Genomes and Genes
Gene Symbol: thrS
Description: threonyl-tRNA synthetase
Alias: ECK1717, JW1709
Species: Escherichia coli str. K-12 substr. MG1655
- Fröhler J, Rechenmacher A, Thomale J, Nass G, Bock A. Genetic analysis of mutations causing borrelidin resistance by overproduction of threonyl-transfer ribonucleic acid synthetase. J Bacteriol. 1980;143:1135-41 pubmed..The regulatory mutations were closely linked to the treonyl-transfer ribonucleic acid synthetase structural gene (thrS), located clockwise to it...
- 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. ..
- Ruan B, Palioura S, Sabina J, Marvin Guy L, Kochhar S, LaRossa R, et al. Quality control despite mistranslation caused by an ambiguous genetic code. Proc Natl Acad Sci U S A. 2008;105:16502-7 pubmed publisher..In this way, E. coli ensures the presence of sufficient functional protein albeit at a considerable energetic cost. ..
- Hennecke H, Bock A, Thomale J, Nass G. Threonyl-transfer ribonucleic acid synthetase from Escherichia coli: subunit structure and genetic analysis of the structural gene by means of a mutated enzyme and of a specialized transducing lambda bacteriophage. J Bacteriol. 1977;131:943-50 pubmed..for resistance against the antibiotic borrelidin, was used to map the position of the ThrRS structural gene (thrS) by P1 transductions...
- Paetz W, Nass G. Biochemical and immunological characterization of threonyl-tRNA synthetase of two borrelidin-resistant mutants of Escherichia coli K12. Eur J Biochem. 1973;35:331-7 pubmed
- 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..This study shows that infC is expressed independently of the promoter of the threonyl-tRNA synthetase (thrS), which is the genes immediately preceding infC...
- Moine H, Romby P, Springer M, Grunberg Manago M, Ebel J, Ehresmann B, et al. Escherichia coli threonyl-tRNA synthetase and tRNA(Thr) modulate the binding of the ribosome to the translational initiation site of the thrS mRNA. J Mol Biol. 1990;216:299-310 pubmed..This repression/derepression double control allows precise adjustment of the rate of synthesis of threonyl-tRNA synthetase to the tRNA level in the cell. ..
- 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..These genes are clustered closely together with the genes for threonyl-tRNA synthetase (thrS) and translation initiation factor IF3 (infC); the gene order is thrS infC pheS pheT...
- Sankaranarayanan R, Dock Bregeon A, Rees B, Bovee M, Caillet J, Romby P, et al. Zinc ion mediated amino acid discrimination by threonyl-tRNA synthetase. Nat Struct Biol. 2000;7:461-5 pubmed publisher..This study demonstrates that the zinc ion is neither strictly catalytic nor structural and suggests how the zinc ion ensures that only amino acids that possess a hydroxyl group attached to the beta-position are activated...
- Johnson E, Cohen G, Saint Girons I. Threonyl-transfer ribonucleic acid synthetase and the regulation of the threonine operon in Escherichia coli. J Bacteriol. 1977;129:66-70 pubmed..The gene, called thrS, coding for threonyl-tRNA synthetase was located around 30 min on the E. coli map...
- Comer M, Dondon J, Graffe M, Yarchuk O, Springer M. Growth rate-dependent control, feedback regulation and steady-state mRNA levels of the threonyl-tRNA synthetase gene of Escherichia coli. J Mol Biol. 1996;261:108-24 pubmedThe expression of the gene thrS encoding threonyl-tRNA synthetase is under the control of two apparently different regulatory loops: translational feedback regulation and growth rate-dependent control...
- Springer M, Graffe M, Butler J, Grunberg Manago M. Genetic definition of the translational operator of the threonine-tRNA ligase gene in Escherichia coli. Proc Natl Acad Sci U S A. 1986;83:4384-8 pubmedThe Escherichia coli gene thrS that codes for threonine-tRNA ligase (tRNAThr ligase, formerly threonine-tRNA synthetase, EC 18.104.22.168) has previously been shown to be negatively autoregulated at the level of translation...
- Schulman L, Pelka H. An anticodon change switches the identity of E. coli tRNA(mMet) from methionine to threonine. Nucleic Acids Res. 1990;18:285-9 pubmed..These results indicate that the anticodon is the major element which determines the identity of both threonine and methionine tRNAs. ..
