of GroES protein from 3 M Gdn HCl was probed functionally by measuring the extent of inhibition of GroEL ATPase activity and the enhancement of lactate dehydrogenase refolding yields in the presence of GroEL and ADP . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The first ORF encoded a polypeptide of 97 amino acids , GroES homologue , and the second ORF encoded a polypeptide of 544 amino acids , GroEL homologue . ^^^ A comparison of the deduced amino acid sequences revealed that the primary structures of the 5 . cholerae GroES and GroEL proteins showed significant homology with those of the GroES and GroEL proteins of other bacteria . ^^^ The results showed that the groES and groEL from 5 . cholerae were expressed in E . coli , and groE mutants harboring 5 . cholerae groESL genes regained growth ability at high temperature . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Thus , an important function of GroES in the regulation of the activity of GroEL for substrates is to displace the bound substrate by competing for its binding site . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
We have studied how nucleotides ( ADP , AMP PNP , and ATP ) and the co chaperonin GroES influence the GroEL affected refolding of apo alpha lactalbumin . ^^^ When GroES was absent , the interaction between GroEL and alpha lactalbumin could be well represented by a `` cooperative binding ' ' model in which GroEL has two binding sites for alpha lactalbumin with the affinity of the second site being tenfold weaker than that of the first , so that there is negative cooperativity between the two sites . ^^^ When GroES was present , ATP as well as ADP and AMP PNP were effective in reducing the affinity between GroEL and the refolding intermediate of alpha lactalbumin . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The chaperonin GroEL is a double toriodal assembly that with its cochaperonin GroES facilitates protein folding with an ATP dependent mechanism . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
GroEL / GroES promote dissociation / reassociation cycles of a heterodimeric intermediate during alpha ( 2 ) beta ( 2 ) protein assembly . ^^^ Whereas the mechanism of GroEL / GroES mediated protein folding has been extensively studied , the role of these chaperonins in oligomeric protein assembly remains poorly understood . ^^^ Dilution of the denaturant resulted in a rapid recovery of BCKD independent of the chaperonins GroEL / GroES . ^^^ Mixing experiments with radiolabeled and unlabeled protein substrates provided direct evidence that GroEL / GroES promote dissociation and subunit exchange between bad heterodimers . ^^^ Our data support the thesis that chaperonins GroEL / GroES mediate iterative annealing of nonproductive assembly intermediates at the quaternary structure level . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
In vitro reconstitution of active ribulose bisphosphate carboxylase ( Rubisco ) from unfolded polypeptides is facilitated by the molecular chaperones : chaperonin 60 from Escherichia coli ( groEL ) , yeast mitochondria ( hsp 60 ) or chloroplasts ( Rubisco sub unit binding protein ) , together with chaperonin 10 from E . coli ( groES ) , and Mg ATP . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
This kinetic behaviour is consistent with the GroEL ring passing through distinct functional states in a binding encapsulation folding process , with the T form having high substrate affinity ( binding ) , the R form being able to bind GroES but retaining substrate affinity ( encapsulation ) , and the R * form retaining high GroES affinity but allowing the substrate to dissociate into the enclosed cavity ( folding ) . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The rapid degradation of the abnormal fusion protein CRAG in Escherichia coli requires the molecular chaperones GroEL , GroES , and trigger factor and proceeds through the formation of a CRAG GroEL trigger factor complex . ^^^ Dissociation of CRAG from GroEL was necessary for its digestion by the ClpP protease , because in a groES temperature sensitive mutant , CRAG was stable and accumulated on GroEL . ^^^ Therefore , we suggest that CRAG degradation proceeds through multiple rounds of substrate binding to GroEL , followed by their GroES dependent dissociation , which allows further digestion by the protease . ^^^ In this multistep process , GroEL and GroES function repeatedly , apparently to allow further degradation of CRAG and its fragments by the protease . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The affinity of the GroEL / GroES complex for peptides under conditions of protein folding . ^^^ The affinity of four short peptides for the Escherichia coli molecular chaperone GroEL was studied in the presence of the co chaperone GroES and nucleotides . ^^^ Our data show that binding of GroES to one ring enhances the interaction of the peptides with the opposite GroEL ring , a finding that was related to the structural readjustments in GroEL following GroES binding . ^^^ We further report that the GroEL / GroES complex has a high affinity for peptides during ATP hydrolysis when protein substrates would undergo repeated cycles of assisted folding . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Third , and most importantly , CsaA exhibited chaperone like properties by stimulating the reactivation of heat denatured firefly luciferase in groEL , groES , dnaK and grpE mutant strains of E . coli , and by preventing the aggregation of heat denatured luciferase in vitro . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Hydrophilic residues at the apical domain of GroEL contribute to GroES binding but attenuate polypeptide binding . ^^^ The GroES binding site at the apical domain of GroEL , mostly consisting of hydrophobic residues , overlaps largely with the substrate polypeptide binding site . ^^^ Essential contribution of hydrophobic interaction to the binding of both GroES and polypeptide was exemplified by the mutant GroEL ( L237Q ) which lost the ability to bind either of them . ^^^ For GroES binding , N 265 is essential since GroEL ( N265A ) is unable to bind GroES . ^^^ E 238 contributes to rapid GroES binding to GroEL because GroEL ( E238A ) is extremely sluggish in GroES binding . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Herein , the relationship between cooperative ATP binding by GroEL and the kinetics of GroE assisted folding of two substrates with different GroES dependence , mouse dihydrofolate reductase ( mDHFR ) and mitochondrial malate dehydrogenase , is examined by using cooperativity mutants of GroEL . ^^^ Inter ring negative cooperativity in ATP binding by GroEL is found to affect the kinetic partitioning of mDHFR , but not of mitochondrial malate dehydrogenase , between folding in solution and folding in the cavity underneath GroES . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The chaperonin GroEL binds nonnative substrate protein in the central cavity of an open ring through exposed hydrophobic residues at the inside aspect of the apical domains and then mediates productive folding upon binding ATP and the cochaperonin GroES . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Pyruvate dehydrogenase kinase ( PDK ) isoforms 2 and 3 were produced via co expression with the chaperonins GroEL and GroES and purified with high specific activities in affinity tag free forms . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Interactions of GroEL / GroES with a heterodimeric intermediate during alpha 2beta 2 assembly of mitochondrial branched chain alpha ketoacid dehydrogenase . cis capping of the native like 86 kDa intermediate by GroES . ^^^ We showed previously that the interaction of an alphabeta heterodimeric intermediate with GroEL / GroES is essential for efficient alpha ( 2 ) beta ( 2 ) assembly of human mitochondrial branched chain alpha ketoacid dehydrogenase . ^^^ Surprisingly , in the presence of Mg ADP , GroES was able to cap the GroEL alphabeta complex in cis , despite the size of 86 kDa of the heterodimer ( with a His ( 6 ) tag and a linker ) . ^^^ Incubation of the GroEL alphabeta complex with Mg ATP and GroES resulted in dissociation and discharge of both the alpha and beta subunits from GroEL . ^^^ The beta subunit upon binding to GroEL underwent further folding in the cis cavity sequestered by GroES . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
GroES consists of seven identical 10 kDa subunits and is involved in assisting protein folding as the partner of another oligomeric protein , the GroEL chaperonin . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Major HSPs are molecular chaperones , including DnaK , DnaJ and GrpE , and GroEL and GroES , and proteases . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Trigger factor expressed in Escherichia coli confirms its additional chaperone functions , as shown by its association with chaperones GroEL and GroES after induction of misfolding . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
When the E . coli chaperone genes GroEL , GroES , DnaK , DnaJ and GrpE were coexpressed with manganese catalase , a significant fraction of the overproduced protein was partitioned into the soluble fraction . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
