Abstract
Aminoacyl-tRNA synthetases specifically charge tRNAs with their cognate amino acids. A prototype for the most complex aminoacyl-tRNA synthetases is the four-subunit glycyl-tRNA synthetase from Escherichia coli, encoded by two open reading frames. We examined the glycyl-tRNA synthetase gene from Chlamydia trachomatis, a genetically isolated bacterium, and identified only a single open reading frame for the chlamydial homolog (glyQS). This is the first report of a prokaryotic glycyl-tRNA synthetase encoded by a single gene.
Full Text
The Full Text of this article is available as a PDF (318.8 KB).
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Allen J. E., Locksley R. M., Stephens R. S. A single peptide from the major outer membrane protein of Chlamydia trachomatis elicits T cell help for the production of antibodies to protective determinants. J Immunol. 1991 Jul 15;147(2):674–679. [PubMed] [Google Scholar]
- Becker Y. The chlamydia: molecular biology of procaryotic obligate parasites of eucaryocytes. Microbiol Rev. 1978 Jun;42(2):274–306. doi: 10.1128/mr.42.2.274-306.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Calendar R., Berg P. Purification and physical characterization of tyrosyl ribonucleic acid synthetases from Escherichia coli and Bacillus subtilis. Biochemistry. 1966 May;5(5):1681–1690. doi: 10.1021/bi00869a033. [DOI] [PubMed] [Google Scholar]
- Cusack S., Härtlein M., Leberman R. Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases. Nucleic Acids Res. 1991 Jul 11;19(13):3489–3498. doi: 10.1093/nar/19.13.3489. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Devereux J., Haeberli P., Smithies O. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 1984 Jan 11;12(1 Pt 1):387–395. doi: 10.1093/nar/12.1part1.387. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ge Q., Trieu E. P., Targoff I. N. Primary structure and functional expression of human Glycyl-tRNA synthetase, an autoantigen in myositis. J Biol Chem. 1994 Nov 18;269(46):28790–28797. [PubMed] [Google Scholar]
- Gerloff R. K., Ritter D. B., Watson R. O. Studies on thermal denaturation of DNA from various chlamydiae. J Infect Dis. 1970 Jan;121(1):65–69. doi: 10.1093/infdis/121.1.65. [DOI] [PubMed] [Google Scholar]
- Giegé R., Puglisi J. D., Florentz C. tRNA structure and aminoacylation efficiency. Prog Nucleic Acid Res Mol Biol. 1993;45:129–206. doi: 10.1016/s0079-6603(08)60869-7. [DOI] [PubMed] [Google Scholar]
- Hackstadt T., Todd W. J., Caldwell H. D. Disulfide-mediated interactions of the chlamydial major outer membrane protein: role in the differentiation of chlamydiae? J Bacteriol. 1985 Jan;161(1):25–31. doi: 10.1128/jb.161.1.25-31.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hanke T., Bartmann P., Hennecke H., Kosakowski H. M., Jaenicke R., Holler E., Böck A. L-phenylalanyl-tRNA synthetase of Escherichia coli K-10. A reinvestigation of molecular weight and subunit structure. Eur J Biochem. 1974 Apr 16;43(3):601–607. doi: 10.1111/j.1432-1033.1974.tb03447.x. [DOI] [PubMed] [Google Scholar]
- Keng T., Webster T. A., Sauer R. T., Schimmel P. Gene for Escherichia coli glycyl-tRNA synthetase has tandem subunit coding regions in the same reading frame. J Biol Chem. 1982 Nov 10;257(21):12503–12508. [PubMed] [Google Scholar]
- Kingsbury D. T., Weiss E. Lack of deoxyribonucleic acid homology between species of the genus Chlamydia. J Bacteriol. 1968 Oct;96(4):1421–1423. doi: 10.1128/jb.96.4.1421-1423.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Nada S., Chang P. K., Dignam J. D. Primary structure of the gene for glycyl-tRNA synthetase from Bombyx mori. J Biol Chem. 1993 Apr 15;268(11):7660–7667. [PubMed] [Google Scholar]
- Newhall W. J., 5th Biosynthesis and disulfide cross-linking of outer membrane components during the growth cycle of Chlamydia trachomatis. Infect Immun. 1987 Jan;55(1):162–168. doi: 10.1128/iai.55.1.162-168.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ostrem D. L., Berg P. Glycyl transfer ribonucleic acid synthetase from Escherichia coli: purification, properties, and substrate binding. Biochemistry. 1974 Mar 26;13(7):1338–1348. doi: 10.1021/bi00704a006. [DOI] [PubMed] [Google Scholar]
