Glu-tRNAGln amidotransferase: A novel heterotrimeric enzyme required for correct decoding of glutamine codons during translation

The three genes, gatC , gatA , and gatB , which constitute the transcriptional unit of the Bacillus subtilis glutamyl-tRNA Gln amidotransferase have been cloned. Expression of this transcriptional unit results in the production of a heterotrimeric protein that has been purified to homogeneity. The e...

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Veröffentlicht in:Proceedings of the National Academy of Sciences - PNAS 1997-10, Vol.94 (22), p.11819-11826
Hauptverfasser: Curnow, Alan W, Hong, Kwang-Won, Yuan, Robert, Kim, Sung-Il
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Sprache:eng
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Zusammenfassung:The three genes, gatC , gatA , and gatB , which constitute the transcriptional unit of the Bacillus subtilis glutamyl-tRNA Gln amidotransferase have been cloned. Expression of this transcriptional unit results in the production of a heterotrimeric protein that has been purified to homogeneity. The enzyme furnishes a means for formation of correctly charged Gln-tRNA Gln through the transamidation of misacylated Glu-tRNA Gln , functionally replacing the lack of glutaminyl-tRNA synthetase activity in Gram-positive eubacteria, cyanobacteria, Archaea, and organelles. Disruption of this operon is lethal. This demonstrates that transamidation is the only pathway to Gln-tRNA Gln in B. subtilis and that glutamyl-tRNA Gln amidotransferase is a novel and essential component of the translational apparatus.
ISSN:0027-8424
1091-6490
DOI:10.1073/PNAS.94.22.11819