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

Alan W. Curnow, Kwang Won Hong, Robert Yuan, Sung Il Kim, Orlando Martins, Wade Winkler, Tina M. Henkin, Dieter Söll

Research output: Contribution to journalArticlepeer-review

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Abstract

The three genes, gatC, gatA, and gatB, which constitute the transcriptional unit of the Bacillus subtilis glutamyl-tRNAGln 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-tRNAGln through the transamidation of misacylated Glu-tRNAGln, 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-tRNAGln in B. subtilis and that glutamyl-tRNAGln amidotransferase is a novel and essential component of the translational apparatus.

Original languageEnglish
Pages (from-to)11819-11826
Number of pages8
JournalProceedings of the National Academy of Sciences of the United States of America
Volume94
Issue number22
DOIs
StatePublished - 28 Oct 1997

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