Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 11819-11826 |
| Number of pages | 8 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Volume | 94 |
| Issue number | 22 |
| DOIs | |
| State | Published - 1997 |
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