In an effort to develop genetically engineered Brucella abortus ( BA ) vaccines , the genes encoding heat shock proteins ( HSPs ) GroEL , GroES , and HtrA were cloned and expressed in the BAC TO BAC Baculovirus System , and the kinetics of protein expression were analyzed using various insect cell lines in suspension cultures , different cell densities in suspension cultures , multiplicities of infection and recombinant virus replication times . ^^^ Under these conditions BA recombinant HSPs were expressed as follows : GroEL at 16 % of the total cellular proteins ( 105microg / ml concentration ) ; GroES 2 % ( 15 . 25microg / ml ) ; and HtrA 8 % ( 84 . 48microg / ml ) . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The genes groES and groEL were transcribed as one strongly heat inducible bicistronic mRNA which exhibited exactly the same induction kinetic as the dnaK operon . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Functional regions inferred from mutation studies and the Escherichia coli GroEL 3D crystal complexes are evaluated in a multiple alignment across 43 diverse HSP 60 sequences , centering on ATP / ADP and Mg2+ binding sites , on residues interacting with substrate , on GroES contact positions , on interface regions between monomers and domains , and on residues important in allosteric conformational changes . ^^^ A large number of charged residues line the central cavity of the GroEL GroES complex in the substrate releasing conformation . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Furthermore , GroEL requires a cofactor ( GroES ) that is not present in the type 2 chaperonins . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Escherichia coli molecular chaperone GroEL and co chaperone GroES are well known to assist the folding / refolding of a diverse range of substrate proteins . ^^^ Despite this , there have been relatively few reports of the GroEL / GroES molecular chaperone system being used as a biotechnology tool for protein folding / refolding . ^^^ In this paper , a solution phase protein folding bioreactor is described that involves the complete GroEL / GroES system . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
We determined the N terminal amino acid sequence of three highly induced proteins ; comparing these proteins to databases we identified them to be the well known heat shock proteins GroES , GroEL , and DnaK . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
De novo synthesis of the 10 and 60 kDa heat shock proteins ( GroES and GroEL ) was considerably lower ( 0 . 04 and 0 . 9 % of total label , respectively ) , indicating only low levels of stress . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The molecular chaperones GroEL and GroES were expressed in recombinant E . coli and purified by anion exchange chromatography . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Expression of E 1 component of human branched chain alpha keto acid dehydrogenase complex in Escherichia coli by cotransformation with chaperonins GroEL and GroES . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Some highly conserved eubacterial enzymes appear not to be encoded by U . urealyticum , including the cell division protein FtsZ , chaperonins GroES and GroEL , and ribonucleoside diphosphate reductase . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The folding of nascent mitochondrial aspartate aminotransferase synthesized in a cell free extract can be assisted by GroEL and GroES . ^^^ However , it refolds rapidly and in good yield in the presence of the intramitochondrial chaperone homologues GroEL and GroES . ^^^ In this report , we demonstrate that GroEL and GroES can also facilitate the folding of nascent pmAspAT in reticulocyte lysate under conditions where it otherwise would not . ^^^ The GroEL trapped species appear to be among the productive pmAspAT folding intermediates formed in RRL or they at least appear to equilibrate with these intermediates , since they become import competent after GroES stimulated release from GroEL . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
High hydrostatic pressure can probe the effects of functionally related ligands on the quaternary structures of the chaperonins GroEL and GroES . ^^^ We investigated the effects of high hydrostatic pressure in the range of 1 3 kilobars on tetradecameric GroEL , heptameric GroES , and the GroEL GroES complex . ^^^ Pressure versus time profiles and kinetics of the dissociation of both GroEL and GroES at fixed pressures were monitored by light scattering . ^^^ Unlike GroEL , GroES monomers do reassociate readily . ^^^ Interestingly , the GroEL GroES complex is very stable in the range of 1 2 . 5 kilobars . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Early genetic studies identified the Escherichia coli groES and groEL genes because mutations in them blocked the growth of bacteriophages lambda and T 4 . ^^^ Subsequent genetic and biochemical analyses have shown that GroES and GroEL constitute a chaperonin machine , absolutely essential for E . coli growth , because it is needed for the correct folding of many of its proteins . ^^^ In spite of very little sequence identity to GroES , the bacteriophage T 4 encoded Gp 31 protein and the bacteriophage RB 49 encoded CocO protein are bona fide GroEL cochaperonins , even capable of substituting for GroES in E . coli growth . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Pseudo T even bacteriophage RB 49 encodes CocO , a cochaperonin for GroEL , which can substitute for Escherichia coli ' s GroES and Bacteriophage T 4 ' s Gp 31 . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Three heat shock proteins , GroEL , GroES , and DnaK , were significantly up regulated in PHB accumulating cells . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The heptameric Gp 31 co chaperonin from bacteriophage T 4 , an analogue of GroES , was used as a scaffold to display the GroEL minichaperones . ^^^ Although single minichaperones ( residues 193 335 to 191 376 of GroEL ) have certain chaperone activities in vitro and in vivo , they can not refold heat and dithiothreitol denatured mitochondrial malate dehydrogenase ( mtMDH ) , a reaction that normally requires GroEL , its co chaperonin GroES and ATP . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
We found that the mutation E191G , which is responsible for the temperature sensitive ( ts ) Escherichia coli allele groEL 44 and is located in the hinge region between the intermediate and apical domains of GroEL , appears to function by weakening the binding of GroES , without destabilizing the overall structure of GroEL 44 mutant . ^^^ We introduced , therefore , the mutation E191G into GroEL ( SR 1 ) in order to generate a single ring mutant that may have weaker binding of GroES and hence be active . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Accompanying binding of ATP and GroES to one ring of GroEL , that ring undergoes a large en bloc domain movement , in which the apical domain twists upward and outward . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The possibility that GroEL can remove non native proteins from kinetic traps by unfolding them either during polypeptide binding to the chaperonin or during the subsequent ATP dependent formation of folding active complexes with the co chaperonin GroES has also been explored . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
In growth above pH 7 , three stress proteins were induced : GroES ( HspA ) , GroEL ( HspB ) , and the antioxidant AhpC homolog TsaA . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The amount of the expressed GroEL and GroES protein were about 40 % and 15 % of the total cellular proteins , respectively . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
One of the proposed roles of the GroEL GroES cavity is to provide an `` infinite dilution ' ' folding chamber where protein substrate can fold avoiding deleterious off pathway aggregation . ^^^ Surprisingly , under these `` nonpermissive ' ' folding conditions , GS can reactivate with GroEL and ATP alone and does not require the encapsulation by GroES . ^^^ Our data also suggest that the GroEL GroES encapsulated environment is not required under all nonpermissive folding conditions . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The chaperonins GroEL and GroES were shown to facilitate the refolding of urea unfolded rhodanese in an ATP dependent process at 25 or 37 degrees C . ^^^ At low temperature , GroEL retains its ability to form a complex with urea unfolded rhodanese or with GroES . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
MgATP alone can increase the rate of GroEL assisted reactivation of cAAT , yet the presence of GroES is mandatory for mAAT . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Chemical reconstitution of recombinant bovine adrenal mitochondrial apoadrenodoxin was carried out in the presence of the nonhomologous chaperone protein GroEL and of the cochaperone GroES , both in the presence and in the absence of ATP . ^^^ GroES and ATP had no effect by themselves , and did not enhance the effect of GroEL . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Among the up regulated polypeptides , a biotin carboxyl carrier protein and enzymes involved in DNA synthesis and repair were identified during the early stress response , while the universal chaperonins GroEL and GroES corresponded to a later response . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
We describe a conceptual framework for understanding how the GroEL GroES system assists misfolded proteins to reach their native states . ^^^ A key idea in our framework is that , with coordinated ATP hydrolysis and GroES binding , GroEL participates actively by repeatedly unfolding the substrate protein ( SP ) , provided that it is trapped in one of the misfolded states . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