- Nogueira T, de Smit M, Graffe M, Springer M. The relationship between translational control and mRNA degradation for the Escherichia coli threonyl-tRNA synthetase gene. J Mol Biol. 2001;310:709-22 pubmedExpression of thrS, the gene encoding Escherichia coli threonyl-tRNA synthetase, is negatively autoregulated at the translational level...
- Wada M, Sekine K, Itikawa H. Participation of the dnaK and dnaJ gene products in phosphorylation of glutaminyl-tRNA synthetase and threonyl-tRNA synthetase of Escherichia coli K-12. J Bacteriol. 1986;168:213-20 pubmed
- Springer M, Graffe M, Dondon J, Grunberg Manago M, Romby P, Ehresmann B, et al. Translational control in E. coli: the case of threonyl-tRNA synthetase. Biosci Rep. 1988;8:619-32 pubmedGenetic studies have shown that expression of the E. coli threonyl-tRNA synthetase (thrS) gene is negatively auto-regulated at the translational level...
- Nass G, Poralla K, Zahner H. Effect of the antibiotic Borrelidin on the regulation of threonine biosynthetic enzymes in E. coli. Biochem Biophys Res Commun. 1969;34:84-91 pubmed
- 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..Further evidence is provided for this model by the features of pheS, T regulation in vivo (see the accompanying paper). ..
- Maloy S, Stewart V. Autogenous regulation of gene expression. J Bacteriol. 1993;175:307-16 pubmed
- Brunel C, Caillet J, Lesage P, Graffe M, Dondon J, Moine H, et al. Domains of the Escherichia coli threonyl-tRNA synthetase translational operator and their relation to threonine tRNA isoacceptors. J Mol Biol. 1992;227:621-34 pubmedThe expression of the gene for threonyl-tRNA synthetase (thrS) is negatively autoregulated at the translational level in Escherichia coli...
- 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. ..
- Butler J, Springer M, Dondon J, Grunberg Manago M. Posttranscriptional autoregulation of Escherichia coli threonyl tRNA synthetase expression in vivo. J Bacteriol. 1986;165:198-203 pubmedFive mutations in thrS, the gene for threonyl-tRNA synthetase, have been characterized, and the sites of the mutations have been localized to different regions of the thrS gene by recombination with M13 phage carrying portions of the thrS ..
- Mayaux J, Fayat G, Fromant M, Springer M, Grunberg Manago M, Blanquet S. Structural and transcriptional evidence for related thrS and infC expression. Proc Natl Acad Sci U S A. 1983;80:6152-6 pubmedThe nucleotide sequence of thrS, the gene encoding dimeric Escherichia coli threonyl-tRNA synthetase [L-threonine:tRNAThr ligase (AMP forming), 22.214.171.124], has been determined...
- 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. ..
- Hasegawa T, Miyano M, Himeno H, Sano Y, Kimura K, Shimizu M. Identity determinants of E. coli threonine tRNA. Biochem Biophys Res Commun. 1992;184:478-84 pubmed..coli tRNA(THR) for threonyl-tRNA synthetase. Discriminator base, A73, is not involved in threonine charging activity. ..
- Springer M, Plumbridge J, Butler J, Graffe M, Dondon J, Mayaux J, et al. Autogenous control of Escherichia coli threonyl-tRNA synthetase expression in vivo. J Mol Biol. 1985;185:93-104 pubmedThe regulation of the expression of thrS, the structural gene for threonyl-tRNA synthetase, was studied using several thrS-lac fusions cloned in lambda and integrated as single copies at att lambda...
- Torres Larios A, Dock Bregeon A, Romby P, Rees B, Sankaranarayanan R, Caillet J, et al. Structural basis of translational control by Escherichia coli threonyl tRNA synthetase. Nat Struct Biol. 2002;9:343-7 pubmed..The finding of other thrS operators that have this conserved motif leads to a generalization of this regulatory mechanism to a subset of Gram-..
- Sankaranarayanan R, Dock Bregeon A, Romby P, Caillet J, Springer M, Rees B, et al. The structure of threonyl-tRNA synthetase-tRNA(Thr) complex enlightens its repressor activity and reveals an essential zinc ion in the active site. Cell. 1999;97:371-81 pubmed..A zinc ion found in the active site is implicated in amino acid recognition/discrimination...
