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Proc Natl Acad Sci U S A. 1997 Oct 28;94(22):11819-26.

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

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  • 1Department of Molecular Biophysics, Yale University, New Haven, CT 06520-8114, USA.

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.

Comment in

  • Once there were twenty. [Proc Natl Acad Sci U S A. 1997]
PMID:
9342321
[PubMed - indexed for MEDLINE]
PMCID:
PMC23611
Free PMC Article

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