| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.18416329 |
| With the availability of the three dimensional structure of the complex between multisubunit PheRS and tRNAPhe , a fuller picture of the specific tRNA aaRS interactions is beginning to emerge . 0.18416329^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.084473338 |
| The structural similarity between PheRS and histidyl tRNA synthetase extends to the amino acid binding site , which is normally unique for each enzyme . 0.084473338^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| A thermosensitive E . coli mutant is described which has at least two defects in vitro : a thermolabile initiation factor IF 3 activity and a modified L phenylalanine : tRNAPhe ligase ( EC 6 . 1 . 1 . 20 ) activity . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| The relationship between thermostability and functional activities of phenylalanyl tRNA synthetases ( EC 6 . 1 . 1 . 20 ) from E . coli and Thermus thermophilus has been studied . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| Phenylalanyl tRNA synthetases [ L phenylalanine : tRNAPhe ligase ( AMP forming ) , EC 6 . 1 . 1 . 20 ] from Escherichia coli , yeast cytoplasm , and mammalian cytoplasm have an unusual conserved alpha 2 beta 2 quaternary structure that is shared by only one other aminoacyl tRNA synthetase . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| Phenylalanyl tRNA synthetase ( EC 6 . 1 . 1 . 20 ) from human placenta was isolated and purified using fractionation with polyethyleneglycol and chromatography on hydroxylapatite , heparin Sepharose and mono S . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| Genet . 151 , 17 26 ] exhibits two defects in vitro , one in the initiation factor IF 3 and the other in the L phenylalanine : tRNA Phe ligase ( EC 6 . 1 . 1 . 20 ) . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| Changes in phenylalanyl tRNA synthetase ( L phenylalanine : tRNAPhe ligase , EC 6 . 1 . 1 . 20 ) and leucyl tRNA synthetase ( L leucine : tRNALeu ligase . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| Duplexes ( formula : see text ) are especially significant as they : ( 1 ) correspond to a natural sequence , the dihydrouridine loop neck region , common to several tRNA molecules ; ( 2 ) correspond to a proposed , partial recognition site for yeast phenylalanyl tRNA ligase ( EC 6 . 1 . 1 . 20 ) ; and ( 3 ) represent the first demonstration of a duplex with four base pairs , one of which is an A U pair . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| Phenylalanyl tRNA synthetase ( EC 6 . 1 . 1 . 20 ) from the extreme thermophile Thermus thermophilus HB 8 has been isolated and crystallized . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| Affinity labelling has been employed to localize the substrate binding sites on the enzyme subunits of phenylalanyl tRNA synthetase ( L phenylalanine : tRNAPhe ligase , EC 6 . 1 . 1 . 20 ) of Escherichia coli MRE 600 ( alpha 2 beta 2 type ) . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| Homogeneous yeast cytoplasmic and mitochondrial phenylalanyl tRNA synthetases ( L phenylalanine : tRNAPhe ligase ( AMP forming ) , EC 6 . 1 . 1 . 20 ) are analysed for structural differences . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| Escherichia coli threonyl tRNA synthetase ( EC 6 . 1 . 1 . 3 ) expression has been examined in an acellular protein synthesizing system programmed with a plasmid DNA carrying thrS , infC , pheS , and pheT , the gene for threonyl tRNA synthetase , initiation factor 3 , and the two protomers of phenylalanyl tRNA synthetase ( EC 6 . 1 . 1 . 20 ) , respectively . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| Experimental data on affinity labeling of phenylalanyl tRNA synthetase ( L phenylalanine : tRNAPhe ligase ( AMP forming ) , EC 6 . 1 . 1 . 20 ) of Escherichia coli MRE 600 with N bromoacetyl [ 14C ] phenylalanyl tRNA are treated in terms of the model suggested . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| Phenylalanyl tRNA synthetase ( EC 6 . 1 . 1 . 20 ) has been purified to homogeneity from a 100 fold overproducing Escherichia coli strain carrying a hybrid pBR 322 plasmid containing the pheS pheT locus . