pheT

Summary

Gene Symbol: pheT
Description: phenylalanine tRNA synthetase, beta subunit
Alias: ECK1711, JW1703
Species: Escherichia coli str. K-12 substr. MG1655

Top Publications

  1. Moor N, Repkova M, Yamkovoy V, Lavrik O. Alterations at the 3'-CCA end of Escherichia coli and Thermus thermophilus tRNA(Phe) do not abolish their acceptor activity. FEBS Lett. 1994;351:241-2 pubmed
    ..Nevertheless the CCA sequence at the 3'-end of tRNA(Phe) does not seem to be an absolute requirement for tRNA aminoacylation. ..
  2. Elseviers D, Gallagher P, Hoffman A, Weinberg B, Schwartz I. Molecular cloning and regulation of expression of the genes for initiation factor 3 and two aminoacyl-tRNA synthetases. J Bacteriol. 1982;152:357-62 pubmed
    ..The results suggest that the genes for initiation factor 3 and phenylalanyl- and threonyl-tRNA synthetase are regulated by different mechanisms. ..
  3. Peterson E, Pan T, Coleman J, Uhlenbeck O. In vitro selection of small RNAs that bind to Escherichia coli phenylalanyl-tRNA synthetase. J Mol Biol. 1994;242:186-92 pubmed
    ..This approach should assist in the detection of motifs that resemble tRNA, but are too dissimilar to be identified by sequence comparison. ..
  4. Springer M, Trudel M, Graffe M, Plumbridge J, Fayat G, Mayaux J, et al. Escherichia coli phenylalanyl-tRNA synthetase operon is controlled by attenuation in vivo. J Mol Biol. 1983;171:263-79 pubmed
    ..indicate that phenylalanyl-tRNA synthetase is controlled by attenuation in a way analogous to several amino acid biosynthetic operons. ..
  5. Holler E, Wang C, Ford N. Detection of ligand-induced conformational changes in phenylalanyl-tRNA synthetase of Escherichia coli K10 by laser light scattering. Biochemistry. 1981;20:861-7 pubmed
    ..It is established by comparison that of the two possible binding sites for each Mg2+ and tRNAPhe the diffusion constant reflects occupation of only a single class of sites. ..
  6. Baltzinger M, Holler E. Kinetics of acyl transfer ribonucleic acid complexes of Escherichia coli phenylalanyl-tRNA synthetase. A conformational change is rate limiting in catalysis. Biochemistry. 1982;21:2460-7 pubmed
    ..The reaction was bimolecular with rate constants of 50 microM-1 s-1 and 15 s-1 for association and dissociation, respectively. ..
  7. Mayaux J, Springer M, Graffe M, Fromant M, Fayat G. IS4 transposition in the attenuator region of the Escherichia coli pheS,T operon. Gene. 1984;30:137-46 pubmed
    ..171 (1983) 239-261; Springer et al., J. Mol. Biol. 171 (1983) 263-279]. The IS4 insertion site described here is compared to the other known sites and the effect of IS4 transposition on the expression of neighbouring genes is discussed. ..
  8. Yarus M. Phenylalanyl-tRNA synthetase and isoleucyl-tRNA Phe : a possible verification mechanism for aminoacyl-tRNA. Proc Natl Acad Sci U S A. 1972;69:1915-9 pubmed
    ..Thus, a common generalization needs to be modified: an amino acid is not necessarily committed to a given (incorrect) anticodon when it is incorporated into aminoacyl-tRNA. It may be possible to correct it thereafter. ..
  9. Hountondji C, Schmitter J, Beauvallet C, Blanquet S. Affinity labeling of Escherichia coli phenylalanyl-tRNA synthetase at the binding site for tRNAPhe. Biochemistry. 1987;26:5433-9 pubmed
    ..coli methionyl- and tyrosyl-tRNA synthetases [Hountondji, C., Dessen, P., & Blanquet, S. (1986) Biochimie 68, 1071-1078]. ..

More Information

Publications63

  1. Plumbridge J, Springer M. Genes for the two subunits of phenylalanyl-tRNA synthesis of Escherichia coli are transcribed from the same promoter. J Mol Biol. 1980;144:595-600 pubmed
  2. Khodyreva S, Moor N, Ankilova V, Lavrik O. Phenylalanyl-tRNA synthetase from E. coli MRE-600: analysis of the active site distribution on the enzyme subunits by affinity labelling. Biochim Biophys Acta. 1985;830:206-12 pubmed
    ..In our opinion, the catalytic center of tRNA aminoacylation is formed in the contact region of subunits, and the aminoacyl moiety is transferred into tRNA (from the alpha- into beta-subunit in the region of their contact). ..
