Genomes and Genes
Gene Symbol: gltX
Description: glutamyl-tRNA synthetase
Alias: ECK2394, JW2395
Species: Escherichia coli str. K-12 substr. MG1655
- Lapointe J, Delcuve G. Thermosensitive mutants of Escherichia coli K-12 altered in the catalytic Subunit and in a Regulatory factor of the glutamy-transfer ribonucleic acid synthetase. J Bacteriol. 1975;122:352-8 pubmed..GluRS) of a partial revertants (ts plus or minus) of the thermosensitive (ts) mutant strain JP1449 (LOcus gltx) and of a ts mutant strain EM111-ts1 with a lesion in or near the locus gltx have been studied to find the relation ..
- Sherman J, Rogers M, Soll D. Competition of aminoacyl-tRNA synthetases for tRNA ensures the accuracy of aminoacylation. Nucleic Acids Res. 1992;20:2847-52 pubmed..In addition, we show that the discriminator base (position 73) and the first base of the anticodon are important for recognition by E. coli tyrosyl-tRNA synthetase. ..
- Powers D, Ginsburg A. Monomeric structure of glutamyl-tRNA synthetase in Escherichia coli. Arch Biochem Biophys. 1978;191:673-9 pubmed
- Kern D, Lapointe J. The catalytic mechanism of glutamyl-tRNA synthetase of Escherichia coli. Evidence for a two-step aminoacylation pathway, and study of the reactivity of the intermediate complex. Eur J Biochem. 1980;106:137-50 pubmed
- Brun Y, Sanfaçon H, Breton R, Lapointe J. Closely spaced and divergent promoters for an aminoacyl-tRNA synthetase gene and a tRNA operon in Escherichia coli. Transcriptional and post-transcriptional regulation of gltX, valU and alaW. J Mol Biol. 1990;214:845-64 pubmedThe transcription of the gltX gene encoding the glutamyl-tRNA synthetase and of the adjacent valU and alaW tRNA operons of Escherichia coli K-12 has been studied...
- Kaplan S, Atherly A, Barrett A. Synthesis of stable RNA in stringent Escherichia coli cells in the absence of charged transfer RNA. Proc Natl Acad Sci U S A. 1973;70:689-92 pubmed..In this regard tetracycline and the "relaxed" gene product appear to be analogous. ..
- 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
- Sylvers L, Rogers K, Shimizu M, Ohtsuka E, Soll D. A 2-thiouridine derivative in tRNAGlu is a positive determinant for aminoacylation by Escherichia coli glutamyl-tRNA synthetase. Biochemistry. 1993;32:3836-41 pubmed..coli GluRS. This is only the second example of a tRNA modification acting as a positive determinant for interaction with its cognate aminoacyl-tRNA synthetase. ..
- Lapointe J, Soll D. Glutamyl transfer ribonucleic acid synthetase of Escherichia coli. II. Interaction with intact glutamyl transfer ribonucleic acid. J Biol Chem. 1972;247:4975-81 pubmed
- Liu J, Lin S, Blochet J, Pezolet M, Lapointe J. The glutamyl-tRNA synthetase of Escherichia coli contains one atom of zinc essential for its native conformation and its catalytic activity. Biochemistry. 1993;32:11390-6 pubmed..coli. ..
- Russell R, Pittard A. Mutants of Escherichia coli unable to make protein at 42 C. J Bacteriol. 1971;108:790-8 pubmed..Another mutant has been shown to possess a temperature-sensitive tryptophanyl-transfer ribonucleic acid synthetase, but this is not responsible for inability to grow at 42 C on media containing tryptophan. ..
- Kern D, Lapointe J. The glutamyl-tRNA synthetase of Escherichia coli: substrate-induced protection against its thermal inactivation. Nucleic Acids Res. 1979;7:501-15 pubmed..The protection constants determined from this study are similar to the dissociation constants determined by direct binding experiments and to the Km values determined kinetically. ..
- Lin S, Brisson A, Liu J, Roy P, Lapointe J. Higher specific activity of the Escherichia coli glutamyl-tRNA synthetase purified to homogeneity by a six-hour procedure. Protein Expr Purif. 1992;3:71-4 pubmed..This difference is discussed in relation to the generation of microheterogeneity in proteins during their purification. ..
- 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. ..
- Lapointe J, Soll D. Glutamyl transfer ribonucleic acid synthetase of Escherichia coli. I. Purification and properties. J Biol Chem. 1972;247:4966-74 pubmed
- Dubois D, Blais S, Huot J, Lapointe J. A C-truncated glutamyl-tRNA synthetase specific for tRNA(Glu) is stimulated by its free complementary distal domain: mechanistic and evolutionary implications. Biochemistry. 2009;48:6012-21 pubmed publisher..These results confirm the modular nature of GluRS and support the model of a "recent" fusion of domains 4 and 5 to a proto-GluRS containing the catalytic domain and able to recognize its tRNA substrate(s). ..
