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Gene Review

glnS  -  glutamyl-tRNA synthetase

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK0668, JW0666
 
 
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Disease relevance of glnS

  • The location of the glnS gene within the 13.5-kilobase E. coli DNA transducing fragment was determined by genetic means [1].
 

High impact information on glnS

  • Mutations in glnS (the gene encoding GlnRS) that compensate for impaired aminoacylation were isolated by genetic selection [2].
  • Two glnS mutants were obtained by using opal suppressors differing in the nucleotides composing the base pair at 3.70: glnS113 with an Asp-235-->Asn change selected with GLNA3U70 (GLN carrying G3-->A and C70-->U changes), and glnS114 with a Gln-318-->Arg change selected with GLNU70 (GLN carrying a C70-->U change) [2].
  • 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 [3].
  • Glutaminyl-tRNA synthetase has been purified by a simple, two-column procedure from an Escherichia coli K12 strain carrying the glnS structural gene on plasmid pBR322 [4].
  • Oligopeptides scattered throughout the primary sequence of glutaminyl-tRNA synthetase were sequenced by the gas chromatographic-mass spectrometric method and matched to the theoretical peptides derived from the translated DNA sequence [4].
 

Chemical compound and disease context of glnS

 

Biological context of glnS

  • The glnS gene was recloned into plasmid pBR322 and its nucleotide sequence was established [1].
  • No further gene is found in this operon which in both organisms is directly adjacent to the gene glnS [8].
  • The single amino acid change responsible for the mischarging phenotype was identified at amino acid 235 in the translated glnS gene [6].
  • Its amino acid sequence and its gene (glnS) sequence are known [9].
  • Sequence data and evolutionary arguments suggest that a similarity may exist between the C-terminal end of glutaminyl-tRNA synthetase (GlnRS) and the catalytic domain of glutamine amidotransferases (GATs) [10].
 

Associations of glnS with chemical compounds

 

Regulatory relationships of glnS

  • glnS-lacZ fusions have been used to isolate mutations which enhance expression of the glnS gene [11].
 

Other interactions of glnS

 

Analytical, diagnostic and therapeutic context of glnS

References

  1. Escherichia coli glutaminyl-tRNA synthetase. I. Isolation and DNA sequence of the glnS gene. Yamao, F., Inokuchi, H., Cheung, A., Ozeki, H., Söll, D. J. Biol. Chem. (1982) [Pubmed]
  2. Functional communication in the recognition of tRNA by Escherichia coli glutaminyl-tRNA synthetase. Rogers, M.J., Adachi, T., Inokuchi, H., Söll, D. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  3. In vivo and in vitro transcription of the Escherichia coli glutaminyl-tRNA synthetase gene. Cheung, A.Y., Söll, D. J. Biol. Chem. (1984) [Pubmed]
  4. Escherichia coli glutaminyl-tRNA synthetase. II. Characterization of the glnS gene product. Hoben, P., Royal, N., Cheung, A., Yamao, F., Biemann, K., Söll, D. J. Biol. Chem. (1982) [Pubmed]
  5. Amino acid discrimination by a class I aminoacyl-tRNA synthetase specified by negative determinants. Bullock, T.L., Uter, N., Nissan, T.A., Perona, J.J. J. Mol. Biol. (2003) [Pubmed]
  6. Escherichia coli glutaminyl-tRNA synthetase: a single amino acid replacement relaxes rRNA specificity. Uemura, H., Conley, J., Yamao, F., Rogers, J., Söll, D. Protein Seq. Data Anal. (1988) [Pubmed]
  7. Characterization of a urea induced molten globule intermediate state of glutaminyl-tRNA synthetase from Escherichia coli. Das, B.K., Bhattacharyya, T., Roy, S. Biochemistry (1995) [Pubmed]
  8. Analysis of the nag regulon from Escherichia coli K12 and Klebsiella pneumoniae and of its regulation. Vogler, A.P., Lengeler, J.W. Mol. Gen. Genet. (1989) [Pubmed]
  9. Misaminoacylation by glutaminyl-tRNA synthetase: relaxed specificity in wild-type and mutant enzymes. Hoben, P., Uemura, H., Yamao, F., Cheung, A., Swanson, R., Sumner-Smith, M., Söll, D. Fed. Proc. (1984) [Pubmed]
  10. Origin of glutaminyl-tRNA synthetase: an example of palimpsest? Di Giulio, M. J. Mol. Evol. (1993) [Pubmed]
  11. Characterization of cis-acting mutations which increase expression of a glnS-lacZ fusion in Escherichia coli. Plumbridge, J., Söll, D. Mol. Gen. Genet. (1989) [Pubmed]
  12. Regulation of biosynthesis of aminoacyl-transfer RNA synthetases and of transfer-RNA in Escherichia coli. Morgan, S., Larossa, R., Cheung, A., Low, B., Söll, D. Arch. Biol. Med. Exp. (1979) [Pubmed]
  13. Site-directed mutagenesis to fine-tune enzyme specificity. Uemura, H., Rogers, M.J., Swanson, R., Watson, L., Söll, D. Protein Eng. (1988) [Pubmed]
 
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