glutaminyl tRNA synthetase


Gene Symbol: glutaminyl tRNA synthetase
Description: glutamyl-tRNA synthetase
Alias: ECK0668, JW0666
Species: Escherichia coli str. K-12 substr. MG1655

Top Publications

  1. Hayase Y, Jahn M, Rogers M, Sylvers L, Koizumi M, Inoue H, et al. Recognition of bases in Escherichia coli tRNA(Gln) by glutaminyl-tRNA synthetase: a complete identity set. EMBO J. 1992;11:4159-65 pubmed
    ..In addition, the interaction of G2, G3 and G10 with GlnRS via the 2-amino group is significant for tRNA discrimination. Based on these results, and on earlier data, we propose a complete set of bases as identity elements for tRNA(Gln). ..
  2. Ibba M, Hong K, Sherman J, Sever S, Soll D. Interactions between tRNA identity nucleotides and their recognition sites in glutaminyl-tRNA synthetase determine the cognate amino acid affinity of the enzyme. Proc Natl Acad Sci U S A. 1996;93:6953-8 pubmed
    ..The ability of tRNA to optimize amino acid recognition reveals a novel mechanism for maintaining translational fidelity and also provides a strong basis for the coevolution of tRNAs and their cognate synthetases. ..
  3. Rould M, Perona J, Steitz T. Structural basis of anticodon loop recognition by glutaminyl-tRNA synthetase. Nature. 1991;352:213-8 pubmed
    ..These interactions suggest that the entire anticodon loop provides essential sites for glutaminyl tRNA synthetase discrimination among tRNA molecules.
  4. Chang C, Lin G, Chen S, Chiu W, Chen W, Wang C. Promoting the formation of an active synthetase/tRNA complex by a nonspecific tRNA-binding domain. J Biol Chem. 2008;283:30699-706 pubmed publisher
    ..These results not only underscore the significance of nonspecific tRNA binding in aminoacylation, but also provide insights into the mechanism of the formation of aminoacyl-tRNAs. ..
  5. Kitabatake M, Ibba M, Hong K, Soll D, Inokuchi H. Genetic analysis of functional connectivity between substrate recognition domains of Escherichia coli glutaminyl-tRNA synthetase. Mol Gen Genet. 1996;252:717-22 pubmed
  6. Englisch Peters S, Conley J, Plumbridge J, Leptak C, Soll D, Rogers M. Mutant enzymes and tRNAs as probes of the glutaminyl-tRNA synthetase: tRNA(Gln) interaction. Biochimie. 1991;73:1501-8 pubmed
    ..This correlates with the classification of GlnRS as a class I aminoacyl-tRNA synthetase. Mutations in tRNA(Gln) are discussed which affect the recognition of GlnRS and the current concept of glutamine identity in E coli is reviewed. ..
  7. Rogers M, Weygand Durasevic I, Schwob E, Sherman J, Rogers K, Adachi T, et al. Selectivity and specificity in the recognition of tRNA by E coli glutaminyl-tRNA synthetase. Biochimie. 1993;75:1083-90 pubmed
  8. Folk W. Molecular weighr of Escherichia coli glutaminyl transfer ribonucleic acid synthetase, and isolation of its complex with glutamine transfer ribonucleic acid. Biochemistry. 1971;10:1728-32 pubmed
  9. Uter N, Gruic Sovulj I, Perona J. Amino acid-dependent transfer RNA affinity in a class I aminoacyl-tRNA synthetase. J Biol Chem. 2005;280:23966-77 pubmed

More Information


  1. Rould M, Perona J, Soll D, Steitz T. Structure of E. coli glutaminyl-tRNA synthetase complexed with tRNA(Gln) and ATP at 2.8 A resolution. Science. 1989;246:1135-42 pubmed
    ..The central domain of this synthetase binds ATP, glutamine, and the acceptor end of the tRNA as well as making specific interactions with the acceptor stem.2+t is ..
  2. Rogers M, Adachi T, Inokuchi H, Soll D. Functional communication in the recognition of tRNA by Escherichia coli glutaminyl-tRNA synthetase. Proc Natl Acad Sci U S A. 1994;91:291-5 pubmed
    ..The GlnRS mutants isolated suggest that perturbation of the interactions with the inside of the tRNA L shape results in relaxed anticodon recognition. ..
  3. Inokuchi H, Hoben P, Yamao F, Ozeki H, Soll D. Transfer RNA mischarging mediated by a mutant Escherichia coli glutaminyl-tRNA synthetase. Proc Natl Acad Sci U S A. 1984;81:5076-80 pubmed
    ..This is an example of mischarging phenotype conferred by a mutation in an aminoacyl-tRNA synthetase gene; the results are discussed in the context of earlier genetic studies with mutant tRNAs. ..