- Kern D, Potier S, Boulanger Y, Lapointe J. The monomeric glutamyl-tRNA synthetase of Escherichia coli. Purification and relation between its structural and catalytic properties. J Biol Chem. 1979;254:518-24 pubmed..A single sulfhydryl group of the native enzyme reacts with 5,5'-dithiobis(2-nitrobenzoic acid) causing no loss of enzymatic activity, whereas four such groups per enzyme react in the presence of 4 M guanidine HCl. ..
- Weygand Durasevic I, Schwob E, Soll D. Acceptor end binding domain interactions ensure correct aminoacylation of transfer RNA. Proc Natl Acad Sci U S A. 1993;90:2010-4 pubmed..Thus, the stability of the noncognate complex may be the basis for mischarging in vivo. ..
- Rogers K, Soll D. Discrimination among tRNAs intermediate in glutamate and glutamine acceptor identity. Biochemistry. 1993;32:14210-9 pubmed..The kinetic evaluation of the anticodon switch mutants suggests that overlap in anticodon recognition is avoided through specificity for the third anticodon position coupled with divergent preferences for the wobble base. ..
- Breton R, Sanfaçon H, Papayannopoulos I, Biemann K, Lapointe J. Glutamyl-tRNA synthetase of Escherichia coli. Isolation and primary structure of the gltX gene and homology with other aminoacyl-tRNA synthetases. J Biol Chem. 1986;261:10610-7 pubmedThe gltX gene encoding the glutamyl-tRNA synthetase of Escherichia coli and adjacent regulatory regions was isolated and sequenced. The structural gene encodes a protein of 471 amino acids whose molecular weight is 53,810...
- Hecht S, Chinualt A. Position of aminoacylation of individual Escherichia coli and yeast tRNAs. Proc Natl Acad Sci U S A. 1976;73:405-9 pubmed..The results indicate that the initial position of aminoacylation is not uniform for all tRNAs, although for individual tRNAs the specificity has been conserved during the evolution from a prokaryotic to eukaryotic organism. ..
- Sekine S, Nureki O, Tateno M, Yokoyama S. The identity determinants required for the discrimination between tRNAGlu and tRNAAsp by glutamyl-tRNA synthetase from Escherichia coli. Eur J Biochem. 1999;261:354-60 pubmed
- Kern D, Lapointe J. The catalytic mechanism of glutamyl-tRNA synthetase of Escherichia coli. A steady-state kinetic investigation. Eur J Biochem. 1981;115:29-38 pubmed..The results are discussed in the light of the two-step aminoacylation pathway catalyzed by this synthetase. ..
- Champagne N, Lapointe J. Influence of FIS on the transcription from closely spaced and non-overlapping divergent promoters for an aminoacyl-tRNA synthetase gene (gltX) and a tRNA operon (valU) in Escherichia coli. Mol Microbiol. 1998;27:1141-56 pubmedThe gltX gene, encoding the glutamyl-tRNA synthetase (GluRS), and the valU operon, whose transcripts contain three tRNAVal/UAC and one tRNALys/UUU, are adjacent and divergently transcribed...
- Kern D, Lapointe J. Catalytic mechanism of glutamyl-tRNA synthetase from Escherichia coli. Reaction pathway in the aminoacylation of tRNAGlu. Biochemistry. 1980;19:3060-8 pubmed
- Banerjee R, Dubois D, Gauthier J, Lin S, Roy S, Lapointe J. The zinc-binding site of a class I aminoacyl-tRNA synthetase is a SWIM domain that modulates amino acid binding via the tRNA acceptor arm. Eur J Biochem. 2004;271:724-33 pubmed
- Smith J, Daum H. Nucleotide sequence of the purM gene encoding 5'-phosphoribosyl-5-aminoimidazole synthetase of Escherichia coli K12. J Biol Chem. 1986;261:10632-6 pubmed..The presumptive purM promoter is located in this region, thus suggesting that both purine loci share a common mechanism of regulation mediated through this sequence. ..
- Kern D, Lapointe J. Glutamyl transfer ribonucleic acid synthetase of Escherichia coli. Effect of alteration of the 5-(methylaminomethyl)-2-thiouridine in the anticodon of glutamic acid transfer ribonucleic acid on the catalytic mechanism. Biochemistry. 1979;18:5819-26 pubmed
- Núñez H, Lefimil C, Min B, Soll D, Orellana O. In vivo formation of glutamyl-tRNA(Gln) in Escherichia coli by heterologous glutamyl-tRNA synthetases. FEBS Lett. 2004;557:133-5 pubmed..Testing the capacity to complement a thermosensitive E. coli gltX mutant and to suppress an E. coli trpA49 missense mutant we examined the properties of heterologous gltX genes...
- Brun Y, Breton R, Lanouette P, Lapointe J. Precise mapping and comparison of two evolutionarily related regions of the Escherichia coli K-12 chromosome. Evolution of valU and lysT from an ancestral tRNA operon. J Mol Biol. 1990;214:825-43 pubmedTwo tRNA operons have been found near the gltX gene encoding the glutamyl-tRNA synthetase of Escherichia coli K-12...
