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Glu-tRNA Gln amidotransferase: A novel heterotrimeric enzyme required for correct decoding of glutamine codons during translation
Open accessAbstract
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.
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Metadata
- Authors
- Curnow, A. W., Hong, K.-W., Yuan, R., Kim, S.-I., Martins, O., Winkler, W., Henkin, T. M., & Söll, D.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1997-10-28
- Volume
- 94
- Issue
- 22
- Pages
- 11819-11826
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2147302373
- Cited by
- 313
- References
- 0
- FWCI
- 5.40
- Type
- journal article
- Language
- en
- Open access
- green
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