  3. Kodama K, Fukuzawa S, Sakamoto K, Nakayama H, Kigawa T, Yabuki T, et al. A new protein engineering approach combining chemistry and biology, part I; site-specific incorporation of 4-iodo-L-phenylalanine in vitro by using misacylated suppressor tRNAPhe. Chembiochem. 2006;7:1577-81 pubmed
    ..coli cell-free system. Our approach will find wide application in protein engineering since an aryl iodide tag on proteins can be used for site-specific functionalization of proteins. ..
  4. Reeh S, Pedersen S, Neidhardt F. Transient rates of synthesis of five amionacyl-transfer ribonucleic acid synthetases during a shift-up of Escherichia coli. J Bacteriol. 1977;129:702-6 pubmed
  5. Mulivor R, Rappaport H. Analysis of the binding of phenylalanine to phenylalanyl-tRNA synthetase. J Mol Biol. 1973;76:123-34 pubmed
  6. Beyer D, Kroll H, Endermann R, Schiffer G, Siegel S, Bauser M, et al. New class of bacterial phenylalanyl-tRNA synthetase inhibitors with high potency and broad-spectrum activity. Antimicrob Agents Chemother. 2004;48:525-32 pubmed
    ..pneumoniae sepsis model in rats. Treatment with the phenyl-thiazolylurea-sulfonamides reduced the bacterial titer in various organs by up to 3 log units, supporting the potential value of Phe-RS as a target in antibacterial therapy. ..
  7. Mayaux J, Fayat G, Panvert M, Springer M, Grunberg Manago M, Blanquet S. Control of phenylalanyl-tRNA synthetase genetic expression. Site-directed mutagenesis of the pheS, T operon regulatory region in vitro. J Mol Biol. 1985;184:31-44 pubmed
  8. Trudel M, Springer M, Graffe M, Fayat G, Blanquet S, Grunberg Manago M. Regulation of E.coli phenylalanyl-tRNA synthetase operon in vivo. Biochim Biophys Acta. 1984;782:10-7 pubmed
    The phenylalanyl-tRNA synthetase operon is composed of two adjacent, cotranscribed genes, pheS and pheT, corresponding respectively to the small and large subunit of phenylalanyl-tRNA synthetase...
  9. Dessen P, Ducruix A, Hountondji C, May R, Blanquet S. Neutron scattering study of the binding of tRNAPhe to Escherichia coli phenylalanyl-tRNA synthetase. Biochemistry. 1983;22:281-4 pubmed
    ..Wang, C. C., & Ford, N.C., Jr. (1981) Biochemistry 20, 861-867] where the addition of either MgCl2 or tRNAPhe was shown to cause dramatic changes of the apparent translational diffusion constant of phenylalanyl-tRNA synthetase. ..
  10. Krauss G, Pingoud A, Boehme D, Riesner D, Peters F, Maas G. Equivalent and non-equivalent binding sites for tRNA on aminoacyl-tRNA synthetases. Eur J Biochem. 1975;55:517-29 pubmed
    ..The binding data are discussed with respect to the tertiary structure of the tRNAs, the subunit structure of the synthetases and the possible physical basis for the non-equivalence of binding sites. ..
  11. Wu T, Wood D, Stein P, Comer M. Transcription of a gene cluster coding for two aminoacyl-tRNA synthetases and an initiation factor in Escherichia coli. J Mol Biol. 1984;173:177-209 pubmed
    The alpha and beta subunits of phenylalanyl-tRNA synthetase are encoded by the pheS and pheT genes, respectively...
  12. Pages D, Buckingham R. Mutants of pheV in Escherichia coli affecting control by attenuation of the pheS, T and pheA operons. Two distinct mechanisms for de-attenuation. J Mol Biol. 1990;216:17-24 pubmed
  13. Springer M, Graffe M, Mayaux J, Dardel F, Fayat G, Blanquet S, et al. Open reading frames in the control regions of the phenylalanyl-tRNA synthetase operon of E. coli. Biochimie. 1987;69:1065-70 pubmed
    ..The present report shows that, in fact, the only open reading frame to be translated efficiently is the leader peptide itself. The alternative leader peptide and the terminator peptide are both translated at a negligible rate. ..
  14. Lagerkvist U, Akesson B, Brändén R. Aminoacyl adenylate, a normal intermediate or a dead end in aminoacylation of transfer ribonucleic acid. J Biol Chem. 1977;252:1002-6 pubmed
    ..With all five ligases the steady state rate of transfer from the preformed aminoacyl-adenylate complex to tRNA was approximately the same as that of the overall reaction. ..