- Dock Bregeon A, Sankaranarayanan R, Romby P, Caillet J, Springer M, Rees B, et al. Transfer RNA-mediated editing in threonyl-tRNA synthetase. The class II solution to the double discrimination problem. Cell. 2000;103:877-84 pubmed..As a consequence, the editing mechanism of both classes of synthetases can be described as mirror images, as already seen for tRNA binding and amino acid activation. ..
- Bovee M, Pierce M, Francklyn C. Induced fit and kinetic mechanism of adenylation catalyzed by Escherichia coli threonyl-tRNA synthetase. Biochemistry. 2003;42:15102-13 pubmed..Here, a pre-steady state kinetic analysis of the ThRS-catalyzed adenylation reaction was carried out by monitoring changes in intrinsic tryptophan fluorescence...
- Sacerdot C, Caillet J, Graffe M, Eyermann F, Ehresmann B, Ehresmann C, et al. The Escherichia coli threonyl-tRNA synthetase gene contains a split ribosomal binding site interrupted by a hairpin structure that is essential for autoregulation. Mol Microbiol. 1998;29:1077-90 pubmed..Using a combination of in vivo and in vitro approaches, we show here that the ribosome binds to thrS mRNA at two non-contiguous sites: region -12 to +16 comprising the SD sequence and the AUG codon and, unexpectedly, ..
- Minajigi A, Francklyn C. Aminoacyl transfer rate dictates choice of editing pathway in threonyl-tRNA synthetase. J Biol Chem. 2010;285:23810-7 pubmed publisher..Thus, the relative contributions of pre- and post-transfer editing in ThrRS are subject to modulation by the rate of aminoacyl transfer. ..
- Graffe M, Dondon J, Caillet J, Romby P, Ehresmann C, Ehresmann B, et al. The specificity of translational control switched with transfer RNA identity rules. Science. 1992;255:994-6 pubmed..This identity swap in the leader messenger RNA indicates that tRNA identity rules may be extended to interactions of synthetases with other RNAs. ..
- Nass G, Thomale J. Alteration of structure of level of threonyl-tRNA-synthetase in Borrelidin resistant mutants of E. coli. FEBS Lett. 1974;39:182-6 pubmed
- Brunel C, Romby P, Moine H, Caillet J, Grunberg Manago M, Springer M, et al. Translational regulation of the Escherichia coli threonyl-tRNA synthetase gene: structural and functional importance of the thrS operator domains. Biochimie. 1993;75:1167-79 pubmed..It should serve as an articulation to provide an appropriate spacing between domains 2 and 4. Furthermore, it is possibly involved in ribosome binding. ..
- 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
- 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. ..
- Romby P, Springer M. Bacterial translational control at atomic resolution. Trends Genet. 2003;19:155-61 pubmed..The data also give some clues about how the binding of the synthetase to its mRNA inhibits translation. ..
- Caillet J, Nogueira T, Masquida B, Winter F, Graffe M, Dock Bregeon A, et al. The modular structure of Escherichia coli threonyl-tRNA synthetase as both an enzyme and a regulator of gene expression. Mol Microbiol. 2003;47:961-74 pubmed..Based on these results, and recent structural data, we have constructed a computer-derived molecular model for the operator-threonyl-tRNA synthetase complex, which sheds light on several essential aspects of the regulatory mechanism. ..
- Moine H, Romby P, Springer M, Grunberg Manago M, Ebel J, Ehresmann C, et al. Messenger RNA structure and gene regulation at the translational level in Escherichia coli: the case of threonine:tRNAThr ligase. Proc Natl Acad Sci U S A. 1988;85:7892-6 pubmed..Previous work showed that the expression of the Escherichia coli threonine:tRNAThr ligase (EC 126.96.36.199)-encoding gene (thrS) is negatively autoregulated at the translational level and that a region called the operator that is located ..