We have sequenced the operon encoding the major heat shock proteins GroES and GroEL in the gram positive food borne pathogen Listeria monocytogenes . ^^^ The operon has a conserved orientation in the order groES groEL . ^^^ Upstream of groES and in the opposite orientation is a gene encoding a homologue of the Bacillus subtilis protein YdiL , while downstream of groEL is a gene encoding a putative bile hydrolase . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Application of fluorescence resonance energy transfer to the GroEL GroES chaperonin reaction . ^^^ Here it is applied to the GroEL GroES chaperonin system to examine the ATP driven dynamics that underlie protein folding by this chaperone . ^^^ Relying on the known structures of GroEL and GroES , sites for attachment of fluorescent probes are designed into the sequence of both proteins . ^^^ Because these sites are brought close in space when GroEL and GroES form a complex , excitation energy can pass from a donor to an acceptor chromophore by FRET . ^^^ While in ideal circumstances FRET can be used to measure distances , significant population heterogeneity in the donor to acceptor distances in the GroEL GroES complex makes distance determination difficult . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Genetic experiments have shown that the GroEL / GroES chaperone machine of Escherichia coli is absolutely essential , not only for bacterial growth but also for the propagation of many bacteriophages including lambda . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The deduced amino acid sequence displays strong identity / similarity with other cyanobacterial GroES and GroEL proteins . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Molecular cloning of groESL locus , and purification and characterization of chaperonins , GroEL and GroES , from Bacillus brevis . ^^^ GroEL protected from thermal inactivation of and showed refolding promoting activity for malate dehydrogenase , strictly depending on the presence of ATP and GroES . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Folding of malate dehydrogenase inside the GroEL GroES cavity . ^^^ A ' rack ' mechanism of initial protein unfolding proposes that , upon GroES and ATP binding , the polypeptide is stretched between the binding sites on the twisting apical domains of GroEL before complete release into the chamber . ^^^ When bound to GroEL , MDH exhibits a core of partially protected secondary structure that is only modestly deprotected upon ATP and GroES binding . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The peptide , which was attached to the N terminus , included the amino acid sequence of the mobile loop of GroES that has been demonstrated to interact with the chaperonin , GroEL . ^^^ Two dimensional gel electrophoresis analysis showed that approximately 15 fold more GroES loop Bax was produced under these conditions than under standard conditions and that GroEL and DnaK were elevated approximately 3 fold . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Refolding of bovine mitochondrial rhodanese by chaperonins GroEL and GroES . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
A substrate for the E . coli chaperonins GroEL and GroES . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Assembly and disassembly of GroEL and GroES complexes . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
To obtain more sequence data from groESL genes of Enterococcus faecalis , the full length sequence of the E . faecalis groESL genes containing groES ( 285 bp ) , spacer ( 57 bp ) , and groEL ( 1 , 626 bp ) was determined . ^^^ A database search of GenBank revealed that the deduced E . faecalis GroES and GroEL proteins show significant homology to the GroES and GroEL proteins of other bacteria . ^^^ The GroEL ( groEL ) of E . faecalis had the highest identity with Streptococcus pneumoniae ( 81 . 8 % amino acid sequence identity and 73 . 0 % nucleotide sequence identity ) , followed by Lactococcus zeae , while GroES ( groES ) had 60 . 2 % ( 64 . 6 % ) identity with Lactobacillus zeae and 58 . 5 % ( 66 . 2 % ) identity with Lactococcus lactis , followed by 57 . 0 % ( 65 . 5 % ) identity with Bacillus subtilis . ^^^ Dot blot hybridization using either groES or groEL as the probe distinguished E . faecalis clearly from other species , indicating that both genes can be used as suitable targets for E . faecalis identification . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
We have analyzed the dynamics of the chaperonin ( GroEL ) cochaperonin ( GroES ) interaction at the single molecule level . ^^^ In the presence of ATP and non native protein , binding of GroES to the immobilized GroEL occurred at a rate that is consistent with bulk kinetics measurements . ^^^ However , the release of GroES from GroEL occurred after a lag period ( approximately 3 s ) that was not recognized in earlier bulk phase studies . ^^^ This observation suggests a new kinetic intermediate in the GroEL GroES reaction pathway . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
To achieve this , a fully functional system consisting of GroEL , the cochaperone GroES , and ATP is necessary . ^^^ One of these open questions is the importance of so called `` football ' ' complexes consisting of GroEL and two bound GroES rings . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Binding , encapsulation , and release of nonnative proteins by GroEL and its cochaperone GroES are controlled by the binding and hydrolysis of ATP . ^^^ In one ring of GroEL ATP , the apical ( substrate binding ) domains are extremely disordered , consistent with the high mobility needed for them to achieve the 60 degrees elevation and 90 degrees twist of the GroES bound state . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
From N terminal sequences of 15 major spots , DnaK , GroEL , GroES , alkyl hydroperoxide reductase , aldehyde dehydrogenase , succinyl coenzyme A ( CoA ) synthetase , 30S ribosomal protein S 6 , and ATP synthase alpha subunit were identified . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The GroEL / GroES chaperonin system mediates the folding of a range of newly synthesized polypeptides in the bacterial cytosol . ^^^ Using a rapid biotin streptavidin based inhibition of chaperonin function , we show that the cage formed by GroEL and its cofactor GroES can have a dual role in promoting folding . ^^^ First , enclosure of nonnative protein in the GroEL : GroES complex is essential for folding to proceed unimpaired by aggregation . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Neither GroEL nor GroES , expressed in trans , affected Cyt1Aa as did P 20 . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Co expression of p 16 with the chaperonins GroEL and GroES has allowed its purification in a soluble form . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The bacterial chaperonin GroEL functions with its cofactor GroES in assisting the folding of a wide range of proteins in an ATP dependent manner . ^^^ GroEL GroES constitute one of the main chaperone systems in the Escherichia coli cytoplasm . ^^^ The chaperonin facilitates protein folding by enclosing substrate proteins in a cage defined by the GroEL cylinder and the GroES cap where folding can take place in a protected environment . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
GroEL is an 800 kDa molecular chaperone , which , along with its co chaperonin GroES , promotes protein folding both in vitro and in the bacterial cell . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
For purifying the proteins , we applied the principle of heat stability for GroELx and pI difference for GroESx to minimize copurification with the hosts GroEL and GroES , respectively . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The chaperonin GroEL drives its protein folding cycle by cooperatively binding ATP to one of its two rings , priming that ring to become folding active upon GroES binding , while simultaneously discharging the previous folding chamber from the opposite ring . ^^^ These observations , together with the effects of ATP binding to a GroEL GroES ADP complex , suggest structural models for the ATP induced reduction in affinity for polypeptide and for cooperativity . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
GroEL / GroES mediated folding of a protein too large to be encapsulated . ^^^ The chaperonin GroEL binds nonnative proteins too large to fit inside the productive GroEL GroES cis cavity , but whether and how it assists their folding has remained unanswered . ^^^ We observed that aconitase folding both in vivo and in vitro requires both GroEL and GroES , and proceeds via multiple rounds of binding and release . ^^^ Following the phase of ATP / GroES dependent refolding , GroEL stably bound apoaconitase , releasing active holoenzyme upon Fe ( 4 ) S ( 4 ) cofactor formation , independent of ATP and GroES . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Molecular mechanisms of chaperonin GroEL GroES function . ^^^ The dynamics of the GroEL GroES complex is investigated with a coarse grained model . ^^^ The nature of the most important ( slowest ) normal modes reveals a wide variety of motions uniquely dependent upon the central cavity of the structure , including opposed torsional rotation of the two GroEL rings accompanied by the alternating compression and expansion of the GroES cap binding region , bending , shear , opposed radial breathing of the cis and trans rings , and stretching and contraction along the protein assembly ' s long axis . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
To improve the production of oligo 1 , 6 glucosidase from the obligately thermophilic Bacillus thermoglucosidasius KP 1006 in Escherichia coli , the combined expression of oligo 1 , 6 glucosidase with various chaperone proteins of Hsp ( heat shock protein ) 60 team proteins ( GroES and GroEL ) or Hsp 70 team proteins ( GrpE , DnaK and DnaJ ) from the same thermophile was examined . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Rhodanese can partially refold in its GroEL GroES ADP complex and can be released to give a homogeneous product . ^^^ Molecular chaperones GroEL and GroES facilitate reactivation of denatured rhodanese which folds poorly unless the process is assisted . ^^^ Rhodanese partially folds while in the GroEL GroES ADP complex , but it does not significantly reach an active state . ^^^ Partially folded rhodanese can be released from the GroEL GroES ADP complex by subdenaturing concentrations of urea as a homogeneous species that is committed to fold to the native conformation with little or no partitioning to the aggregated state . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Western analysis identified five E . coli molecular chaperones including DnaK , DnaJ , GrpE , GroEL , and GroES . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Requirement for GroEL / GroES dependent protein folding under nonpermissive conditions of macromolecular crowding . ^^^ Their folding becomes dependent on the complete GroEL / GroES chaperonin system and is not affected by trap GroEL , indicating that folding has to occur in the chaperonin cavity with release of nativelike proteins into the bulk solution . ^^^ In addition , we demonstrate that efficient folding in the chaperonin cavity requires ATP hydrolysis , as formation of ternary GroEL / GroES complexes with substrate proteins in the presence of ADP results only in very inefficient reactivation . ^^^ However , protein refolding reactions using ADP fluoroaluminate complexes , or single ring GroEL and GroES under conditions where only a single round of ATP hydrolysis occurs , yield large amounts of refolded enzymes . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Addition of reduced glutathione , oxidized glutathione , protein disulfide isomerase and molecular chaperones , GroEL and GroES , increased the solubility and the antigen binding activity of the Fab fragment greatly . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The former proteins included several molecular chaperones ( GroEL , GroES , DnaK , GrpE , and CbpA ) , proteins involved in acid resistance ( HdeA , HdeB , and GadA ) , the `` starvation lipoprotein ' ' ( Slp ) , cytolysin ClyA ( HlyE or SheA ) , and several enzymes involved in metabolic pathways , whereas most of the latter proteins proved to be biosynthetic enzymes . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Reactivation by GroEL required a reductant and the enzyme substrate , but not GroES or ATP . ^^^ Additionally , the mechanism for the GroEL facilitated reactivation of rhodanese shown here appears to be different than that for the chaperonin assisted folding of chemically unfolded polypeptides in which a nucleotide and sometimes GroES is required . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
