| Interacting proteins: P00374 and P10809 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P00374 and P10809 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P00374 and P10809 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P00374 and P10809 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P00374 and P10809 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P00374 and P10809 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P00374 and P10809 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P00374 and P10809 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P00374 and P10809 |
Pubmed |
SVM Score :0.72572426 |
| The mutant EcDHFR 1 ( 7 ) 136 binds to GroEL with a stoichiometry of 4 5 mol of DHFR per mol of GroEL tetradecamer , while murine DHFR binds to GroEL with a stoichiometry of 2 mol of DHFR per mol of GroEL tetradecamer . 0.72572426^^^ In contrast , murine DHFR shows a strong interaction with GroEL . 0.52339542^^^ |
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| Interacting proteins: P00374 and P10809 |
Pubmed |
SVM Score :0.0 |
| Under standard import conditions , no significant association of DHFR with hsp 60 could be detected . ^^^ |
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| Interacting proteins: P00374 and P10809 |
Pubmed |
SVM Score :0.0 |
| Our data argue against this model : import intermediates of cytochromes c 1 and b 2 were found only outside the inner membrane ; maturation of these proteins was independent of the matrix localized hsp 60 chaperone ; and dihydrofolate reductase linked to the presequence of either cytochrome was imported to the intermembrane space in the absence of ATP . ^^^ |
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| Interacting proteins: P00374 and P10809 |
Pubmed |
SVM Score :0.0 |
| The Hsp 60 was required to prevent the thermal inactivation in vivo of native dihydrofolate reductase ( DHFR ) imported into mitochondria . ^^^ |
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| Interacting proteins: P00374 and P10809 |
Pubmed |
SVM Score :0.0 |
| The spontaneous refolding of chemically denatured dihydrofolate reductase ( DHFR ) is completely arrested by chaperonin 60 ( GroEL ) . ^^^ |
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| Interacting proteins: P00374 and P10809 |
Pubmed |
SVM Score :0.0 |
| 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 . ^^^ |
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| Interacting proteins: P00374 and P10809 |
Pubmed |
SVM Score :0.0 |
| We sought to identify the site on the Escherichia coli chaperonin groEL , where the `` molten globule ' ' like intermediate of dihydrofolate reductase ( DHFR ) becomes bound , by examining in the scanning transmission electron microscope complexes formed between groEL and DHFR molecules bearing covalently crosslinked 1 . 4 nm gold clusters . ^^^ |
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| Interacting proteins: P00374 and P10809 |
Pubmed |
SVM Score :0.0 |
| 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 . ^^^ |
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| Interacting proteins: P00374 and P10809 |
Pubmed |
SVM Score :0.0 |
| Ligand induced conformational changes of GroEL alone and with bound rhodanese , citrate synthase , or dihydrofolate reductase were studied by limited proteolysis . ^^^ Strikingly , only with Mg2+ / ATP or K+ / Mg2+ / ATP an additional fragment of approximately 25 kDa was generated during digestion of GroEL alone or with bound rhodanese or dihydrofolate reductase , but not with bound citrate synthase . ^^^ |
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| Interacting proteins: P00374 and P10809 |
Pubmed |
SVM Score :0.0 |
| Here we describe the conformational properties of human dihydrofolate reductase ( DHFR ) bound to GroEL at different stages of its ATP driven folding reaction , determined by hydrogen exchange labeling and electrospray ionization mass spectrometry . ^^^ |
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| Interacting proteins: P00374 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 . ^^^ |
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| Interacting proteins: P00374 and P10809 |
Pubmed |
SVM Score :0.0 |
| Here we have studied a substrate protein , human dihydrofolate reductase ( DHFR ) , observing in stopped flow fluorescence experiments that it can rapidly bind to GroEL at various stages of folding . ^^^ |
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| Interacting proteins: P00374 and P10809 |
Pubmed |
SVM Score :0.0 |
| Cooperative effects of potassium , magnesium , and magnesium ADP on the release of Escherichia coli dihydrofolate reductase from the chaperonin GroEL . ^^^ Previous investigation has shown that at 22 degrees C and in the presence of the chaperonin GroEL , the slowest step in the refolding of Escherichia coli dihydrofolate reductase ( EcDHFR ) reflects release of a late folding intermediate from the cavity of GroEL ( Clark AC , Frieden C , 1997 , J Mol Biol 268 : 512 525 ) . ^^^ |
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| Interacting proteins: P00374 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 . ^^^ |
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| Interacting proteins: P00374 and P10809 |
Pubmed |
SVM Score :0.0 |
| The aims of the present study were ( 1 ) to develop and test a sensitive and reproducible method for the study of gene expression in staphylococci and ( 2 ) to study the expression of five housekeeping genes which are involved in nucleic acid metabolism ( gmk , guanylate kinase ; the dihydrofolate reductase [ DHFR ] gene ) , glucose metabolism ( tpi , triosephosphate isomerase ) , and protein metabolism ( the 16S rRNA gene ; hsp 60 , heat shock protein 60 ) during in vitro exponential and stationary growth . ^^^ |
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| Interacting proteins: P00374 and P10809 |
Pubmed |
SVM Score :0.0 |
| We found that the binding of aconitase , alpha lactalbumin , and murine dihydrofolate reductase to GroEL falls in line with our present model and have also predicted the exact regions of their binding to GroEL . ^^^ |
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| Interacting proteins: P00374 and P10809 |
Pubmed |
SVM Score :0.0 |
| 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 . ^^^ |
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| Interacting proteins: P00374 and P10809 |
Pubmed |
SVM Score :0.0 |
| Using stopped flow fluorescence techniques , we have examined both the refolding and unfolding reactions of four structurally homologous dihydrofolate reductases ( murine DHFR , wild type E . coli DHFR , and two E . coli DHFR mutants ) in the presence and absence of the molecular chaperonin GroEL . ^^^ We show that GroEL binds the unfolded conformation of each DHFR with second order rate constants greater than 3 10 10 ( 7 ) M ( 1 ) s ( 1 ) at 22 degrees C . ^^^ Due to this kinetic partitioning , three different mechanisms can be proposed for the formation of stable complexes between GroEL and either murine DHFR or the two E . coli DHFR mutants . ^^^ |
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| Interacting proteins: P00374 and P10809 |
Pubmed |
SVM Score :0.0 |
| In general , the data demonstrate that the overall binding free energy for the interaction of GroEL with native DHFR is the sum of the free energy for the first step in DHFR unfolding , which is unfavorable , and the free energy of binding the non native conformation , which is favorable . ^^^ |
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