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Papers In Press, published online ahead of print October 3, 2001
Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114
Corresponding Author: soll{at}trna.chem.yale.edu
Aminoacyl-tRNA is generally formed by aminoacyl-tRNA synthetases, a family of twenty enzymes essential for accurate protein synthesis. However, most bacteria generate one of the two amide aminoacyl-tRNAs, Asn-tRNA or Gln-tRNA, by transamidation of mischarged Asp-tRNAAsn or Glu-tRNAGln catalyzed by a heterotrimeric amidotransferase (encoded by the gatA, gatB and gatC genes). The Chlamydia trachomatis genome sequence reveals genes for eighteen synthetases while those for asparaginyl-tRNA synthetase and glutaminyl-tRNA synthetase are absent. Yet the genome harbors three gat genes in an operon-like arrangement (gatCAB). We reasoned that Chlamydia uses the gatCAB-encoded amidotransferase to generate both Asn-tRNA and Gln-tRNA. C. trachomatis aspartyl-tRNA synthetase and glutamyl-tRNA synthetase were shown to be non-discriminating synthetases that form the misacylated tRNAAsn and tRNAGln species. A preparation of pure heterotrimeric recombinant C. trachomatis amidotransferase converted Asp-tRNAAsn and Glu-tRNAGln into Asn-tRNA and Gln-tRNA, respectively. The enzyme used glutamine, asparagine or ammonia as amide donors in the presence of either ATP or GTP. These results suggest that Chlamydia trachomatis employs the dual-specificity gatCAB-encoded amidotransferase and eighteen aminoacyl-tRNA synthetases to create the complete set of twenty aminoacyl-tRNAs.
J. Biol. Chem, 10.1074/jbc.M109494200
Submitted on October 2, 2001
Revised on October 3, 2001
Accepted on October 3, 2001
A single amidotransferase forms asparaginyl-tRNA and glutaminyl-tRNA in Chlamydia trachomatis
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