ArticleNature2010
Two enzymes bound to one transfer RNA assume alternative conformations for consecutive reactions.
Article in Nature, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 58 citations in OpenAlex.
- The tRNA identity landscape for aminoacylation and beyond.Nucleic acids research · 2023Review
- Sequential action of a tRNA base editor in conversion of cytidine to pseudouridine.Nature communications · 2022Article
- Clinically Relevant Mutations of Mycobacterial GatCAB Inform Regulation of Translational Fidelity.mBio · 2021Article
- Indirect Routes to Aminoacyl-tRNA: The Diversity of Prokaryotic Cysteine Encoding Systems.Frontiers in genetics · 2021Article
- Structure of the dihydrolipoamide succinyltransferase catalytic domain from Escherichia coli in a novel crystal form: a tale of a common protein crystallization contaminant.Acta crystallographica. Section F, Structural biology communications · 2019Article
- Pathogenic variants in glutamyl-tRNANature communications · 2018Article
- Structural basis for tRNA-dependent cysteine biosynthesis.Nature communications · 2017Article
- Aminoacyl-tRNA Synthetases in the Bacterial World.EcoSal Plus · 2016Review
- The crystal structure of human GlnRS provides basis for the development of neurological disorders.Nucleic acids research · 2016Article
- The tRNA Elbow in Structure, Recognition and Evolution.Life (Basel, Switzerland) · 2016Review
- A Comprehensive Genomic Analysis Reveals the Genetic Landscape of Mitochondrial Respiratory Chain Complex Deficiencies.PLoS genetics · 2016Article
- Structural basis for methyl-donor-dependent and sequence-specific binding to tRNA substrates by knotted methyltransferase TrmD.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Structural Basis for Specific Inhibition of tRNA Synthetase by an ATP Competitive Inhibitor.Chemistry & biology · 2015Article
- Dispensability of zinc and the putative zinc-binding domain in bacterial glutamyl-tRNA synthetase.Bioscience reports · 2015Article
- tRNA biology in mitochondria.International journal of molecular sciences · 2015Review
- Structure of the Pseudomonas aeruginosa transamidosome reveals unique aspects of bacterial tRNA-dependent asparagine biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Gene rearrangements in gekkonid mitochondrial genomes with shuffling, loss, and reassignment of tRNA genes.BMC genomics · 2014Article
- Ancient translation factor is essential for tRNA-dependent cysteine biosynthesis in methanogenic archaea.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Crystallization and preliminary X-ray crystallographic analysis of a bacterial Asn-transamidosome.Acta crystallographica. Section F, Structural biology communications · 2014Article
- Crystal structure of Saccharomyces cerevisiae mitochondrial GatFAB reveals a novel subunit assembly in tRNA-dependent amidotransferases.Nucleic acids research · 2014Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In most bacteria and all archaea, glutamyl-tRNA synthetase (GluRS) glutamylates both tRNA(Glu) and tRNA(Gln), and then Glu-tRNA(Gln) is selectively converted to Gln-tRNA(Gln) by a tRNA-dependent amidotransferase. The mechanisms by which the two enzymes recognize their substrate tRNA(s), and how they cooperate with each other in Gln-tRNA(Gln) synthesis, remain to be determined. Here we report the formation of the 'glutamine transamidosome' from the bacterium Thermotoga maritima, consisting of tRNA(Gln), GluRS and the heterotrimeric amidotransferase GatCAB, and its crystal structure at 3.35 A resolution. The anticodon-binding body of GluRS recognizes the common features of tRNA(Gln) and tRNA(Glu), whereas the tail body of GatCAB recognizes the outer corner of the L-shaped tRNA(Gln) in a tRNA(Gln)-specific manner. GluRS is in the productive form, as its catalytic body binds to the amino-acid-acceptor arm of tRNA(Gln). In contrast, GatCAB is in the non-productive form: the catalytic body of GatCAB contacts that of GluRS and is located near the acceptor stem of tRNA(Gln), in an appropriate site to wait for the completion of Glu-tRNA(Gln) formation by GluRS. We identified the hinges between the catalytic and anticodon-binding bodies of GluRS and between the catalytic and tail bodies of GatCAB, which allow both GluRS and GatCAB to adopt the productive and non-productive forms. The catalytic bodies of the two enzymes compete for the acceptor arm of tRNA(Gln) and therefore cannot assume their productive forms simultaneously. The transition from the present glutamylation state, with the productive GluRS and the non-productive GatCAB, to the putative amidation state, with the non-productive GluRS and the productive GatCAB, requires an intermediate state with the two enzymes in their non-productive forms, for steric reasons. The proposed mechanism explains how the transamidosome efficiently performs the two consecutive steps of Gln-tRNA(Gln) formation, with a low risk of releasing the unstable intermediate Glu-tRNA(Gln).
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