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Originally published In Press as doi:10.1074/jbc.M109494200 on October 3, 2001

J. Biol. Chem., Vol. 276, Issue 49, 45862-45867, December 7, 2001
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A Single Amidotransferase Forms Asparaginyl-tRNA and Glutaminyl-tRNA in Chlamydia trachomatis*

Gregory RaczniakDagger §, Hubert D. BeckerDagger , Bokkee MinDagger , and Dieter SöllDagger ||**

From the Dagger  Department of Molecular Biophysics and Biochemistry and || Chemistry, Yale University, New Haven, Connecticut 06520-8114

Aminoacyl-tRNA is generally formed by aminoacyl-tRNA synthetases, a family of 20 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 18 synthetases, whereas 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 C. trachomatis employs the dual specificity gatCAB-encoded amidotransferase and 18 aminoacyl-tRNA synthetases to create the complete set of 20 aminoacyl-tRNAs.

* Supported by a grant from the NIGMS, National Institutes of Health.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ A predoctoral fellow of the Heyl Foundation. Present address: Eastern Virginia Medical School, 721 Fairfax Avenue, Norfolk, VA 23507-2000.

A European Molecular Biology postdoctoral fellow.

** To whom correspondence should be addressed: Dept. of Molecular Biophysics and Biochemistry, Yale University, P. O. Box 208114, 266 Whitney Ave., New Haven, CT 06520-8114. Tel.: 203-432-6200; Fax: 203-432-6202; E-mail: soll@trna.chem.yale.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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