  15. Roy H, Ling J, Irnov M, Ibba M. Post-transfer editing in vitro and in vivo by the beta subunit of phenylalanyl-tRNA synthetase. EMBO J. 2004;23:4639-48 pubmed
    ..This loss in aromatic amino-acid discrimination in vivo revealed that editing by phenylalanyl-tRNA synthetase is essential for faithful translation of the genetic code. ..
  16. Fayat G, Mayaux J, Sacerdot C, Fromant M, Springer M, Grunberg Manago M, et al. Escherichia coli phenylalanyl-tRNA synthetase operon region. Evidence for an attenuation mechanism. Identification of the gene for the ribosomal protein L20. J Mol Biol. 1983;171:239-61 pubmed
    The nucleotide sequences of pheS and of the beginning of pheT have been determined. The genes pheS and pheT code, respectively, for the small and large subunits of phenylalanyl-tRNA synthetase, an alpha 2 beta 2 enzyme...
  17. Cusack S, Hartlein M, Leberman R. Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases. Nucleic Acids Res. 1991;19:3489-98 pubmed
  18. Ibba M, Kast P, Hennecke H. Substrate specificity is determined by amino acid binding pocket size in Escherichia coli phenylalanyl-tRNA synthetase. Biochemistry. 1994;33:7107-12 pubmed
    ..Tyrosine activation was also improved with this mutant, but the resulting enzyme-Tyr-adenylate complex was rapidly hydrolyzed, indicating the presence of a proofreading mechanism in E. coli phenylalanyl-tRNA synthetase. ..
  19. Mechulam Y, Fayat G, Blanquet S. Sequence of the Escherichia coli pheST operon and identification of the himA gene. J Bacteriol. 1985;163:787-91 pubmed
    ..Another open reading frame (prp) was revealed downstream from pheT which was identified as himA, the gene for the alpha subunit of the integration host factor.
  20. Ibba M, Soll D. Aminoacyl-tRNA synthesis. Annu Rev Biochem. 2000;69:617-50 pubmed
    ..This article reviews current knowledge of the biochemical, structural, and evolutionary facets of aminoacyl-tRNA synthesis. ..
  21. Wilson R, Roe B. Presence of the hypermodified nucleotide N6-(delta 2-isopentenyl)-2-methylthioadenosine prevents codon misreading by Escherichia coli phenylalanyl-transfer RNA. Proc Natl Acad Sci U S A. 1989;86:409-13 pubmed
    ..The results of these experiments indicate that while ms2i6A is not required for normal aminoacylation of tRNAPhe, its presence stabilizes codon-anticodon interaction and thereby prevents misreading of the genetic code. ..
  22. Plumbridge J, Springer M. Escherichia coli phenylalanyl-tRNA synthetase operon: transcription studies of wild-type and mutated operons on multicopy plasmids. J Bacteriol. 1982;152:661-8 pubmed
    ..gene for threonyl-tRNA synthetase, thrS, and those for the two subunits of phenylalanyl-tRNA synthetases, pheS and pheT, is described...
  23. Ducruix A, Hounwanou N, Reinbolt J, Boulanger Y, Blanquet S. Purification and reversible subunit dissociation of overproduced Escherichia coli phenylalanyl-tRNA synthetase. Biochim Biophys Acta. 1983;741:244-50 pubmed
    ..from a 100-fold overproducing Escherichia coli strain carrying a hybrid pBR322 plasmid containing the pheS-pheT locus. The purified enzyme is identical to the phenylalanyl-tRNA synthetase isolated form an haploid strain...
  24. Danenberg P, Santi D. Inhibition of phenylalanyl-tRNA synthetase by aromatic guanidines and amidines. J Med Chem. 1975;18:528-30 pubmed
    ..Inhibition by these compounds appears to be specific for phenylalanyl-tRNA synthetase and requires the presence of a phenyl ring as well as the amidine or guanidine moiety. ..
  25. Vlassov V, Khodyreva S. Equilibrium screening-dialysis investigation of the nucleotide sequences in the tRNAPhe recognized by phenylalanyl-tRNA synthetase (Escherichia coli). FEBS Lett. 1978;96:95-8 pubmed
  26. Airas R. Magnesium dependence of the measured equilibrium constants of aminoacyl-tRNA synthetases. Biophys Chem. 2007;131:29-35 pubmed
    ..Thus Mg(2+) ions seem to have an active catalytic role, not only in the activation of the amino acid, but in the posttransfer steps of the aminoacyl-tRNA synthetase reaction, too. ..
