ArticleProceedings of the National Academy of Sciences of the United States of America1997
Glu-tRNAGln amidotransferase: a novel heterotrimeric enzyme required for correct decoding of glutamine codons during translation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 134 papers.
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134 citing papers in PubMed.
- Article
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- Exploration of genes encoding KEGG pathway enzymes in rhizospheric microbiome of the wild plant Abutilon fruticosum.AMB Express · 2024Article
- Structural basis of the amidase ClbL central to the biosynthesis of the genotoxin colibactin.Acta crystallographica. Section D, Structural biology · 2023Article
- Review
- Genomics-Based Reconstruction and Predictive Profiling of Amino Acid Biosynthesis in the Human Gut Microbiome.Microorganisms · 2022Article
- Ribosome profiling enhances understanding of mycobacterial translation.Frontiers in microbiology · 2022Review
- Clinically Relevant Mutations of Mycobacterial GatCAB Inform Regulation of Translational Fidelity.mBio · 2021Article
- Morphological change of coiled bacterium Spirosoma linguale with acquisition of β-lactam resistance.Scientific reports · 2021Article
- Mitochondrial Aminoacyl-tRNA Synthetase and Disease: The Yeast Contribution for Functional Analysis of Novel Variants.International journal of molecular sciences · 2021Review
- Review
- Transfer RNAs: diversity in form and function.RNA biology · 2021Review
- Aminoacyl-tRNA Synthetases as Valuable Targets for Antimicrobial Drug Discovery.International journal of molecular sciences · 2021Review
- Article
- Aminoacyl-tRNA synthetases.RNA (New York, N.Y.) · 2020Review
- The structural basis of the genetic code: amino acid recognition by aminoacyl-tRNA synthetases.Scientific reports · 2020Article
- Forward Genetics Reveals aFrontiers in microbiology · 2020Article
74 more citing papers are in PubMed but not listed here.
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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.
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