We have observed that isolated GroEL complexes from stationary cultures contain various polypeptides that can be released from the chaperonin by GroES and / or ATP , and identified two such polypeptides as the proteins GatY and UP 12 . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The amount of the larger fragment increased after addition of GroEL , GroES , and ATP but decreased when ATP was replaced by the nonhydrolyzable ATP analog ATPgammaS . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The heat shock protein GroEL is a double ring structured chaperonin that assists the folding of many newly synthesized proteins in Escherichia coli and the refolding in vitro , with the cochaperonin GroES , of conformationally damaged proteins . ^^^ It is most interesting that the ML analysis of codon substitutions in the different branches of the phylogenetic tree strongly supports the action of positive selection in the different lineages of BUCHNERA : Additionally , the new sliding window analysis of the complete groEL sequence reveals different regions of the molecule under the action of positive selection , mainly located in the apical domain , that are important for both peptide and GroES binding . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The molecular masses of GroES and GroEL proteins were calculated to be 10 , 153 and 56 , 893 Da , respectively . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
NMR analysis of a 900K GroEL GroES complex . ^^^ We tested the resolving power of these techniques by examining the isotope labelled homoheptameric co chaperonin GroES ( M ( r ) 72K ) , either free in solution or in complex with the homotetradecameric chaperonin GroEL ( M ( r ) 800K ) or with the single ring GroEL variant SR 1 ( M ( r ) 400K ) . ^^^ These amino acids belong to a mobile loop region of GroES that forms contacts with GroEL . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Brucella abortus resists the microbicidal mechanisms of macrophages , and the expression of its heat shock proteins ( HSPs ) such as GroEL , GroES and HtrA may play a role in this resistance . ^^^ To elucidate the role of these proteins in protection against Brucella challenge , individual , divalent or trivalent baculovirus ( BV ) recombinants of B . abortus GroEL , GroES and / or HtrA were injected into BALB / c mice either as protein expressing whole cells or as purified proteins . ^^^ Antibodies were observed against B . abortus GroEL and HtrA , but not against GroES . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The Escherichia coli chaperonin machine is composed of two members , GroEL and GroES . ^^^ The GroEL chaperonin can bind 10 15 % of E . coli ' s unfolded proteins in one of its central cavities and help them fold in cooperation with the GroES cochaperonin . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Blocking the GroES apical domain binding site in GroEL rendered the chaperonin inactive in binding GroES and in assisting the folding of denatured rhodanese , but still capable of binding non native proteins , supporting the conclusion that GroES and substrate proteins have , at least partially , distinct binding sites even in the intact GroEL tetradecamer . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The lengths of the groES genes from the 10 species listed above ranged from 282 to 288 bp , and the full length sequences of groEL determined for 4 species ( S . anginosus , S . constellatus , S . gordonii , and S . sanguis ) revealed that each was 1 , 623 bp . ^^^ The intergenic region ( spacer ) between the groES and groEL genes varies in size ( 15 to 111 bp ) and sequence between species . ^^^ The variation of the groES sequences among the species tested was greater ( 62 . 1 to 95 . 1 % nucleotide sequence identities ) than that of the groEL sequences ( 77 . 2 to 95 . 2 % nucleotide sequence identities ) . ^^^ Phylogenetic analysis of the groES and groEL genes yielded evolutionary trees similar to the tree constructed by use of the 16S rRNA gene . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Herein , correlated mutations in chaperonins are analyzed to unravel routes of allosteric communication in GroEL and in its complex with its co chaperonin GroES . ^^^ It is shown that analysis of correlated mutations in the chaperonin family can provide information about pathways of allosteric communication within GroEL and between GroEL and GroES . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The bacterial chaperonin GroEL requires GroES to reduce aggregation and cell death in a COS 7 cell model of Huntington ' s disease . ^^^ Here we show that the bacterial chaperonin GroEL can reduce aggregation of mutant huntingtin in COS 7 cells and requires GroES for efficient activity , analogous to what has been described in bacteria . ^^^ The reduction in aggregation of mutant huntingtin by GroEL / GroES was associated with protection against polyglutamine induced cell death . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
GroEL substrate GroES ternary complexes are an important transient intermediate of the chaperonin cycle . ^^^ GroEL C138W is a mutant form of Escherichia coli GroEL , which forms an arrested ternary complex composed of GroEL , the co chaperonin GroES and the refolding protein molecule rhodanese at 25 degrees C . ^^^ The simultaneous binding of GroES and substrate to the cis ring suggested that an efficient transfer of substrate protein into the GroEL central cavity was assured by the binding of GroES prior to complete substrate release from the apical domain . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Genetic immunization with Ehrlichia ruminantium GroEL and GroES homologues . ^^^ Ehrlichia ruminantium GroEL and GroES genes were amplified from E . ruminantium Welgevonden genomic DNA and were cloned into genetic vaccine and Salmonella expression vectors . ^^^ Both GroEL and GroES induced low levels of protection in Balb / c and C57BL / 6J mice immunized with the Salmonella expression vectors . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Encapsulation of an 86 kDa assembly intermediate inside the cavities of GroEL and its single ring variant SR 1 by GroES . ^^^ We described previously that during the assembly of the alpha ( 2 ) beta ( 2 ) heterotetramer of human mitochondrial branched chain alpha ketoacid dehydrogenase ( BCKD ) , chaperonins GroEL / GroES interact with the kinetically trapped heterodimeric ( alphabeta ) intermediate to facilitate conversion of the latter to the native BCKD heterotetramer . ^^^ This large heterodimeric intermediate is accommodated as an entity inside cavities of GroEL and its single ring variant SR 1 and is encapsulated by GroES as indicated by the resistance of the heterodimer to tryptic digestion . ^^^ In contrast , an unfolded BCKD fusion protein of similar size , which also resides in the GroEL or SR 1 cavity , is too large to be capped by GroES . ^^^ The cis capping mechanism is consistent with the high level of BCKD activity recovered with the GroEL alphabeta complex , GroES , and Mg ATP . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Putative heat shock proteins DnaK , DnaJ , GrpE , GroES and GroEL ( 70 , 43 , 24 , 10 and 55 kDa , respectively ) were among the proteins whose synthesis was induced in response to acid adaptation . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Inactivation is not due to irreversible covalent modification , since GroEL can reactivate both C3S E and WT E in the presence of GroES and ATP . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The Escherichia coli proteins GroEL and GroES were the first chaperones to be studied in detail and have thus become a role model for assisted protein folding in general . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The chaperones GroES , GroEL and DnaK contributed to stabilization of DnaA 204 protein . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The sequence analysis of 2229 bp of the groESL operon reveals two open reading frames of 288 nucleotides ( groES ) and 1653 nucleotides ( groEL ) separated by 20 nucleotides . ^^^ The deduced amino acid sequence of R . typhi GroES and GroEL shows a high degree of identity with other bacterial GroES and GroEL . ^^^ Reverse transcriptase polymerase chain reaction and Northern blot analysis indicated that both groES and groEL are transcribed as a single mRNA . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
We also determined that general molecular chaperones GroEL and GroES had no effects on the solubility of scFvs when co expressed with scFv in E . coli . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Here , we present a method for the large scale purification of human PP2Amt using an Escherichia coli host , coexpressing the chaperonins GroEL and GroES . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Truncated variants were inactive as minichaperones as they failed to restore the growth of groEL 140 cells at 43 degrees C whether or not GroES was co expressed . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Only C . trachomatis groEL 1 and groES together complemented a temperature sensitive E . coli groEL mutant . ^^^ Complementation did not occur with groEL 2 or groEL 3 alone or together with groES . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The Escherichia coli chaperonin system , GroEL GroES , facilitates folding of substrate proteins ( SPs ) that are otherwise destined to aggregate . ^^^ To describe the molecular basis for the changes in the nature of SP GroEL interactions we use the crystal structures of GroEL ( T state ) , GroEL ATP ( R state ) and the GroEL GroES ( ADP ) ( 7 ) ( R ' ' state ) complex to determine the residue specific changes in the accessible surface area and the number of tertiary contacts as a result of the T > R > R ' ' transitions . ^^^ In the course of the T > R transition the microenvironment of the SP changes which suggests that GroEL is an annealing machine even without GroES . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