  27. Eriani G, Delarue M, Poch O, Gangloff J, Moras D. Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. Nature. 1990;347:203-6 pubmed
    ..Surprisingly, this partition of aaRS in two classes is found to be strongly correlated on the functional level with the acylation occurring either on the 2' OH (class I) or 3' OH (class II) of the ribose of the last nucleotide of tRNA. ..
  28. Plumbridge J, Springer M, Graffe M, Goursot R, Grunberg Manago M. Physical localisation and cloning of the structural gene for E. coli initiation factor IF3 from a group of genes concerned with translation. Gene. 1980;11:33-42 pubmed
    ..One plasmid, containing a 3.3 kb PstI fragment inserted into pBR322, does not code for any of the synthetase genes but causes strains carrying it to overproduce IF3. ..
  29. Neidhardt F, Bloch P, Pedersen S, Reeh S. Chemical measurement of steady-state levels of ten aminoacyl-transfer ribonucleic acid synthetases in Escherichia coli. J Bacteriol. 1977;129:378-87 pubmed
  30. Delamarche C, Vacher J, Buckingham R. Mutants affecting tRNA(Phe) from Escherichia coli. Studies of the suppression of thermosensitive phenylalanyl-tRNA synthetase. Eur J Biochem. 1987;168:365-9 pubmed
    ..This mutation, C(-6)----T(-6), restores expression of the mutant U2 to about the level of wild-type tRNA(Phe). ..
  31. Hennecke H. Use of mutant enzymes to demonstrate the presence of two active sites on phenylalanyl-tRNA synthetase from Eschericia coli. FEBS Lett. 1976;72:182-6 pubmed
  32. Airas R. Differences in the magnesium dependences of the class I and class II aminoacyl-tRNA synthetases from Escherichia coli. Eur J Biochem. 1996;240:223-31 pubmed
    ..The binding of ATP to the E. aminoacyl-tRNA complex also speeds up the dissociation of the aminoacyl-tRNA from most of these enzymes. ..
  33. Gavini N, Pulakat L. The tRNA species for redundant genetic codons NNU and NNC. A thought on the absence of phenylalanine tRNA with AAA anticodon in Escherichia coli. J Biol Chem. 1992;267:2240-3 pubmed
    ..coli. ..
  34. Gabius H, von der Haar F, Cramer F. Evolutionary aspects of accuracy of phenylalanyl-tRNA synthetase. A comparative study with enzymes from Escherichia coli, Saccharomyces cerevisiae, Neurospora crassa, and turkey liver using phenylalanine analogues. Biochemistry. 1983;22:2331-9 pubmed
  35. Fayat G, Fromant M, Kalogerakos T, Blanquet S. Effect of the overproduction of phenylalanyl- and threonyl-tRNA synthetases on tRNAPhe and tRNAThr concentrations in E. coli cells. Biochimie. 1983;65:221-5 pubmed
    ..The answer is that the levels of these tRNAs are not changed by selective increase of the cognate synthetases. ..
  36. Peterson E, Uhlenbeck O. Determination of recognition nucleotides for Escherichia coli phenylalanyl-tRNA synthetase. Biochemistry. 1992;31:10380-9 pubmed
    ..However, recognition of the tRNA central core nucleotides is unique to E. coli FRS.(ABSTRACT TRUNCATED AT 250 WORDS) ..
  37. Comer M, Bock A. Genes for the alpha and beta subunits of the phenylalanyl-transfer ribonucleic acid synthetase of Escherichia coli. J Bacteriol. 1976;127:923-33 pubmed
    ..The gene order, as determined by transduction is aroD-pps-pheT-pheS. The pheS and pheT genes are close together and may be immediately adjacent.
  38. Ankilova V, Vlassov V, Knorre D, Melamed N, Nuzdihna N. Involvement of the D-stem of tRNAPhe (E. coli) in interaction with phenylalanyl-tRNA synthetase as shown by chemical modification. FEBS Lett. 1975;60:168-71 pubmed
  39. Mayaux J, Blanquet S. Binding of zinc to Escherichia coli phenylalanyl transfer ribonucleic acid synthetase. Comparison with other aminoacyl transfer ribonucleic acid synthetases. Biochemistry. 1981;20:4647-54 pubmed
  40. Pallanck L, Schulman L. Anticodon-dependent aminoacylation of a noncognate tRNA with isoleucine, valine, and phenylalanine in vivo. Proc Natl Acad Sci U S A. 1991;88:3872-6 pubmed
  41. Lavrik O, Moor N, Khodyreva S. Phenylalanyl-tRNA synthetase from E. coli MRE-600: localization of the phenylalanine binding sites on the subunits by affinity reagents. Mol Biol Rep. 1982;8:123-6 pubmed
    ..Transfer of the aminoacyl moiety from the alpha subunit to the beta subunit of the enzyme was assumed to take place in the process of catalysis of the aminoacylation reaction. ..