- Musier Forsyth K, Beuning P. Role of zinc ion in translational accuracy becomes crystal clear. Nat Struct Biol. 2000;7:435-6 pubmed
- Bedouelle H. Symmetrical interactions between the translational operator of the thrS gene and dimeric threonyl transfer RNA synthetase. J Mol Biol. 1993;230:704-8 pubmedThreonyl-tRNA synthetase from Escherichia coli represses the translation of its coding gene, thrS, by binding an operator located in the leader region of its messenger RNA...
- Nureki O, Kohno T, Sakamoto K, Miyazawa T, Yokoyama S. Chemical modification and mutagenesis studies on zinc binding of aminoacyl-tRNA synthetases. J Biol Chem. 1993;268:15368-73 pubmed..These results indicate that the Zn(2+)-binding sequences are important for catalysis and recognition in the aminoacylation reactions of a subgroup of aminoacyl-tRNA synthetases. ..
- Theobald A, Springer M, Grunberg Manago M, Ebel J, Giege R. Tertiary structure of Escherichia coli tRNA(3Thr) in solution and interaction of this tRNA with the cognate threonyl-tRNA synthetase. Eur J Biochem. 1988;175:511-24 pubmed..These data are discussed in the light of the tRNA/synthetase recognition problem and of the structural and functional properties of the tRNA-like structure present in the operator region of the thrS mRNA.
- Lestienne P, Plumbridge J, Grunberg Manago M, Blanquet S. Autogenous repression of Escherichia coli threonyl-tRNA synthetase expression in vitro. J Biol Chem. 1984;259:5232-7 pubmed..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 ..
- Mans R, Pleij C, Bosch L. tRNA-like structures. Structure, function and evolutionary significance. Eur J Biochem. 1991;201:303-24 pubmed
- Caillet J, Graffe M, Eyermann F, Romby P, Springer M. Mutations in residues involved in zinc binding in the catalytic site of Escherichia coli threonyl-tRNA synthetase confer a dominant lethal phenotype. J Bacteriol. 2007;189:6839-48 pubmed..Overproduction of the inactive enzyme represses the expression of the wild-type chromosomal copy of the gene to an extent incompatible with bacterial growth. ..
- 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..The construction of three lambda bacteriophages containing parts of the structural gene for threonyl-tRNA synthetase, thrS, and those for the two subunits of phenylalanyl-tRNA synthetases, pheS and pheT, is described...
- Torres Larios A, Sankaranarayanan R, Rees B, Dock Bregeon A, Moras D. Conformational movements and cooperativity upon amino acid, ATP and tRNA binding in threonyl-tRNA synthetase. J Mol Biol. 2003;331:201-11 pubmed..The structural analysis suggests that, while the small substrates can bind in any order, they must be in place before productive tRNA binding can occur. ..
- Ruan B, Bovee M, Sacher M, Stathopoulos C, Poralla K, Francklyn C, et al. A unique hydrophobic cluster near the active site contributes to differences in borrelidin inhibition among threonyl-tRNA synthetases. J Biol Chem. 2005;280:571-7 pubmed publisher..g. Helicobacter pylori). This study illustrates how one class of natural product inhibitors affects aminoacyl-tRNA synthetase function, providing potentially useful information for structure-based inhibitor design...
- Kim C, Han K, Ryu K, Kim B, Kim K, Choi S, et al. N-terminal domains of native multidomain proteins have the potential to assist de novo folding of their downstream domains in vivo by acting as solubility enhancers. Protein Sci. 2007;16:635-43 pubmed..The solubilizing ability of N-terminal domains would contribute to the autonomous folding of multidomain proteins in vivo, and based on these results, we propose a model of how N-terminal domains solubilize their downstream domains. ..
- Romby P, Brunel C, Caillet J, Springer M, Grunberg Manago M, Westhof E, et al. Molecular mimicry in translational control of E. coli threonyl-tRNA synthetase gene. Competitive inhibition in tRNA aminoacylation and operator-repressor recognition switch using tRNA identity rules. Nucleic Acids Res. 1992;20:5633-40 pubmed..The present data demonstrate that the anticodon-like sequence is one major determinant for the identity of the operator and the regulation specificity. It further shows that the tRNA-like operator obeys to tRNA identity rules. ..
- Springer M, Graffe M, Dondon J, Grunberg Manago M. tRNA-like structures and gene regulation at the translational level: a case of molecular mimicry in Escherichia coli. EMBO J. 1989;8:2417-24 pubmed