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A single amidotransferase forms amide aminoacyl-tRNAs in Chlamydia trachomatis

Record Type:	Electronic resources : Monograph/item
Title/Author:	A single amidotransferase forms amide aminoacyl-tRNAs in Chlamydia trachomatis
Author:	Raczniak, Gregory Aaron.
Description:	113 p.
Notes:	Director: Dieter Soll.
Notes:	Source: Dissertation Abstracts International, Volume: 65-03, Section: B, page: 1310.
Contained By:	Dissertation Abstracts International65-03B.
Subject:	Biology, Molecular.
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3125289
ISBN:	0496725793

A single amidotransferase forms amide aminoacyl-tRNAs in Chlamydia trachomatis
Raczniak, Gregory Aaron.

A single amidotransferase forms amide aminoacyl-tRNAs in Chlamydia trachomatis [electronic resource] - 113 p.

Director: Dieter Soll.

Thesis (Ph.D.)--Yale University, 2004.

Aminoacyl-tRNA is generally formed by aminoacyl-tRNA synthetases, a family of twenty conserved 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 tRNA Gln species. A preparation of pure heterotrimeric recombinant amidotransferase converted both 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 ATP and GTP. These results suggest that C. trachomatis employs the dual-specificity gatCAB-encoded amidotransferase and eighteen aminoacyl-tRNA synthetases to provide the complete set of twenty aminoacyl-tRNAs required for protein synthesis.

ISBN: 0496725793Subjects--Topical Terms:

226919
Biology, Molecular.

A single amidotransferase forms amide aminoacyl-tRNAs in Chlamydia trachomatis
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520 # $a Aminoacyl-tRNA is generally formed by aminoacyl-tRNA synthetases, a family of twenty conserved 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 tRNA Gln species. A preparation of pure heterotrimeric recombinant amidotransferase converted both 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 ATP and GTP. These results suggest that C. trachomatis employs the dual-specificity gatCAB-encoded amidotransferase and eighteen aminoacyl-tRNA synthetases to provide the complete set of twenty aminoacyl-tRNAs required for protein synthesis.
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