  4. Arnez J, Steitz T. Crystal structures of three misacylating mutants of Escherichia coli glutaminyl-tRNA synthetase complexed with tRNA(Gln) and ATP. Biochemistry. 1996;35:14725-33 pubmed
    ..In contrast, the change of Ile129 to Thr in GlnRS15 causes virtually no change in the structure of the complex, and the explanation for its ability to misacylate supF is unclear. ..
  5. Ibba M, Thomann H, Hong K, Sherman J, Weygand Durasevic I, Sever S, et al. Substrate selection by aminoacyl-tRNA synthetases. Nucleic Acids Symp Ser. 1995;:40-2 pubmed
  6. Hong K, Ibba M, Weygand Durasevic I, Rogers M, Thomann H, Soll D. Transfer RNA-dependent cognate amino acid recognition by an aminoacyl-tRNA synthetase. EMBO J. 1996;15:1983-91 pubmed
    ..The observed role of RNA as a cofactor in optimizing amino acid activation suggests that the tRNAGln-GlnRS complex may be partly analogous to ribonucleoprotein enzymes where protein-RNA interactions facilitate catalysis. ..
  7. Sherman J, Soll D. Aminoacyl-tRNA synthetases optimize both cognate tRNA recognition and discrimination against noncognate tRNAs. Biochemistry. 1996;35:601-7 pubmed
    ..On the basis of these results, we suggest that the aminoacyl-tRNA synthetases have evolved to balance cognate tRNA recognition and discrimination against noncognate tRNAs. ..
  8. Lloyd A, Thomann H, Ibba M, Soll D. A broadly applicable continuous spectrophotometric assay for measuring aminoacyl-tRNA synthetase activity. Nucleic Acids Res. 1995;23:2886-92 pubmed
    ..Finally, this novel method was used to provide direct evidence for the cooperativity of tRNA and ATP binding to GlnRS. ..
  9. Sherman J, Thomann H, Soll D. Functional connectivity between tRNA binding domains in glutaminyl-tRNA synthetase. J Mol Biol. 1996;256:818-28 pubmed
  10. Cheung A, Soll D. In vivo and in vitro transcription of the Escherichia coli glutaminyl-tRNA synthetase gene. J Biol Chem. 1984;259:9953-8 pubmed
    ..In vitro transcription of glnS is not autogenously regulated by glutaminyl-tRNA synthetase and glutamine; it is also not affected by the presence of tRNA. ..
  11. Wright D, Martinis S, Jahn M, Soll D, Schimmel P. Acceptor stem and anticodon RNA hairpin helix interactions with glutamine tRNA synthetase. Biochimie. 1993;75:1041-9 pubmed
    ..Thus, transduction of the anticodon identity signal may require covalent continuity of the tRNA chain to trigger efficient aminoacylation. ..
  12. 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. ..
  13. Mayer C, Köhrer C, Kenny E, Prusko C, RajBhandary U. Anticodon sequence mutants of Escherichia coli initiator tRNA: effects of overproduction of aminoacyl-tRNA synthetases, methionyl-tRNA formyltransferase, and initiation factor 2 on activity in initiation. Biochemistry. 2003;42:4787-99 pubmed
    ..Other results suggest that the C1xA72 base pair mismatch, unique to eubacterial and organellar initiator tRNAs, may also be important for the binding of fAA-tRNA to IF2. ..
  14. Perona J, Rould M, Steitz T. Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase. Biochemistry. 1993;32:8758-71 pubmed
    ..Catalytic competence of the crystalline enzyme is directly shown by its ability to hydrolyze ATP and release pyrophosphate when crystals of the ternary complex are soaked in mother liquor containing glutamine. ..
  15. Mandal A, Samaddar S, Banerjee R, Lahiri S, Bhattacharyya A, Roy S. Glutamate counteracts the denaturing effect of urea through its effect on the denatured state. J Biol Chem. 2003;278:36077-84 pubmed
    ..For example, glycine betaine counteracts urea denaturation of tubulin but promotes denaturation of S228N lambda-repressor and carbonic anhydrase. Osmolyte counteraction of urea denaturation depends on osmolyte-protein pair. ..
  16. Uter N, Perona J. Long-range intramolecular signaling in a tRNA synthetase complex revealed by pre-steady-state kinetics. Proc Natl Acad Sci U S A. 2004;101:14396-401 pubmed
  17. Sathyapriya R, Vishveshwara S. Structure networks of E. coli glutaminyl-tRNA synthetase: effects of ligand binding. Proteins. 2007;68:541-50 pubmed
    ..coli GlnRS. The formalism used in this study is simple and can be applied to other protein-ligands in general to understand the allosteric changes mediated by the binding of ligands. ..
