ArticleNucleic acids research2015
Trans-oligomerization of duplicated aminoacyl-tRNA synthetases maintains genetic code fidelity under stress.
Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 24 citations in OpenAlex.
- Adaptation of a eukaryote-like ProRS to a prokaryote-like tRNAPro.Nucleic acids research · 2024Article
- An ancient bacterial zinc acquisition system identified from a cyanobacterial exoproteome.PLoS biology · 2024Article
- Symmetrical distributions of aminoacyl-tRNA synthetases during the evolution of the genetic code.Theory in biosciences = Theorie in den Biowissenschaften · 2023Article
- Article
- Protein metalation in biology.Current opinion in chemical biology · 2022Review
- Diversification of aminoacyl-tRNA synthetase activitiesFrontiers in physiology · 2022Review
- Bacterial translation machinery for deliberate mistranslation of the genetic code.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Duplication of leucyl-tRNA synthetase in an archaeal extremophile may play a role in adaptation to variable environmental conditions.The Journal of biological chemistry · 2020Article
- A threonyl-tRNA synthetase-like protein has tRNA aminoacylation and editing activities.Nucleic acids research · 2018Article
- Environmental adaptation ofInternational journal of biological sciences · 2018Article
- Bioinformatic Analysis Reveals Archaeal tRNALife (Basel, Switzerland) · 2017Article
- The complex evolutionary history of aminoacyl-tRNA synthetases.Nucleic acids research · 2017Article
- Sub-Cellular Localization and Complex Formation by Aminoacyl-tRNA Synthetases in Cyanobacteria: Evidence for Interaction of Membrane-Anchored ValRS with ATP Synthase.Frontiers in microbiology · 2016Article
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
Abstract
Aminoacyl-tRNA synthetases (aaRSs) play a key role in deciphering the genetic message by producing charged tRNAs and are equipped with proofreading mechanisms to ensure correct pairing of tRNAs with their cognate amino acid. Duplicated aaRSs are very frequent in Nature, with 25,913 cases observed in 26,837 genomes. The oligomeric nature of many aaRSs raises the question of how the functioning and oligomerization of duplicated enzymes is organized. We characterized this issue in a model prokaryotic organism that expresses two different threonyl-tRNA synthetases, responsible for Thr-tRNA(Thr) synthesis: one accurate and constitutively expressed (T1) and another (T2) with impaired proofreading activity that also generates mischarged Ser-tRNA(Thr). Low zinc promotes dissociation of dimeric T1 into monomers deprived of aminoacylation activity and simultaneous induction of T2, which is active for aminoacylation under low zinc. T2 either forms homodimers or heterodimerizes with T1 subunits that provide essential proofreading activity in trans. These findings evidence that in organisms with duplicated genes, cells can orchestrate the assemblage of aaRSs oligomers that meet the necessities of the cell in each situation. We propose that controlled oligomerization of duplicated aaRSs is an adaptive mechanism that can potentially be expanded to the plethora of organisms with duplicated oligomeric aaRSs.
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