- Gustilo E, Dubois D, Lapointe J, Agris P. E. coli glutamyl-tRNA synthetase is inhibited by anticodon stem-loop domains and a minihelix. RNA Biol. 2007;4:85-92 pubmed..Thus, the RNA constructs are effective tools to study RNA-protein interaction. ..
- Lapointe J, Soll D. Glutamyl transfer ribonucleic acid synthetase of Escherichia coli. 3. Influence of the 46K protein on the affinity of the 56K glutamyl transfer ribonucleic acid synthetase for its substrates. J Biol Chem. 1972;247:4982-5 pubmed
- Madore E, Lipman R, Hou Y, Lapointe J. Evidence for unfolding of the single-stranded GCCA 3'-End of a tRNA on its aminoacyl-tRNA synthetase from a stacked helical to a foldback conformation. Biochemistry. 2000;39:6791-8 pubmed
- Nureki O, Tateno M, Niimi T, Kohno T, Muramatsu T, Kanno H, et al. Mechanisms of molecular recognition of tRNAs by aminoacyl-tRNA synthetases. Nucleic Acids Symp Ser. 1991;:165-6 pubmed..These results indicate that the two tRNAs, unlike other tRNAs studied so far, have some of the "identity determinants" in the D-stem and/or in the anticodon stem. ..
- Madore E, Florentz C, Giege R, Sekine S, Yokoyama S, Lapointe J. Effect of modified nucleotides on Escherichia coli tRNAGlu structure and on its aminoacylation by glutamyl-tRNA synthetase. Predominant and distinct roles of the mnm5 and s2 modifications of U34. Eur J Biochem. 1999;266:1128-35 pubmed
- Sanfaçon H, Levasseur S, Roy P, Lapointe J. Cloning of the gene for Escherichia coli glutamyl-tRNA synthetase. Gene. 1983;22:175-80 pubmed..A physical map of the plasmid, which contains an insert of about 2.7 kb in length, is presented. ..
- Landes C, Perona J, Brunie S, Rould M, Zelwer C, Steitz T, et al. A structure-based multiple sequence alignment of all class I aminoacyl-tRNA synthetases. Biochimie. 1995;77:194-203 pubmed..The alignments also indicate that the class I synthetases may be partitioned into two subgroups: a) MetRS, IleRS, LeuRS, ValRS, CysRS and ArgRS; b) GlnRS, GluRS, TyrRS and TrpRS. ..
- Krüger M, Sørensen M. Aminoacylation of hypomodified tRNAGlu in vivo. J Mol Biol. 1998;284:609-20 pubmed..This is the minimal estimate because the turn-over rate of Glu-tRNAGlu was also reduced in the absence of the 2-thio group. Lack of either modification did not affect mischarging or mistranslation. ..
- Freist W, Gauss D, Soll D, Lapointe J. Glutamyl-tRNA sythetase. Biol Chem. 1997;378:1313-29 pubmed..Besides interactions between the enzyme and the acceptor stem and the anticodon of tRNA(Glu), checking of the dihydrouridine arm and of the variable loop by GluRS are documented. ..
- Brun Y, Lapointe J. Locations of genes in the 52-minute region on the physical map of Escherichia coli K-12. J Bacteriol. 1990;172:4746-7 pubmed
- Dasgupta S, Saha R, Dey C, Banerjee R, Roy S, Basu G. The role of the catalytic domain of E. coli GluRS in tRNAGln discrimination. FEBS Lett. 2009;583:2114-20 pubmed publisher..coli tRNA(Gln). Our results demonstrate that in addition to the anticodon-binding domain, tRNA(Gln) discriminatory elements may be present in the catalytic domain in E. coli GluRS as well. ..
- Liu J, Gagnon Y, Gauthier J, Furenlid L, L Heureux P, Auger M, et al. The zinc-binding site of Escherichia coli glutamyl-tRNA synthetase is located in the acceptor-binding domain. Studies by extended x-ray absorption fine structure, molecular modeling, and site-directed mutagenesis. J Biol Chem. 1995;270:15162-9 pubmed..coli glutaminyl-tRNA synthetase, supports this conclusion and suggests that the 98C-127H segment does not have the characteristics of the classical zinc fingers. ..
- Kern D, Lapointe J. The catalytic mechanism of the glutamyl-tRNA synthetase from Escherichia coli. Detection of an intermediate complex in which glutamate is activated. J Biol Chem. 1980;255:1956-61 pubmed..The AMP-dependent and PPi-independent deacylation of Glu-tRNAGlu is the rate-limiting step of the reverse of the AMP- and PPi-dependent deacylation. ..
- Sherman J, Rogers K, Rogers M, Soll D. Synthetase competition and tRNA context determine the in vivo identify of tRNA discriminator mutants. J Mol Biol. 1992;228:1055-62 pubmed..The identity of a tRNA in vivo is determined by competition among aminoacyl-tRNA synthetases, which is in turn modulated by the nucleotide substitution as well as the tRNA context. ..