- Peterson E. T., Uhlenbeck O. C. Determination of recognition nucleotides for Escherichia coli phenylalanyl-tRNA synthetase. Biochemistry. 1992 Oct 27;31(42):10380–10389. doi: 10.1021/bi00157a028. [DOI] [PubMed] [Google Scholar]
- Putney S. D., Sauer R. T., Schimmel P. R. Purification and properties of alanine tRNA synthetase from Escherichia coli A tetramer of identical subunits. J Biol Chem. 1981 Jan 10;256(1):198–204. [PubMed] [Google Scholar]
- Riley M. Functions of the gene products of Escherichia coli. Microbiol Rev. 1993 Dec;57(4):862–952. doi: 10.1128/mr.57.4.862-952.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Saks M. E., Sampson J. R., Abelson J. N. The transfer RNA identity problem: a search for rules. Science. 1994 Jan 14;263(5144):191–197. doi: 10.1126/science.7506844. [DOI] [PubMed] [Google Scholar]
- Schimmel P. R., Söll D. Aminoacyl-tRNA synthetases: general features and recognition of transfer RNAs. Annu Rev Biochem. 1979;48:601–648. doi: 10.1146/annurev.bi.48.070179.003125. [DOI] [PubMed] [Google Scholar]
- Shiba K., Schimmel P., Motegi H., Noda T. Human glycyl-tRNA synthetase. Wide divergence of primary structure from bacterial counterpart and species-specific aminoacylation. J Biol Chem. 1994 Nov 25;269(47):30049–30055. [PubMed] [Google Scholar]
- Smith D. B., Johnson K. S. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene. 1988 Jul 15;67(1):31–40. doi: 10.1016/0378-1119(88)90005-4. [DOI] [PubMed] [Google Scholar]
- Stephens R. S., Mullenbach G., Sanchez-Pescador R., Agabian N. Sequence analysis of the major outer membrane protein gene from Chlamydia trachomatis serovar L2. J Bacteriol. 1986 Dec;168(3):1277–1282. doi: 10.1128/jb.168.3.1277-1282.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Toth M. J., Schimmel P. Deletions in the large (beta) subunit of a hetero-oligomeric aminoacyl-tRNA synthetase. J Biol Chem. 1990 Jan 15;265(2):1000–1004. [PubMed] [Google Scholar]
- Toth M. J., Schimmel P. Internal structural features of E. coli glycyl-tRNA synthetase examined by subunit polypeptide chain fusions. J Biol Chem. 1986 May 25;261(15):6643–6646. [PubMed] [Google Scholar]
- Wagar E. A., Pang M. The gene for the S7 ribosomal protein of Chlamydia trachomatis: characterization within the chlamydial str operon. Mol Microbiol. 1992 Feb;6(3):327–335. [PubMed] [Google Scholar]
- Wagar E. A., Schachter J., Bavoil P., Stephens R. S. Differential human serologic response to two 60,000 molecular weight Chlamydia trachomatis antigens. J Infect Dis. 1990 Oct;162(4):922–927. doi: 10.1093/infdis/162.4.922. [DOI] [PubMed] [Google Scholar]
- Waller J. -P., Risler J. -L., Monteilhet C., Zelwer C. Crystallisation of trypsin-modified methionyl-tRNA synthetase from Escherichia coli. FEBS Lett. 1971 Aug 15;16(3):186–188. doi: 10.1016/0014-5793(71)80128-x. [DOI] [PubMed] [Google Scholar]
- Webster T. A., Gibson B. W., Keng T., Biemann K., Schimmel P. Primary structures of both subunits of Escherichia coli glycyl-tRNA synthetase. J Biol Chem. 1983 Sep 10;258(17):10637–10641. [PubMed] [Google Scholar]
- Weisburg W. G., Hatch T. P., Woese C. R. Eubacterial origin of chlamydiae. J Bacteriol. 1986 Aug;167(2):570–574. doi: 10.1128/jb.167.2.570-574.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Wichlan D. G., Hatch T. P. Identification of an early-stage gene of Chlamydia psittaci 6BC. J Bacteriol. 1993 May;175(10):2936–2942. doi: 10.1128/jb.175.10.2936-2942.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Winter G., Fersht A. R., Wilkinson A. J., Zoller M., Smith M. Redesigning enzyme structure by site-directed mutagenesis: tyrosyl tRNA synthetase and ATP binding. Nature. 1982 Oct 21;299(5885):756–758. doi: 10.1038/299756a0. [DOI] [PubMed] [Google Scholar]