  42. Springer M, Plumbridge J, Trudel M, Graffe M, Grunberg Manago M. Transcription units around the gene for E. coli translation initiation factor IF3 (infC). Mol Gen Genet. 1982;186:247-52 pubmed
    ..It also shows that the two genes following infC, namely pheS and pheT, which form the phenylalanyl-tRNA synthetase operon, are not expressed from infC's promoter...
  43. Peterson E, Blank J, Sprinzl M, Uhlenbeck O. Selection for active E. coli tRNA(Phe) variants from a randomized library using two proteins. EMBO J. 1993;12:2959-67 pubmed
    ..Finally, the potency of this method is illustrated by the identification of a second class of variants that was isolated by virtue of the presence of an impurity in the FRS preparation. ..
  44. Fayat G, Blanquet S, Dessen P, Batelier G, Waller J. The molecular weight and subunit composition of phenylalanyl-tRNA synthetase from Escherichia coli K-12. Biochimie. 1974;56:35-41 pubmed
  45. Bartmann P, Hanke T, Holler E. Active site stoichiometry of L-phenylalanine: tRNA ligase from Escherichia coli K(-10). J Biol Chem. 1975;250:7668-74 pubmed
    ..Furthermore, it was observed that the activated amino acid could be transferred from both sites to cognate tRNA. ..
  46. Vacher J, Springer M, Buckingham R. Functional mutants of phenylalanine transfer RNA from Escherichia coli. EMBO J. 1985;4:509-13 pubmed
    ..One hypothesis for the mechanism of de-attenuation is that mutant tRNAPhe molecules compete with the wild-type tRNAPhe on the ribosome but are inefficient at some step in the elongation process. ..
  47. Hecht S, Hawrelak S. Interaction of glycyl-L-phenylalanine with Escherichia coli phenylalanyl-tRNA synthetase. Biochemistry. 1974;13:4967-75 pubmed
  48. Wertheimer S, Klotsky R, Schwartz I. Transcriptional patterns for the thrS-infC-rplT operon of Escherichia coli. Gene. 1988;63:309-20 pubmed
  49. Springer M, Mayaux J, Fayat G, Plumbridge J, Graffe M, Blanquet S, et al. Attenuation control of the Escherichia coli phenylalanyl-tRNA synthetase operon. J Mol Biol. 1985;181:467-78 pubmed
    ..The pheST operon is also shown to be derepressed by a cellular excess of phenylalanyl-tRNA synthetase. This derepression is shown to be due to the pheST attenuator. ..
  50. Khan A, Roe B. Aminoacylation of synthetic DNAs corresponding to Escherichia coli phenylalanine and lysine tRNAs. Science. 1988;241:74-9 pubmed
    ..The aminoacylation of synthetic tDNAs demonstrates that the ribose backbone of a tRNA is not absolutely required for tRNA aminoacylation. ..
  51. Mechulam Y, Blanquet S, Fayat G. Dual level control of the Escherichia coli pheST-himA operon expression. tRNA(Phe)-dependent attenuation and transcriptional operator-repressor control by himA and the SOS network. J Mol Biol. 1987;197:453-70 pubmed
    ..the himA gene, encoding the alpha-subunit of integration host factor, was recognized immediately downstream from pheT, possibly forming part of the same transcriptional unit...
  52. Favre A, Ballini J, Holler E. Phenylalanyl-tRNA synthetase induced conformational change of Escherichia coli tRNA phe. Biochemistry. 1979;18:2887-95 pubmed
  53. Baltzinger M, Holler E. Catalytic mechanism of phenylalanyl-tRNA synthetase of Escherichia coli K10. Conformational change and tRNAPhe phenylalanylation are concerted. Biochemistry. 1982;21:2467-76 pubmed
    ..amp; Holler, E. (1979) Biochemistry 18, 2028-2038]. ..
  54. Bobkova E, Mashanov Golikov A, Wolfson A, Ankilova V, Lavrik O. Comparative study of subunits of phenylalanyl-tRNA synthetase from Escherichia coli and Thermus thermophilus. FEBS Lett. 1991;290:95-8 pubmed
    ..Alpha-subunits displayed a distinctly different pH dependence of the surface charge. A spatial model of the oligomeric structure and a putative mechanism for its formation are discussed. ..