  18. Corigliano E, Perona J. Architectural underpinnings of the genetic code for glutamine. Biochemistry. 2009;48:676-87 pubmed publisher
    ..Calculations of electrostatic surface potential in the active site further suggest that a complementary electrostatic environment is also an important determinant of glutamine binding. ..
  19. 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. ..
  20. Arnez J, Steitz T. Crystal structure of unmodified tRNA(Gln) complexed with glutaminyl-tRNA synthetase and ATP suggests a possible role for pseudo-uridines in stabilization of RNA structure. Biochemistry. 1994;33:7560-7 pubmed
    ..An identical water-bridging structure is possible at four of the five other psuedo-uridines in known tRNA structures. ..
  21. Weygand Durasevic I, Rogers M, Soll D. Connecting anticodon recognition with the active site of Escherichia coli glutaminyl-tRNA synthetase. J Mol Biol. 1994;240:111-8 pubmed
    ..Therefore, at least two pathways of communication have been identified in the accurate recognition of tRNA by GlnRS. ..
  22. Balg C, Blais S, Bernier S, Huot J, Couture M, Lapointe J, et al. Synthesis of beta-ketophosphonate analogs of glutamyl and glutaminyl adenylate, and selective inhibition of the corresponding bacterial aminoacyl-tRNA synthetases. Bioorg Med Chem. 2007;15:295-304 pubmed
  23. Schwob E, Soll D. Selection of a 'minimal' glutaminyl-tRNA synthetase and the evolution of class I synthetases. EMBO J. 1993;12:5201-8 pubmed
  24. Perona J, Swanson R, Rould M, Steitz T, Soll D. Structural basis for misaminoacylation by mutant E. coli glutaminyl-tRNA synthetase enzymes. Science. 1989;246:1152-4 pubmed
    ..These results identify specific areas in the structure of the complex that are critical to accurate tRNA discrimination by GlnRS. ..
  25. Hoben P, Royal N, Cheung A, Yamao F, Biemann K, Soll D. Escherichia coli glutaminyl-tRNA synthetase. II. Characterization of the glnS gene product. J Biol Chem. 1982;257:11644-50 pubmed
    ..A single homologous region is shared by at least three of the synthetases examined here. ..
  26. Cheung A, Watson L, Soll D. Two control systems modulate the level of glutaminyl-tRNA synthetase in Escherichia coli. J Bacteriol. 1985;161:212-8 pubmed
    ..Thus, glnS appears to be regulated by two different control systems affecting transcription. Furthermore, our results suggest post-transcriptional regulation of glutaminyl-tRNA synthetase. ..
  27. Rath V, Silvian L, Beijer B, Sproat B, Steitz T. How glutaminyl-tRNA synthetase selects glutamine. Structure. 1998;6:439-49 pubmed
    ..The prior binding of tRNAGln that is required for amino acid activation may result from the terminal nucleotide, A76, packing against and orienting Tyr211, which forms part of the amino acid binding site. ..
  28. Freist W, Gauss D, Ibba M, Soll D. Glutaminyl-tRNA synthetase. Biol Chem. 1997;378:1103-17 pubmed
  29. Gruic Sovulj I, Uter N, Bullock T, Perona J. tRNA-dependent aminoacyl-adenylate hydrolysis by a nonediting class I aminoacyl-tRNA synthetase. J Biol Chem. 2005;280:23978-86 pubmed
    ..Because glutaminyl-tRNA synthetase does not possess a spatially separate editing domain, these data demonstrate that a pre-transfer editing-like reaction can occur within the synthetic site of a class I tRNA synthetase. ..
  30. Chongdar N, Dasgupta S, Datta A, Basu G. Preliminary X-ray crystallographic analysis of an engineered glutamyl-tRNA synthetase from Escherichia coli. Acta Crystallogr F Struct Biol Commun. 2014;70:922-7 pubmed publisher
    ..Here, the design, expression, purification and crystallization of an engineered E. coli GluRS in which two surface residues were mutated to optimize crystal contacts are reported. ..
  31. Thomann H, Ibba M, Hong K, Soll D. Homologous expression and purification of mutants of an essential protein by reverse epitope-tagging. Biotechnology (N Y). 1996;14:50-5 pubmed
  32. Ibba M, Hong K, Soll D. Glutaminyl-tRNA synthetase: from genetics to molecular recognition. Genes Cells. 1996;1:421-7 pubmed
    ..This mechanism now provides a ready explanation as to why the majority of tRNA mischarging events, including those originally described over 25 years ago for GlnRS, impair cellular viability only to a limited degree. ..
