| http://purl.uniprot.org/citations/11585842 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11585842 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11585842 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/11585842 | http://www.w3.org/2000/01/rdf-schema#comment | "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-tRNA(Asn) or Glu-tRNA(Gln) 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 tRNA(Asn) and tRNA(Gln) species. A preparation of pure heterotrimeric recombinant C. trachomatis amidotransferase converted Asp-tRNA(Asn) and Glu-tRNA(Gln) 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."xsd:string |
| http://purl.uniprot.org/citations/11585842 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/11585842 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/11585842 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m109494200"xsd:string |
| http://purl.uniprot.org/citations/11585842 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m109494200"xsd:string |
| http://purl.uniprot.org/citations/11585842 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11585842 |
| http://purl.uniprot.org/citations/11585842 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11585842 |
| http://purl.uniprot.org/citations/11585842 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11585842 |
| http://purl.uniprot.org/citations/11585842 | http://purl.uniprot.org/core/author | "Min B."xsd:string |
| http://purl.uniprot.org/citations/11585842 | http://purl.uniprot.org/core/author | "Min B."xsd:string |
| http://purl.uniprot.org/citations/11585842 | http://purl.uniprot.org/core/author | "Soll D."xsd:string |
| http://purl.uniprot.org/citations/11585842 | http://purl.uniprot.org/core/author | "Soll D."xsd:string |
| http://purl.uniprot.org/citations/11585842 | http://purl.uniprot.org/core/author | "Raczniak G."xsd:string |
| http://purl.uniprot.org/citations/11585842 | http://purl.uniprot.org/core/author | "Raczniak G."xsd:string |
| http://purl.uniprot.org/citations/11585842 | http://purl.uniprot.org/core/author | "Becker H.D."xsd:string |
| http://purl.uniprot.org/citations/11585842 | http://purl.uniprot.org/core/author | "Becker H.D."xsd:string |
| http://purl.uniprot.org/citations/11585842 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
| http://purl.uniprot.org/citations/11585842 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
| http://purl.uniprot.org/citations/11585842 | http://purl.uniprot.org/core/pages | "45862-45867"xsd:string |
| http://purl.uniprot.org/citations/11585842 | http://purl.uniprot.org/core/pages | "45862-45867"xsd:string |
| http://purl.uniprot.org/citations/11585842 | http://purl.uniprot.org/core/title | "A single amidotransferase forms asparaginyl-tRNA and glutaminyl-tRNA in Chlamydia trachomatis."xsd:string |
| http://purl.uniprot.org/citations/11585842 | http://purl.uniprot.org/core/title | "A single amidotransferase forms asparaginyl-tRNA and glutaminyl-tRNA in Chlamydia trachomatis."xsd:string |