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| Adenosine or CpCpA trinucleoside diphosphate can be aminoacylated by phenylalanyl tRNA synthetase [ L phenylalanine : tRNAPhe ligase ( AMP forming ) , EC 6 . 1 . 1 . 20 ] when the reaction takes place in the presence of tRNAPhe deprived of its 3 ' adenosine or pCpCpA terminus . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| Phenylalanyl tRNA synthetase ( EC 6 . 1 . 1 . 20 ) from the extreme thermophile Thermus thermophilus HB 8 has been crystallized with its cognate tRNA . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| While crystals suitable for 10 ray diffraction analyses are available of phenylalanyl tRNA synthetase ( PheRS ) from the thermophilic bacterium Thermus thermophilus , neither the primary structure of its constituent alpha and beta subunits nor the nucleotide sequence of the corresponding pheS and pheT genes were known . ^^^ The sequences reported here will greatly aid in the three dimensional structure determination of T . thermophilus PheRS , a heterotetrameric ( alpha 2 beta 2 ) , class 2 aminoacyl tRNA synthetase . . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| Neither the tertiary structure nor the location of active sites are known for phenylalanyl tRNA synthetase ( PheRS ; alpha 2 beta 2 structure ) , a member of class 2 aminoacyl tRNA synthetases . ^^^ In an attempt to detect the phenylalanine ( Phe ) binding site , two Escherichia coli PheRS mutant strains ( pheS ) , which were resistant to p fluorophenylalanine ( p F Phe ) were analysed genetically . ^^^ We thus propose that motif 3 participates in the formation of the Phe binding site of PheRS . ^^^ In vivo and in vitro results demonstrated that Phe 293 and Phe 295 are not directly involved in substrate binding , but replacements of those residues affected PheRS stability . ^^^ Of particular interest was the Gly 294 PheRS in which presumably an enlarged cavity for the para position of the aromatic ring allowed an increased aminoacylation of tRNA with p F Phe . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| Phenylalanyl tRNA synthetase ( PheRS ; alpha 2 beta 2 subunit structure ) is a member of class 2 of tRNA synthetases . ^^^ We report here the genetic analysis of an Escherichia coli mutant strain which is auxotrophic for phenylalanine because it has a PheRS with a decreased affinity for phenylalanine . ^^^ The mutant pheS gene encoding the PheRS alpha subunit was cloned and sequenced , and the deviation from the wild type gene was found to result in a Gly 191 to Asp 191 exchange . ^^^ Motif 2 may thus participate in the formation of the phenylalanine binding site in PheRS . . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| These three latter aaRS share three new sequence motifs with AspRS , AsnRS , LysRS , HisRS and the beta subunit of PheRS . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| FRS 1 and FRS 2 , the structural genes encoding the large ( alpha ) and small ( beta ) subunits of yeast phenylalanyl tRNA synthetase ( PheRS ) were placed under the control of the lacZ promoter by creating an artificial operon . ^^^ The engineered PheRS has 16 N terminal amino acids from beta galactosidase fused to the beta subunit . ^^^ The product of the FRS 2 FRS1 operon is not able to complement thermosensitive E . coli PheRS , indicating the lack of heterologous aminoacylation in vivo . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| Although its melting profile suggested a loose higher order structure , presumably influenced by the apparent loss of D loop T loop interaction necessary for forming a rigid L shaped tertiary structure , its aminoacylation capacity catalyzed by mt phenylalanyl tRNA synthetase ( PheRS ) was nearly equal to that of Escherichia coli tRNAPhe . ^^^ Misaminoacylation was not observed for the mt tRNAPhe mt PheRS system . ^^^ Comparing the aminoacylation efficiencies of several combinations of tRNAPheS and PheRSs from various sources , including bovine mitochondria , bovine and yeast cytosols , E . coli , Thermus thermophilus , and Sulfolobus acidocaldarius , it was clarified that mt PheRS was able to aminoacylate all the above mentioned tRNAPhe species , albeit with varying degrees of efficiency . ^^^ This broad charging spectrum suggests that mt PheRS possesses a relatively simple recognition mechanism toward its substrate , tRNAPhe . . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| Periodate oxidized tRNA ( Phe ) ( tRNA ( oxPhe ) ) behaves as a specific affinity label of tetrameric Escherichia coli phenylalanyl tRNA synthetase ( PheRS ) . ^^^ Sodium dodecyl sulfate polyacrylamide gel electrophoresis analysis of the PheRS [ 14C ] tRNA ( oxPhe ) covalent complex indicates that the large ( alpha , Mr 87K ) subunit of the enzyme interacts with the 3 ' adenosine of tRNA ( oxPhe ) . ^^^ The [ 14C ] tRNA labeled chymotryptic peptides of PheRS were purified by both gel filtration and reverse phase high performance liquid chromatography . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| Antibodies to Escherichia coli glycyl tRNA synthetase ( GlyRS ) cross react extensively with E . coli phenylalanyl tRNA synthetase ( PheRS ) . ^^^ Although only limited similarities are found in the protein sequences deduced from their known gene sequences , the presence of common epitopes in GlyRS and PheRS adds to a rather long list of physical and chemical similarities between those proteins . ^^^ In addition , antibodies directed at the alpha and beta subunits of GlyRS inhibit both GlyRS and PheRS in the same relative manner , indicating that the function as well as the structure of subunits is similar in each enzyme . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| The ochratoxin A ( OTA ) metabolite ( 4R ) 4 hydroxyochratoxin A [ 4R ) OTA ) inhibits the aminoacylation of phenylalanine tRNA catalyzed by phenylalanyl tRNA synthetase ( PheRS ) with a Ki value of 0 . 9 mM as compared to 1 . 3 mM for OTA . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| The transfer of amino acid to tRNA by Escherichia coli phenylalanyl tRNA synthetase ( PheRS ) was studied using replacements of Ala 294 in the alpha subunit previously shown to have modified amino acid specificity . ^^^ Steady state analysis of tRNA charging showed little difference between wild type and mutants , whereas pre steady state analysis revealed higher rates of tRNA charging by both the A294S PheRS phenylalanyl adenylate and the A294G PheRS p Cl phenylalanyl adenylate . ^^^ Thus a compromise appears to exist between amino acid activation and tRNA charging , because slowing down the first step increases the rate of the second step , possibly as a result of decreased stability of the PheRS . amino acid AMP complex . . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| The loss is only 1 . 5 fold when tRNA ( Phe ) CC 3 ' deoxyadenosine is aminoacylated by yeast cytoplasmic PheRS ( Sprinzl , M . , & Cramer , F . ( 1973 ) Nature 245 , 3 5 ) , indicating mechanistic differences between the two PheRS ' s active sites for the amino acid transfer step . . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| Detailed comparison between the structures of the Escherichia coli biotin synthetase / repressor protein ( BirA ) and the recently solved Thermus thermophilus phenylalanyl tRNA synthetase ( PheRS ) reveals significant similarities outside their respective catalytic domains . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| The alpha 2 beta 2 enzymes exhibit similarities to PheRS ( also an alpha 2 beta 2 enzyme ) . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| The selected cDNA encodes a protein that is a close homolog of one subunit of prokaryote and yeast phenylalanyl tRNA synthetase ( PheRS ) . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| Both analogs have been cross linked to Thermus thermophilus phenylalanyl tRNA synthetase ( PheRS ) and the specificity of the cross linking has been demonstrated . ^^^ Functional activity of the covalent complex of PheRS with the s4U monosubstituted transcript has been shown by aminoacylation of 60 % of the enzyme cross linked tRNA . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| Since OTA is a phenylalanine analogue , this effect could be due to inhibition of phenylalanine tRNA synthetase ( PheRS ) by competition of this mycotoxin with the amino acid . ^^^ Homogeneous PheRS was purified from Bacillus subtilis and from E . coli transformed with the PheRS gene . ^^^ The latter produced about 40 times more PheRS than B . subtilis . ^^^ The Km and Ki values of PheRS , respectively , for phenylalanine and OTA were measured and their concentrations within the cell determined . ^^^ This does not suggest PheRS to be the target of OTA in cell growth and protein synthesis inhibition in Bacillus subtilis . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| Unlike the catalytic alpha subunit , the beta subunit of heterodimeric ( alphabeta ) 2 phenylalanyl tRNA synthetase ( PheRS ) has no invariant functional amino acids directly involved in the aminoacylation process as it is evident from the crystal structure of the T . thermophilus enzyme complexed with tRNAPhe . ^^^ We cloned , sequenced , and expressed human PheRS . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| Remarkably , both rates of aminoacyl transfer and amino acid specificities are greater for RNA 77 than measured for protein PheRS . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| Using consensus sequences derived from conserved regions of the alpha and beta subunits from bacterial PheRS , two partially sequenced cDNA clones were identified . ^^^ Detailed analysis indicates that unlike the ( alphabeta ) 2 structure of the prokaryotic and eukaryotic cytoplasmic forms of PheRS , the human mtPheRS consists of a single polypeptide chain . ^^^ The N terminal 314 amino acid residues appear to be analogous to the alpha subunit of the prokaryotic PheRS , while the C terminal 100 amino acid residues correspond to a region of the beta subunit known to interact with the anticodon of tRNAPhe . ^^^ Comparisons with the sequences of PheRS from yeast and Drosophila mitochondria indicate they are 42 % and 51 % identical with the human mtPheRS , respectively . ^^^ Evolutionary origins of this small monomeric human mtPheRS are unknown , however , implications are that this enzyme is a result of the simplification of the more complex ( alphabeta ) 2 bacterial PheRS in which specific functional regions were retained . . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| The predicted amino acid sequence is 589 amino acids and shares 45 % identity with the yeast cytoplasmic phenylalanyl tRNA synthetase ( PheRS ) regulatory alpha subunit . ^^^ This is the first report of the cloning of the full length cDNA for the murine PheRS regulatory alpha subunit like protein . ^^^ The level of PheRS alpha subunit like mRNA is regulated during differentiation but not during cell cycle progression . . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| Among other mechanisms of toxicity , it has been suggested that OA inhibits phenylalanyl tRNA synthetase ( PheRS ) , thereby reducing protein synthesis . ^^^ Using the crystal structure of PheRS from Thermusthermophilus , we have modeled its interactions with OA as well as with phenylalanyl adenylate ( FAMP ) , the high affinity intermediate substrate of PheRS . ^^^ Our results indicate that while OA may be capable of weakly inhibiting PheRS , the OA PheRS complex can not adopt the same conformation as does FAMP PheRS , contrary to previous assumptions . ^^^ This , in turn , suggests that the previously observed antagonistic effects of aspartame and piroxicam are more likely due to their prevention of OA binding to human serum albumin than to PheRS , which is in agreement with binding studies as well as with preliminary simulations performed in our laboratory . . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| Two ORFs with similarity to non archaeal PheRSs alpha subunits had previously been found in the genome sequence , but these results show that only one of them , MT 742 , is part of the active PheRS . . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| In this study , we incorporate para bromophenylalanine ( p Br phe ) into a model target protein , mouse dihydrofolate reductase ( DHFR ) , by using a bacterial phenylalanyl tRNA synthetase ( PheRS ) variant with relaxed substrate specificity . ^^^ Coexpression of the mutant PheRS and DHFR in a phenylalanine auxotrophic Escherichia coli host strain grown in p Br phe supplemented minimal medium resulted in 88 % replacement of phenylalanine residues by p Br phe ; variation in the relative amounts of phe and p Br phe in the medium allows control of the degree of substitution by the analog . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| The crystal structure of phenylalanyl tRNA synthetase ( PheRS ) from Thermus thermophilus , a class 2 aminoacyl tRNA synthetase , complexed with phenylalanyl adenylate ( Phe AMP ) was determined at 2 . 6 A resolution . ^^^ Crystals of native PheRS were soaked in a solution containing phenylalanine and ATP in the presence of Mn ( 2+ ) ions . ^^^ A sulfate ion , which was identified on the protein surface , may mediate the interactions of PheRS with DNA . ^^^ Visible conformational changes were detected in the active site area adjacent to the position of the Phe AMP , compared with the structure of PheRS complexed with a synthetic adenylate analogue ( phenylalaninyl adenylate ) . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| The h ( mt ) TrpRS shows kinetic properties similar to human mitochondrial phenylalanyl tRNA synthetase ( h ( mt ) PheRS ) , and h ( mt ) TrpRS is not induced by interferon gamma as is hTrpRS . . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| The interaction of Thermus thermophilus phenylalanyl tRNA synthetase ( PheRS ) with the 3 ; terminal nucleotide of tRNAPhe has been studied by affinity labeling to solve the problem arising from 10 ray crystallographic study : the binding sites of phenylalanine and the 3 ; terminal nucleotide base were revealed to be identical in the crystal structures of PheRS complexed with the substrates . tRNAPhe derivatives containing a photoreactive 4 thiouridine ( tRNAPhe s4U 76 ) or 6 thioguanosine residue ( tRNAPhe s6G 76 ) in the 3 ; end have been prepared using terminal tRNA nucleotidyl transferase . ^^^ The results suggest specific binding of the 3 ; terminal nucleotide of tRNAPhe by the catalytic subunit of PheRS in the absence of other substrates . ^^^ Comparative analysis of the cross linked products in the absence and in the presence of small substrates revealed ATP and aminoacyl adenylate to effect the interaction of the tRNAPhe acceptor end with PheRS . ^^^ The correct positioning of the 3 ; terminal nucleotide of tRNAPhe corresponding to the structure of the productive complex with PheRS is therefore promoted only in the presence of all three substrates . . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| Identification , cloning , and expression of a functional phenylalanyl tRNA synthetase ( pheRS ) from Staphylococcus aureus . ^^^ Phenylalanyl tRNA synthetase ( pheRS ) is unique among aminoacyl tRNA synthetases in that it is a heterotetrameric enzyme composed of two alpha subunits and two larger beta subunits . ^^^ In prokaryotes , the alpha and beta subunits of pheRS are encoded by the genes pheS and pheT , respectively . ^^^ We describe the high level overexpression and purification of recombinant S . aureus pheRS using pheS and pheT genes as part of an artificial operon in Escherichia coli . ^^^ For comparative analysis we also report a procedure for the purification of native pheRS from S . aureus ( Oxford Strain ) and demonstrate that Michaelis Menten parameters for both recombinant and native enzyme , at least for phenylalanine tRNA aminoacylation are comparable . . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| Human phenylalanyl tRNA synthetase ( PheRS ) was cloned and expressed in Escherichia coli . ^^^ Three different types of ( alphabeta ) ( 2 ) heterodimers of human PheRS carrying HT at the N terminus of either of two alpha or beta subunits or simultaneously on both of them were overproduced and purified . ^^^ Aminoacylation activity of the overproduced human PheRS in the crude bacterial extract is two orders of magnitude higher than the corresponding activity in human placenta and the yield of the recombinant enzyme overproduced in E . coli is five times higher . . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| GDP . tRNA ] complex with phenylalanyl tRNA synthetase ( PheRS ) , e . g . the formation of the above quaternary complex detected by the gel retardation and surface plasmon resonance techniques . ^^^ PheRS ] complexes were found to be 20 nm and 9 nm , respectively . ^^^ We also revealed a direct interaction of PheRS with eEF1A in the absence of tRNAPhe ( Kd = 21 nm ) . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| The extent of tRNA recognition at the level of binding by Thermus thermophilus phenylalanyl tRNA synthetase ( PheRS ) , one of the most complex class 2 synthetases , has been studied by independent measurements of the enzyme association with wild type and mutant tRNA ( Phe ) s as well as with non cognate tRNAs . ^^^ The data obtained , combined with kinetic data on aminoacylation , clearly show that PheRS exhibits more tRNA selectivity at the level of binding than at the level of catalysis . ^^^ A few backbone mediated contacts of PheRS with the acceptor and anticodon stems revealed in the crystal structure do not contribute to tRNA ( Phe ) discrimination , their role being limited to stabilization of the complex . ^^^ The highest affinity of T . thermophilus PheRS for cognate tRNA , observed for synthetase tRNA complexes , results in 100 3000 fold binding discrimination against non cognate tRNAs . . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| In this paper , we describe a computational protocol ( HierDock ) for predicting the relative energies of binding of phenylalanine analogues to phenylalanyl tRNA synthetase ( PheRS ) . ^^^ Starting with the crystal structure of Thermus thermophilus PheRS without bound ligand , HierDock predicts the binding site of phenylalanine ( Phe ) within 1 . 1 A of that revealed by the crystal structure of PheRS cocrystallized with Phe . ^^^ The calculated binding energies of Phe analogues in PheRS , using HierDock , correlate well with the translational activities of the same analogues in Escherichia coli . ^^^ HierDock identifies p fluorophenylalanine and 3 thienylalanine as especially good substrates for PheRS , in agreement with experiment . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| In particular , it is suggested that the monomeric PheRS from the yeast mitochondrion is a chimera of the alpha and beta chains of the standard tetrameric protein . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| The functional roles of phenylalanine and ATP in productive binding of the tRNA ( Phe ) acceptor end have been studied by photoaffinity labeling ( cross linking ) of T . thermophilus phenylalanyl tRNA synthetase ( PheRS ) with tRNA ( Phe ) analogs containing the s ( 4 ) U residue in different positions of the 3 ' terminal single stranded sequence . ^^^ Both in the absence and presence of phenylalanine , ATP more effectively inhibits the PheRS labeling with the s ( 4 ) U 76 substituted analog of human tRNA ( Phe ) ( tRNA ( Phe ) s ( 4 ) U 76 ) than with E . coli tRNA ( Phe ) s ( 4 ) U 76 : in the first case the labeling of the alpha subunits is inhibited more effectively ; the labeling of the beta subunits is inhibited in the first case and increased in the second case . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| The effect of replacement of tRNA ( Phe ) recognition elements on positioning of the 3 ' terminal nucleotide in the complex with phenylalanyl tRNA synthetase ( PheRS ) from T . thermophilus in the absence or presence of phenylalanine and / or ATP has been studied by photoaffinity labeling with s ( 4 ) U 76 substituted analogs of wild type and mutant tRNA ( Phe ) . ^^^ The main recognition elements of tRNA ( Phe ) , which optimize its initial binding with PheRS , are also involved in generation of the catalytically active complex providing functional conformation of the acceptor arm . . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| The full recovery of the phenylalanyl ( PheRS ) and seryl tRNA synthetase ( SerRS ) activities was achieved in the presence of 4 microM eEF1A , while bovine serum albumin at similar concentration had no renaturation effect . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| Errors during amino acid selection are usually corrected by the editing activity of aminoacyl tRNA synthetases such as phenylalanyl tRNA synthetases ( PheRS ) , which edit misactivated tyrosine . ^^^ Comparison of cytosolic and mitochondrial PheRS from the yeast Saccharomyces cerevisiae suggested that the organellar protein might lack the editing activity . ^^^ Yeast cytosolic PheRS was found to contain an editing site , which upon disruption abolished both cis and trans editing of Tyr tRNA ( Phe ) . ^^^ Wild type mitochondrial PheRS lacked cis and trans editing and could synthesize Tyr tRNA ( Phe ) , an activity enhanced in active site variants with improved tyrosine recognition . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| However , in this work , it was shown that the main event during evolution of phenylalanyl tRNA synthetase ( PheRS ) is a domain loss , and the function / activity of PheRS is not affected by domain losing . ^^^ Generally , the size of genome and number of genes are increased during evolution from bacteria to eukaryote , but the interesting thing is that the type and number of PheRS domains in eukaryote are obviously less than those in bacteria . ^^^ The evolution of PheRS by domain losing seems to be related to the functional evolution of some AARSs from the multiple specificities to the single specificity . . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| The most potent analogue 1b showed IC50=5 nM ( E . faecalis PheRS ) and IC50=2 nM ( S . aureus PheRS ) with high selectivity over the human enzyme . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| In this study , we determined the crystal structures of complexes of T . thermophilus phenylalanyl tRNA synthetase ( PheRS ) with L tyrosine , p chloro phenylalanine , and a nonhydrolyzable tyrosyl adenylate analog . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| Phenylalanyl tRNA synthetase ( PheRS ) is a multidomain ( alphabeta ) 2 heterotetrameric protein responsible for synthesizing Phe tRNA ( Phe ) during protein synthesis . ^^^ Structural studies of PheRS indicated that the B 2 domain is distant from bound tRNA ( Phe ) , leaving the role of this module in question . ^^^ On the basis of homology modeling with other EMAPII domain containing proteins , the 110 amino acid B 2 domain was deleted to produce PheRS deltaB 2 . ^^^ Full length PheRS and PheRS deltaB 2 showed comparable kinetics for in vitro aminoacylation , and both enzymes complemented a defect in phenylalanylation in vivo . ^^^ PheRS deltaB 2 showed a 2 fold drop compared to full length PheRS in the catalytic efficiency ( kcat / KM ) of Tyr tRNA ( Phe ) hydrolysis , suggesting a role for the B 2 domain in post transfer editing . ^^^ |
|
| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| The crystal structure of the ternary complex of ( alphabeta ) ( 2 ) heterotetrameric phenylalanyl tRNA synthetase ( PheRS ) from Thermus thermophilus with cognate tRNA ( Phe ) and a nonhydrolyzable phenylalanyl adenylate analogue ( PheOH AMP ) has been determined at 3 . 1 A resolution . ^^^ The single stranded 3 ' end exhibits a hairpin conformation in contrast to the partial unwinding observed previously in the binary PheRS . tRNA ( Phe ) complex . ^^^ Our data suggest that the idiosyncratic feature of PheRS , which aminoacylates the 2 ' OH group of the terminal ribose , is dictated by the system specific topology of the CCA end binding site . . ^^^ |
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| Interacting proteins: O95363 and Q9NSD9 |
Pubmed |
SVM Score :0.0 |
| Phenylalanyl tRNA synthetase ( PheRS ) hydrolyzes , or edits , misformed tyrosyl tRNA with its editing domain in the beta subunit . ^^^ We report the crystal structure of an N terminal fragment of the PheRS beta subunit ( PheRS beta ( N ) ) from the archaeon , Pyrococcus horikoshii , at 1 . 94 A resolution . ^^^ PheRS beta ( N ) includes the editing domain B3 / 4 , which has archaea / eukarya specific insertions / deletions and adopts a different orientation relative to other domains , as compared with that of bacterial PheRS . ^^^ We prepared Ala substituted mutants of P . horikoshii PheRS for 16 editing pocket residues , of which 12 are archaea / eukarya specific and four are more widely conserved . ^^^ First , the mutations of Leu 202 , Ser 211 , Asp 234 , and Thr 236 made the PheRS incorrectly hydrolyze the cognate Phe tRNA ( Phe ) , indicating that these residues participate in the Tyr hydroxy group recognition and are responsible for discrimination against Phe . ^^^ |
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