  33. Kuriki Y. A nucleotide sequence in the translation start signal region is involved in heat shock-induced translation arrest in Escherichia coli. FEBS Lett. 1990;264:121-4 pubmed
    ..I conclude that the heat shock-induced depression of gene expression is an event taking place at the initiation of translation. ..
  34. Rogers M, Ohgi T, Plumbridge J, Soll D. Nucleotide sequences of the Escherichia coli nagE and nagB genes: the structural genes for the N-acetylglucosamine transport protein of the bacterial phosphoenolpyruvate: sugar phosphotransferase system and for glucosamine-6-phosphate deaminase. Gene. 1988;62:197-207 pubmed
    ..This supports the idea that these two transport and phosphorylation systems may have evolved from a common ancestral gene. ..
  35. McClain W, Schneider J, Gabriel K. Association of tRNA(Gln) acceptor identity with phosphate-sugar backbone interactions observed in the crystal structure of the Escherichia coli glutaminyl-tRNA synthetase-tRNA(Gln) complex. Biochimie. 1993;75:1125-36 pubmed
  36. 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
  37. Bullock T, Uter N, Nissan T, Perona J. Amino acid discrimination by a class I aminoacyl-tRNA synthetase specified by negative determinants. J Mol Biol. 2003;328:395-408 pubmed
    ..The poorly differentiated cognate amino acid-binding site in GlnRS may be a consequence of the late emergence of this enzyme from the eukaryotic lineage of glutamyl-tRNA synthetases. ..
  38. Beresten S, Jahn M, Soll D. Aminoacyl-tRNA synthetase-induced cleavage of tRNA. Nucleic Acids Res. 1992;20:1523-30 pubmed
    ..Our results show that the cleavage is synthetase-specific, that mutant and wild-type tRNA(Gln) species can assume a different conformation, and that modified nucleosides in tRNA enhance the structural stability of the molecule. ..
  39. Plumbridge J, Soll D. The effect of dam methylation on the expression of glnS in E. coli. Biochimie. 1987;69:539-41 pubmed
    ..In dam strains, the expression of glnS is enhanced 2.6-fold. A mutated form of the promoter has been isolated in which the dam methylation site is lost. Expression of this promoter is insensitive to dam methylation. ..
  40. Uter N, Perona J. Active-site assembly in glutaminyl-tRNA synthetase by tRNA-mediated induced fit. Biochemistry. 2006;45:6858-65 pubmed
  41. 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. ..
  42. Sherlin L, Perona J. tRNA-dependent active site assembly in a class I aminoacyl-tRNA synthetase. Structure. 2003;11:591-603 pubmed
  43. Rogers M, Adachi T, Inokuchi H, Soll D. Switching tRNA(Gln) identity from glutamine to tryptophan. Proc Natl Acad Sci U S A. 1992;89:3463-7 pubmed
    ..As the use of the UGA codon as tryptophan in mycoplasma and in yeast mitochondria is conserved, recognition of the UCA anticodon by TrpRS may also be maintained in evolution. ..
  44. Uemura H, Conley J, Yamao F, Rogers J, Soll D. Escherichia coli glutaminyl-tRNA synthetase: a single amino acid replacement relaxes rRNA specificity. Protein Seq Data Anal. 1988;1:479-85 pubmed
  45. Liu D, Magliery T, Schultz P. Characterization of an 'orthogonal' suppressor tRNA derived from E. coli tRNA2(Gln). Chem Biol. 1997;4:685-91 pubmed
    ..The observed correlation between the effects of mutations at very distinct regions of the GlnRS-tRNA and possibly the ribosomal/tRNA complexes may contribute in part to the fidelity of protein biosynthesis. ..
  46. Liu D, Magliery T, Pastrnak M, Schultz P. Engineering a tRNA and aminoacyl-tRNA synthetase for the site-specific incorporation of unnatural amino acids into proteins in vivo. Proc Natl Acad Sci U S A. 1997;94:10092-7 pubmed
    ..The mutant GlnRS and engineered tRNA also constitute a functional synthetase-tRNA pair in vivo. The nature of the GlnRS mutations, which occur both at the protein-tRNA interface and at sites further away, is discussed. ..