METHODS : To examine if C pneumoniae infection is associated with ARMD , serum samples from 25 consecutive patients with ARMD and from 18 without the disease were collected and assayed for the presence of the antibodies to C pneumoniae elementary bodies , Chlamydia trachomatis heat shock protein 60 ( cHsp 60 ) , C trachomatis heat shock protein 10 ( cHsp 10 ) , Escherichia coli GroEL , and E coli GroES . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
We report a novel heterologous system for the expression of catalytically active iron containing NI 1 NHase in Escherichia coli , involving coexpression with the E . coli GroES and GroEL chaperones . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The prokaryotic chaperonin GroEL requires a cofactor , GroES , which serves as a `` lid ' ' enclosing substrates in the central cavity and confers an asymmetry on GroEL required for cooperative transitions driving the reaction . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The double ring chaperonin GroEL binds unfolded protein , ATP , and GroES to the same ring , generating the cis ternary complex in which folding occurs within the cavity capped by GroES ( cis folding ) . ^^^ In ADP and AMPPNP , GroES bound quickly to GroEL but bound very slowly to the GroEL loaded with unfolded rhodanese or malate dehydrogenase . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Molecular characterization of GroES and GroEL homologues from Clostridium botulinum . ^^^ The N terminal amino acid sequences of the purified proteins were closely related to those of other bacterial GroEL and GroES proteins , and both positively cross reacted with Escherichia coli GroEL and GroES antibodies . ^^^ Native GroEL homologue as an oligomeric complex is a weak ATPase whose activity is inhibited by the presence of GroES homologue . ^^^ The sequence included two complete open reading frames ( 282 and 1629 bp ) , which were homologous to the groES and groEL gene family of bacterial proteins . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The architecture of the GroEL GroES ( ADP ) ( 7 ) chaperonin complex . 1 . ^^^ The composite form enclosing the chaperonin complex GroEL GroES ( ADP ) ( 7 ) is derived and decomposed into heptagrammal forms . ^^^ In the chaperonin complex , nine such heptagrammal molecular forms are found : three for each ring ( trans and cis ) of GroEL and three for GroES . ^^^ The change in the folding of the chains in the cis ring of GroEL arising from binding to GroES leaves the chain segmentation invariant . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The architecture of the GroEL GroES ( ADP ) ( 7 ) chaperonin complex . 2 . ^^^ D 59 , 783 794 ] enclose chain segments of symmetry related monomers in the GroEL GroES ( ADP ) ( 7 ) chaperonin complex . ^^^ The change in folding ( polymorphism ) observed in the cis ring of GroEL arising from binding to GroES is discussed . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Folding with and without encapsulation by cis and trans only GroEL GroES complexes . ^^^ Although a cis mechanism of GroEL mediated protein folding , occurring inside a hydrophilic chamber encapsulated by the co chaperonin GroES , has been well documented , recently the GroEL GroES mediated folding of aconitase , a large protein ( 82 kDa ) that could not be encapsulated , was described . ^^^ Here , we have evaluated this mechanism further using trans only complexes in which GroES is closely tethered to one of the two GroEL rings , blocking polypeptide binding by that ring . ^^^ In vitro , trans only folded aconitase with kinetics identical to GroEL GroES . ^^^ Surprisingly , trans only also folded smaller GroEL GroES dependent substrates , Rubisco and malate dehydrogenase , but at rates slower than the cis reaction . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The genes chosen included four likely to be selectively neutral ( acn , groES , groEL , and recA ) and three likely to be under selective pressure ( flaA , mompS , and proA ) . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The DNA region of the Vibrio harveyi chromosome containing the heat shock genes groES and groEL was cloned , and the genes were sequenced . ^^^ These genes are arranged in the chromosome in the order groES groEL . ^^^ Northern hybridization experiments with RNA from 5 . harveyi and a DNA probe carrying both groES and groEL genes showed a single , heat inducible transcript of approximately 2200 nt , indicating that these genes form an operon . ^^^ The ability of the cloned groESL genes to complement E . coli groE mutants was tested : 5 . harveyi groES restored a thermoresistant phenotype to groES bacteria and enabled lambda phage to grow in the mutant cells . 5 . harveyi groEL did not abolish thermosensitivity of groEL bacteria but it complemented the groEL mutant with respect to growth of lambda phage . ^^^ The results suggest that the GroEL chaperone may be more species specific than the GroES co chaperone . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Role of the gamma phosphate of ATP in triggering protein folding by GroEL GroES : function , structure and energetics . ^^^ Productive cis folding by the chaperonin GroEL is triggered by the binding of ATP but not ADP , along with cochaperonin GroES , to the same ring as non native polypeptide , ejecting polypeptide into an encapsulated hydrophilic chamber . ^^^ Aluminium fluoride was observed to stabilize the association of GroES with GroEL , with a substantial release of free energy ( 46 kcal / mol ) . ^^^ To understand the basis of such activation and stabilization , a crystal structure of GroEL GroES ADP . ^^^ Surprisingly , when this structure was compared with that of the previously determined GroEL GroES ADP complex , no other differences were observed . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
We also observed a differential induction of heat shock proteins by low pH as members of the CtsR regulon , ClpE and ClpP were induced at both pH 5 . 5 and 4 . 5 , while HrcA regulated chaperones , GroEL , GroES , DnaK and GrpE were induced only at pH 4 . 5 . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The full sequence of the gene encoding the GroES protein ( groES ) was found directly upstream from groEL . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Although the optimum temperatures for GroESL function are different in psychrophilic , mesophilic , and thermophilic bacteria , the deduced amino acid sequences of C . maris GroES and GroEL showed remarkably high similarity with those of GroES and GroEL from mesophilic and thermophilic bacteria . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
As the groES and groEL genes of P . aeruginosa have now been cloned and their nucleotide sequences determined , the aim of this study was to develop a novel PCR assay for the detection of Pseudomonas spp . from patients with CF by employing conserved primer regions of the groE heat shock protein domain gene . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Crystallization of the chaperonin GroEL GroES complex from Thermus thermophilus HB 8 . ^^^ The chaperonin GroEL GroES ( GroEL / ES ) complex from a thermophilic eubacteria , Thermus thermophilus HB 8 , has been purified and crystallized . ^^^ The GroEL / ES complex is known to be composed of 14 identical GroEL subunits ( 58 kDa ) and seven identical GroES subunits ( 11 kDa ) . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
All three proteins bound nucleotide as effectively as did GroEL , but the binding of GroES in the presence of ATP or ADP was reduced significantly relative to the wild type . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Previous studies have also shown that protein substrates , GroES , and oligopeptides bind to partially overlapped sites on the apical domain surfaces of GroEL . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Particular protein species of GroEL , HyuA , GroES and AtpA appear to be useful surrogate markers for gastric carcinoma detection and consequently should be considered for further prospective studies to assess their predictive value . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Structural studies of the bacterial chaperonin , GroEL , both alone and in complex with its co chaperonin , GroES , have resolved the states of chaperonin that bind and fold non native polypeptides . ^^^ Functional studies have resolved the action of ATP binding and hydrolysis in driving the GroEL GroES machine through its folding active and binding active states , respectively . ^^^ As a polypeptide bound ring becomes associated with GroES , do the large rigid body movements of the GroEL apical domains serve as another source of a potential unfolding action . ^^^ Finally , how do GroEL and GroES serve , as recently recognized , to assist the folding of substrates too large to be encapsulated inside the machine . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Functional characterization of an archaeal GroEL / GroES chaperonin system : significance of substrate encapsulation . ^^^ As shown recently , Archaea of the genus Methanosarcina contain both group 1 ( GroEL / GroES ) and group 2 ( thermosome ) chaperonins in the cytosol . ^^^ Here we report on a detailed functional analysis of the archaeal GroEL / GroES system of Methanosarcina mazei ( Mm ) in comparison to its bacterial counterpart from Escherichia coli ( Ec ) . ^^^ In the absence of ammonium sulfate , malate dehydrogenase fails to be encapsulated by GroES and rather cycles on and off the GroEL trans ring in a non productive reaction . ^^^ These results indicate that the archaeal GroEL / GroES system has preserved the basic encapsulation mechanism of bacterial GroEL and suggest that it has adjusted the length of its reaction cycle to the slower growth rates of Archaea . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Effect of ADP and GroES on interaction of molecular chaperonin GroEL with non native lysozyme ] . ^^^ However , the addition of the co chaperonin GroES together with ADP ( i . e . the formation of the complex of GroEL with GroES ) leads to drastic weakness of the interaction of GroEL with nonnative lysozyme and the efficiency of its aggregation becomes comparable with that in the absence of GroEL . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The chaperonins are a subgroup of oligomeric molecular chaperones ; the best studied examples are chaperonin 60 ( GroEL ) and chaperonin 10 ( GroES ) , both from the bacterium Escherichia coli . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Western analysis identified five E . coli molecular chaperones including DnaK , DnaJ , GrpE , GroEL , and GroES in eluates . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Recovery of approximately 84 % active rhodanese was obtained with either native or oxidized GroEL in the absence of GroES or ATP . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
By monitoring the tryptophan fluorescence changes of GroEL R231W upon ATP addition in the presence and absence of the co chaperonin GroES , we detected a total of four distinct kinetic phases that corresponded to conformational changes of the apical domain and GroES binding . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The group 1 , or bacterial , chaperonin genes groEL and groES occured in the genomes of Methanosarcina species but were not found in any of the other archaea whose genomes have been sequenced . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
For the present study , a nonacylated recombinant form of Tp 38 was coexpressed with GroES and GroEL in E . coli to facilitate the isolation of soluble , properly folded Tp 38 . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The levels of the molecular chaperones GroEL , GroES , and DnaJ were determined by immunoblotting . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
GroEL encapsulates nonnative substrate proteins in a central cavity capped by GroES , providing a safe folding cage . ^^^ We examine single molecule imaging of GFP folding within the cavity , binding release dynamics of GroEL GroES , ensemble measurements of GroEL / substrate FRET , and the initial kinetics of GroEL ATPase activity . ^^^ During the first timer , GroEL is bound to ATP , substrate protein , and GroES . ^^^ ADP , GroES , and substrate depart GroEL after the second timer is complete . ^^^ This mechanism explains how GroES binding to a GroEL substrate complex encapsulates the substrate rather than allowing it to escape into solution . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Here we demonstrate that HrcA represses a second heat shock promoter that controls the expression of groES and groEL , two other major chlamydial heat shock genes . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
It has been shown previously that the double ring structure of GroEL can be converted to a single ring species by site directed amino acid replacements at the ring interface and that the resultant molecule retains many of the crucial chaperonin properties ; it is structurally stable , hydrolytically active , and can bind both the co chaperonin , GroES , and unfolded substrate proteins . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Eighteen major protein species were subjected to peptide mass fingerprinting and identified as the products of 6 known open reading frames ( ORFs ) : the chaperone DnaK ( heat shock 70 K protein ) , chaperonin 60 K ( GroEL protein , heat shock protein B ) , DnaJ like protein djlA ( mucoidy activation protein mucZ ) , elongation factor Ts ( EF Ts ) , ribosomal protein L7 / L12 , and chaperonin 10 K ( GroES protein , heat shock protein A ) . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The ordering and binding of GroES co chaperonin mobile loops accompany an ATP dependent conformational change in the GroEL chaperonin that promotes client protein folding . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The chaperonins GroEL and GroES are essential mediators of protein folding . ^^^ GroEL binds nonnative protein , ATP , and GroES , generating a ternary complex in which protein folding occurs within the cavity capped by GroES ( cis cavity ) . ^^^ We determined the crystal structure of the native GroEL GroES ADP homolog from Thermus thermophilus , with substrate proteins in the cis cavity , at 2 . 8 A resolution . ^^^ The structure around the cis cavity , which encapsulates substrate proteins , shows significant differences from that observed for the substrate free Escherichia coli GroEL GroES complex . ^^^ The apical domain around the cis cavity of the Thermus GroEL GroES complex exhibits a large deviation from the 7 fold symmetry . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Large rigid body domain movements are critical to GroEL mediated protein folding , especially apical domain elevation and twist associated with the formation of a folding chamber upon binding ATP and co chaperonin GroES . ^^^ Here , we have modeled the anisotropic displacements of GroEL domains from various crystallized states , unliganded GroEL , ATPgammaS bound , ADP AlFx / GroES bound , and ADP / GroES bound , using translation libration screw ( TLS ) analysis . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
As observed in other sequenced chlamydial genomes , the groEL gene belongs to an operon comprising another gene encoding the Hsp GroES . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
We demonstrate that a moderately hydrophobic environment , similar to the interior of the GroEL cavity upon complexion with ATP and GroES , is sufficient to accelerate the folding of a frustrated protein by more than an order of magnitude . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
BeF ( 10 ) stops the chaperonin cycle of GroEL GroES and generates a complex with double folding chambers . ^^^ Coupling with ATP hydrolysis and cooperating with GroES , the double ring chaperonin GroEL assists the folding of other proteins . ^^^ Here we report novel GroEL GroES complexes formed in fluoroberyllate ( BeF ( 10 ) ) that can mimic the phosphate part of the enzyme bound nucleotides . ^^^ In ATP , BeF ( 10 ) stops the functional turnover of GroEL by preventing GroES release and produces a symmetric 1 : 2 GroEL GroES complex in which both GroEL rings contain ADP . ^^^ In ADP , the substrate protein loaded GroEL can not bind GroES . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Characterization of the groEL and groES loci in Bifidobacterium breve UCC 2003 : genetic , transcriptional , and phylogenetic analyses . ^^^ The bacterial heat shock response is characterized by the elevated expression of a number of chaperone complexes , including the GroEL and GroES proteins . ^^^ The groES and groEL genes are highly conserved among eubacteria and are typically arranged as an operon . ^^^ Genome analysis of Bifidobacterium breve UCC 2003 revealed that the groES and groEL genes are located in different chromosomal regions . ^^^ The heat inducibility of the groEL and groES genes of B . breve UCC 2003 was verified by slot blot analysis . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The GroEL GroES chaperonin system is required for the assisted folding of many essential proteins . ^^^ Productive folding of this nonnative intermediate is fully dependent on GroEL , GroES , and ATP . ^^^ A general mechanism used by GroEL to push large , recalcitrant proteins like RuBisCO toward their native states thus appears to involve two steps : partial unfolding or rearrangement of a nonnative protein upon capture by a GroEL ring , followed by spatial constriction within the GroEL GroES cavity that favors or enforces compact , folding competent intermediate states . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The GroEL molecular chaperone of Escherichia coli and its cofactor GroES are highly conserved , and are required for the folding of many proteins . ^^^ Most but not all bacteria express single GroEL and GroES proteins . ^^^ Rhizobium leguminosarum strain A 34 encodes three complete operons encoding homologues to GroEL and GroES . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
A conundrum has arisen in the study of the structural states of the GroEL GroES chaperonin machine : When either ATP or ADP is added along with GroES to GroEL , the same asymmetric complex , with one ring in a GroES domed state , is observed by either 10 ray crystallographic study or cryoelectron microscopy . ^^^ In the absence of bound polypeptide , addition of either ATP / GroES or ADP / GroES to GroEL produced the same rapid rate and extent of decrease of FRET ( t ( 1 / 2 ) < 1 sec ) , reflecting similarly rapid apical movement to the same end state and explaining the results of the structural studies , which were all carried out in the absence of substrate polypeptide . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Some highly conserved eubacterial proteins , such as GroEL and GroES , are notably absent . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Phage carrying the tsf : su coat proteins induced more GroEL and GroES , and increased formation of protein : chaperone complexes as compared with their tsf parents . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The groE operon consists of two genes , groES and groEL ; point mutations in either gene conferred the same phenotype , reducing Lac+ adaptive mutation 10 to 20 fold . groE mutant strains had 1 / 10 the amount of error prone DNA polymerase 4 ( Pol 4 ) . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