  47. Yamao F, Inokuchi H, Cheung A, Ozeki H, Soll D. Escherichia coli glutaminyl-tRNA synthetase. I. Isolation and DNA sequence of the glnS gene. J Biol Chem. 1982;257:11639-43 pubmed
    ..5-kilobase E. coli DNA transducing fragment was determined by genetic means. The glnS gene was recloned into plasmid pBR322 and its nucleotide sequence was established. The DNA sequence translates to a protein of 550 amino acids. ..
  48. Bullock T, Rodríguez Hernández A, Corigliano E, Perona J. A rationally engineered misacylating aminoacyl-tRNA synthetase. Proc Natl Acad Sci U S A. 2008;105:7428-33 pubmed publisher
    ..This role for tRNA may persist as a relic of primordial cells in which the evolution of the genetic code was driven by RNA-catalyzed amino acid-RNA pairing. ..
  49. Swanson R, Hoben P, Sumner Smith M, Uemura H, Watson L, Soll D. Accuracy of in vivo aminoacylation requires proper balance of tRNA and aminoacyl-tRNA synthetase. Science. 1988;242:1548-51 pubmed
    ..Thus, limits exist on the relative levels of tRNAs and aminoacyl-tRNA synthetases within a cell. ..
  50. Brombacher E, Dorel C, Zehnder A, Landini P. The curli biosynthesis regulator CsgD co-ordinates the expression of both positive and negative determinants for biofilm formation in Escherichia coli. Microbiology. 2003;149:2847-57 pubmed
    ..coli by contemporary activation of adhesion positive determinants (the curli-encoding csg operons and the product of the yaiC gene) and repression of negative effectors such as yagS and pepD. ..
  51. Bullock T, Sherlin L, Perona J. Tertiary core rearrangements in a tight binding transfer RNA aptamer. Nat Struct Biol. 2000;7:497-504 pubmed
    ..These data suggest that enhanced protein binding to a mutant globular RNA can arise from stabilization of RNA tertiary interactions rather than optimization of RNA-protein contacts. ..
  52. Sherlin L, Bullock T, Newberry K, Lipman R, Hou Y, Beijer B, et al. Influence of transfer RNA tertiary structure on aminoacylation efficiency by glutaminyl and cysteinyl-tRNA synthetases. J Mol Biol. 2000;299:431-46 pubmed
  53. Plumbridge J. Organisation of the Escherichia coli chromosome between genes glnS and glnU, V. Mol Gen Genet. 1987;209:618-20 pubmed
  54. Fukunaga J, Ohno S, Nishikawa K, Yokogawa T. A base pair at the bottom of the anticodon stem is reciprocally preferred for discrimination of cognate tRNAs by Escherichia coli lysyl- and glutaminyl-tRNA synthetases. Nucleic Acids Res. 2006;34:3181-8 pubmed
    ..coli lysyl- and glutaminyl-tRNA synthetases. ..
  55. Yamasaki S, Nakamura S, Terada T, Shimizu K. Mechanism of the difference in the binding affinity of E. coli tRNAGln to glutaminyl-tRNA synthetase caused by noninterface nucleotides in variable loop. Biophys J. 2007;92:192-200 pubmed
    ..We therefore concluded that the sequence difference in the variable loop caused the difference in the internal mobility of the tertiary core region tRNAs and led to the difference in the affinity to ARS through the entropy term. ..
  56. 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. ..
  57. Baick J, Yoon J, Namgoong S, Soll D, Kim S, Eom S, et al. Growth inhibition of Escherichia coli during heterologous expression of Bacillus subtilis glutamyl-tRNA synthetase that catalyzes the formation of mischarged glutamyl-tRNA1 Gln. J Microbiol. 2004;42:111-6 pubmed
    ..coli GlutRNA1 Gln, and converts it to the cognate Gln-tRNA1 Gln species. B. subtilis GluRS-dependent Glu-tRNA1 Gln formation may cause growth inhibition in the transformed E. coli strain, possibly due to abnormal protein synthesis. ..
  58. Liu J, Ibba M, Hong K, Soll D. The terminal adenosine of tRNA(Gln) mediates tRNA-dependent amino acid recognition by glutaminyl-tRNA synthetase. Biochemistry. 1998;37:9836-42 pubmed
    ..These data now show that Asp66, Tyr211 and Phe233 mediate tRNA-dependent cognate amino acid recognition via the invariant 3'-terminal adenosine of tRNA(Gln). ..
  59. Faxén M, Plumbridge J, Isaksson L. Codon choice and potential complementarity between mRNA downstream of the initiation codon and bases 1471-1480 in 16S ribosomal RNA affects expression of glnS. Nucleic Acids Res. 1991;19:5247-51 pubmed
    ..We also give evidence that supports the idea that the presence of rare codons near the beginning of the mRNA can affect expression. ..