We determined the groESL sequences ( groES , groEL , and the intergenic spacer ) of 10 clinically relevant Enterococcus species and evaluated the feasibility of identifying Enterococcus species on the basis of these sequences . ^^^ The lengths and sequences of the intergenic regions ( spacers between the groES and groEL genes ) are quite variable ( 17 to 57 bp in length ) among Enterococcus species but are conserved in strains within each species , with only a few exceptions . ^^^ Considerable variation of groES or groEL sequences was also observed . ^^^ The evolutionary trees of groES or groEL sequences revealed similarities among Enterococcus species . ^^^ However , the overall intraspecies variation of groES was less than that of groEL . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Trigger factor ( TF ) , a ribosome tethered chaperone , and DnaK are known to exhibit overlapping co translational roles , whereas the cage shaped GroEL , with the aid of the co chaperonin , GroES , and ATP , is believed to be implicated in folding only after the polypeptides are released from the ribosome . ^^^ However , the recent finding that GroEL GroES overproduction permits the growth of E . coli cells lacking both TF and DnaK raised questions regarding the separate roles of these chaperones . ^^^ Here , we report the puromycin sensitive association of GroEL GroES with translating ribosomes in vivo . ^^^ Further experiments in vitro , using a reconstituted cell free translation system , clearly demonstrate that GroEL associates with the translation complex and accomplishes proper folding by encapsulating the newly translated polypeptides in the central cavity formed by GroES . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The single ring mutant of GroEL with its simplified composition , but unaltered capability of binding substrates and the co chaperone GroES , is a more suited system for AFM studies . ^^^ High resolution topographical imaging and the interaction of the co chaperone GroES were used to assign the orientations of SR EL in comparison with the physically bisected GroEL . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Among the various polyols used , glycerol was the most effective in enhancing the CS refolding yield , and a complete recovery of enzymatic activity was obtained at 7 m glycerol and 10 mug / ml protein , a result superior to the action of the molecular chaperones GroEL and GroES in vitro . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
For cells grown under noncontrolled pH the expression of the Hsp 70 , GroES and GroEL , measured by Western blotting , was enhanced . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Proteomic analysis also revealed increased synthesis of the heat shock proteins DnaK , GrpE , GroEL and GroES in the absence of HspR . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Although many bacteria contain only a single groE operon encoding the essential chaperones GroES and GroEL , examples of bacteria containing more than one groE operon are common . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Why GroES is unable to fold the T 4 capsid protein in conjunction with GroEL is unknown . ^^^ Here we show that gp 23 binds to the GroEL heptameric ring opposite to the ring that is bound by gp 31 ( the so called trans ring ) , while no binding to the trans ring of the GroEL GroES complex is observed . ^^^ Although gp 23 can be enclosed within the folding cage of the GroEL gp 31 complex , encapsulation within the GroEL GroES complex is not possible . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Most notable among the non responsive genes were those encoding the molecular chaperones DnaK , GroEL and GroES , which are considered to be up regulated by sessile growth . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
With the aid of cochaperonin GroES and ATP , double ring shaped GroEL encapsulates non native substrate proteins inside the cavity of the GroEL ES complex . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Among those genes induced upon adherence to human epithelial cells in culture was rpoH , which encodes a homolog of the heat shock sigma factor , sigma ( 32 ) ( RpoH ) , as well as genes of the RpoH regulon , groEL and groES . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The E . coli chaperonin GroEL and its cofactor GroES promote protein folding by sequestering nonnative polypeptides in a cage like structure . ^^^ These proteins appear to populate kinetically trapped intermediates during folding ; they are stabilized by TF / DnaK against aggregation but reach native state only upon transfer to GroEL / GroES . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The molecular chaperone GroES , together with GroEL from Escherichia coli , is the best characterized protein of the molecular chaperone family . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Using this method the GroEL , FtsZ , DnaK , and GroES proteins were successfully identified from Escherichia coli after separation on two dimensional gels , immunostaining , and on membrane digestion . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The intergenic spacer between groES and groEL appears to be a unique marker for species , with a variable size ( ranging from 111 to 310 bp ) and sequence . ^^^ Phylogenetic analysis of groES and groEL separated the eight serotypes into two major clusters . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Both vectors use the strong promoter preceding the groESL operon ( codes for the essential heat shock proteins GroES and GroEL ) of Bacillus subtilis fused to the lac operator allowing their induction by addition of ITPG . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Sequence analysis revealed an operon containing two genes of 294 ( groES ) and 1632 nucleotides ( groEL ) separated by a 55 nt intergenic spacer . ^^^ Deduced amino acid sequences for B . bacilliformis GroEL and GroES revealed a high degree of identity with homologues from other Bartonella and alpha Protebacteria . ^^^ Northern blot analysis indicated that groES and groEL are co transcribed as a single mRNA of approximately 2 . 4 kb . ^^^ Functional expression and complementation of temperature sensitive Escherichia coli groES or groEL mutants with the cloned operon allowed them to grow at otherwise restrictive temperatures . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The reaction cycle and the major structural states of the molecular chaperone GroEL and its cochaperone , GroES , are well characterized . ^^^ In this study , we investigated the substrate protein human dihydrofolate reductase ( hDHFR ) while bound to GroEL or to a single ring analog , SR 1 , by NMR spectroscopy in solution under conditions where hDHFR was efficiently recovered as a folded , enzymatically active protein from the stable complexes upon addition of ATP and GroES . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
While testing the broad applicability of this technique , we have discovered that osmolytes greatly simplify the chaperonin reaction by eliminating the requirement for the co chaperonin GroES which is normally involved in encapsulating folding proteins within the GroEL GroES cavity . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
We observed that GroES and GroEL of A . aceti had high amino acid sequence homologies to GroES and GroEL of Escherichia coli and Bacillus subtilis . ^^^ Phylogenetic analysis revealed that the A . aceti GroES and GroEL are very closely related to those of other alpha purple proteobacteria . ^^^ A . aceti that overexpressed the groESL was more resistant than the control strain to Stressors such as heat , ethanol , or acetic acid , indicating that GroES and GroEL are closely associated with the characteristic nature of Acetobacter and play an important role in acetic acid fermentation . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
We used DNA affinity chromatography to purify proteins that interact with HrcA in vivo and identified a higher order complex consisting of HrcA , GroEL , and GroES . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
GroES . substrate protein complex from Thermus thermophilus , one GroEL subunit makes contact with two GroES subunits . ^^^ GroES complex is also in contact with GroES ; ( 2 ) when Leu was replaced by Lys ( GroEL ( L309K ) ) or other charged residues , chaperone activity was largely lost ; ( 3 ) the GroEL ( L309K ) . substrate complex failed to bind GroES to produce a stable GroEL ( L309K ) . ^^^ GroES . substrate complex , whereas free GroEL ( L309K ) bound GroES normally ; ( 4 ) the GroEL ( L309K ) . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Mass spectrometry analysis of 7 significant spots indicated that osmotic stress in desiccated IJs was associated with the induction of actin , Proteasome regulatory particle ( ATPase like ) , GroEL chaperonin , GroES co chaperonin and transposase family member . ^^^ GroEL and GroES are members of the Hsp 60 family of chaperons . . ^^^ GroEL and GroES are members of the Hsp 60 family of chaperons . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The sequence of local conformational changes by which GroEL and its cofactor GroES assist protein folding can be explored using the polarity sensitive fluorescence probe Nile Red . ^^^ To explore the sequence of local polarity changes , substrate , GroES , and various nucleotides were added in different orders ; the resulting changes in emission intensity provide insight into the sequence of conformational changes occurring during GroEL mediated protein folding . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Modulation of costimulatory molecules CD80 / CD86 on B cells and macrophages by stress proteins GroEL , GroES and DnaK . ^^^ The aim of this study was to evaluate the effect of the Heat Shock Proteins GroES , GroEL and DnaK on the expression of the costimulatory molecules CD80 / CD86 in B cells and macrophages . ^^^ Our results showed that , on B cells , GroES and GroEL stimulated the expression of CD 86 but did not induce the increase of the CD 80 expression . ^^^ GroES and GroEL also stimulated the expression of CD 80 and CD 86 on macrophages . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
These immunogenic spots were assigned to 6 proteins by MALDI MS and nLC ESI MS / MS : Cu Zn SOD , BCSP 31 , L7 / L12 , GroEL , GroES , and DnaK . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
In DAC 2 , the volume of the cavity is doubled ( as happens when ATP and GroES bind to GroEL ) and the SP pore interaction simultaneously changes from hydrophobic to hydrophilic . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Allosteric signaling of ATP hydrolysis in GroEL GroES complexes . ^^^ The double ring chaperonin GroEL and its lid like cochaperonin GroES form asymmetric complexes that , in the ATP bound state , mediate productive folding in a hydrophilic , GroES encapsulated chamber , the so called cis cavity . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Bacterial chaperonin , GroEL , together with its co chaperonin , GroES , facilitates the folding of a variety of polypeptides . ^^^ GroES then encapsulates the substrate and triggers its release into the central cavity of the GroEL / ES complex for folding . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
One of the most studied chaperone complexes is the GroEL GroES complex . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The proteomics study also suggested the possibility of posttranslational modifications in the chaperones DnaK , AhpC , GroES ( DVU 1977 ) , and GroEL ( DVU 1976 ) and also several periplasmic ABC transporters . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The type 2 DAH7P synthase from Mycobacterium tuberculosis was co expressed as native and selenomethionine substituted protein with the Escherichia coli chaperonins GroEL and GroES in E . coli , purified and crystallized . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Bacteriophage T 4 produces a GroES analogue , gp 31 , which cooperates with the Escherichia coli GroEL to fold its major coat protein gp 23 . ^^^ Comparison of this fitted structure with that of the GroEL GroES ADP structure previously determined by cryo electron microscopy shows that the folding cage is expanded . ^^^ At 56 kDa , gp 23 is close to the maximum size limit of a polypeptide that is thought to fit inside the GroEL GroES folding cage . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
GAPDH thermodenatured in the presence of GroEL can not be reactivated by the addition of GroES , Mg2+ , and ATP . ^^^ In contrast , GAPDH denatured in guanidine hydrochloride ( GAPDHden ) is reactivated in the presence of GroEL , GroES , Mg2+ , and ATP , yielding 11 15 % of its original activity , while the spontaneous reactivation yields only 2 3 % . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Interestingly , neither of the groESL operon genes , which encode the GroEL chaperone and its cochaperone GroES , responded to heat shock . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
We have identified five structural rearrangements in GroEL induced by the ordered binding of ATP and GroES . ^^^ However , a second optical signal , carried by a protein substrate bound to GroEL , responds neither to formation of the R ( 2 ) state nor to the binding of GroES . ^^^ GroES cavity , and is not yet displaced from its sites of interaction with GroEL . ^^^ GroES ) the strength of interaction between GroEL and GroES is greatly enhanced , and there is a large and coincident loss of fluorescence signal intensity in the labeled protein substrate , indicating that there is either a displacement from its binding sites on GroEL or at least a significant change of environment . ^^^ This ensures efficient encapsulation of the polypeptide within the GroEL central cavity underneath GroES . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Additional proteins with enhanced expression included those involved in the general ( GroEL , GroES ) and oxidative ( Tpx , Ahp ) stress responses , two known adhesins ( Peb 1 , FlaC ) , and proteins involved in biosynthesis , energy generation , and catabolic functions . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Structural features of the GroEL GroES nano cage required for rapid folding of encapsulated protein . ^^^ GroEL and GroES form a chaperonin nano cage for proteins up to approximately 60 kDa to fold in isolation . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Co translational binding of GroEL to nascent polypeptides is followed by post translational encapsulation by GroES to mediate protein folding . ^^^ The eubacterial chaperonins GroEL and GroES are essential chaperones and primarily assist protein folding in the cell . ^^^ Although the molecular mechanism of the GroEL system has been examined previously , the mechanism by which GroEL and GroES assist folding of nascent polypeptides during translation is still poorly understood . ^^^ Employing the same system here , we further characterized the mechanism by which GroEL assists folding of translated proteins via encapsulation into the GroEL GroES cavity . ^^^ Furthermore , GroES is capable of interacting with the GroEL nascent peptide ribosome complex , and experiments using a single ring variant of GroEL clearly indicate that GroES association occurs only at the trans ring , not the cis ring , of GroEL . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
In order to fold non native proteins , chaperonin GroEL undergoes numerous conformational changes and GroES binding in the ATP dependent reaction cycle . ^^^ Using this system , we visualized the GroES binding to and dissociation from individual GroEL with a lifetime of 6 s ( k=0 . 17 s ( 1 ) ) . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
KfiA was expressed in a C terminal six His fusion protein in BL 21 star cells coexpressing chaperone proteins GroEL and GroES . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
It has been shown that the chaperonin GroEL , together with GroES co chaperonin and Lon ATP dependent protease are involved in the regulation of expression of the Vibrio fischeri lux operon in Escherichia coli cells . ^^^ It is supposed that GroEL / GroES is responsible for the folding of the LuxR protein , and Lon protease degrades the LuxR protein either before its folding into an active globule or at denaturing . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
Co expression of chaperonin GroEL / GroES enhances in vivo folding of yeast mitochondrial aconitase and alters the growth characteristics of Escherichia coli . ^^^ Over last two decades many researchers have demonstrated the mechanisms of how the Escherichia coli chaperonin GroEL and GroES work in the binding and folding of different aggregation prone substrate proteins both in vivo and in vitro . ^^^ However , preliminary aspects , such as influence of co expressing GroEL and GroES on the over expression of other recombinant proteins in E . coli cells and subsequent growth aspects , as well as the conditions for optimum production of recombinant proteins in presence of recombinant chaperones have not been properly investigated . ^^^ In the present study we have demonstrated the temperature dependent growth characteristics of E . coli cells , which are over expressing recombinant aconitase and how the co expression of E . coli chaperonin GroEL and GroES influence the growth rate of the cells and in vivo folding of recombinant aconitase . ^^^ Presence of co expressed GroEL reduces the aconitase over expression drastically ; however , exogenous GroEL & GroES together compensate this reduction . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
PBMC were tested for secretion of tumor necrosis factor alpha ( TNF alpha ) , interferon gamma ( IFN gamma ) , interleukin 5 ( IL 5 ) and IL 10 in response to complex ( whole cells , culture filtrate and cell walls ) , single secreted ( Ag85B , ESAT 6 , MPT 64 , PstS and MPT 70 ) and single cytosolic ( DnaK , GroES and GroEL ) antigens of Mycobacterium tuberculosis . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
The bacterial chaperonin GroEL , along with its co chaperonin GroES , is probably the best studied example of this family of protein folding machine . ^^^ In this review , we examine some of the general properties of proteins that do not fold well in the absence of GroEL and then consider how folding of these proteins is enhanced by GroEL and GroES . ^^^ Recent experimental and theoretical studies suggest that chaperonins like GroEL and GroES employ a combination of protein isolation , unfolding , and conformational restriction to drive protein folding under conditions where it is otherwise not possible . . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
METHODS : We validated the use of tissue microarray ( TMA ) technology , in combination with immunohistochemistry ( IHC ) , to test antibodies ( GroEL , GroES , GspD , Ndk and Pyk ) raised against differentially expressed proteins under an interferon gamma ( IFN gamma ) induced model of chlamydial persistence . ^^^ Subsequently , it was shown in a second TMA including archival atheromatous heart tissues from 12 patients undergoing heart transplantation , that GroEL , GroES , GspD and Pyk were expressed in atheromatous heart tissue specimens as well , and were detectable morphologically within lesions by IHC . ^^^ CONCLUSION : TMA technology proved useful in documenting functional proteomics data with the morphologic distribution of GroEL , GroES , GspD , Ndk and Pyk within formalin fixed , paraffin embedded cell pellets and tissues from patients with severe coronary atherosclerosis . ^^^ The antibodies GroEL and GroES , which were upregulated under persistence in proteomic analysis , displayed positive reaction in atheromatous heart tissue from 10 out of 12 patients . ^^^
Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
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Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
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Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
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Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
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Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
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Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
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Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
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Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
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Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
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Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
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Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
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Interacting proteins: P61604 and P10809	Pubmed	SVM Score :0.0
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