ArticlePhilosophical transactions of the Royal Society of London. Series B, Biological sciences2011
Mistranslation and its control by tRNA synthetases.
Article in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 38 citations in OpenAlex.
- The ZN domain acts as a dynamic switch coordinating multiple-step aminoacylation in bacterial leucyl-tRNA synthetase.Nucleic acids research · 2026Article
- Translation accuracy in E. coli.Nucleic acids research · 2026Article
- A metal ion mediated functional dichotomy encodes plasticity during translation quality control.Nature communications · 2025Article
- Design principles and functional basis of enantioselectivity of alanyl-tRNA synthetase and a chiral proofreader during protein biosynthesis.Nucleic acids research · 2023Article
- Article
- Efficacy of epetraborole against Mycobacterium abscessus is increased with norvaline.PLoS pathogens · 2021Article
- Bacterial translation machinery for deliberate mistranslation of the genetic code.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- A molecular link between cell wall biosynthesis, translation fidelity, and stringent response inProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Aminoacyl-tRNA synthetases.RNA (New York, N.Y.) · 2020Review
- 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
- Modulating Mistranslation Potential of tRNAGenetics · 2019Article
- Error-prone protein synthesis in parasites with the smallest eukaryotic genome.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Editing activity for eliminating mischarged tRNAs is essential in mammalian mitochondria.Nucleic acids research · 2018Article
- Review
- MS-READ: Quantitative measurement of amino acid incorporation.Biochimica et biophysica acta. General subjects · 2017Article
- Structural Insights into the Polyphyletic Origins of Glycyl tRNA Synthetases.The Journal of biological chemistry · 2016Article
- Stress Response and Adaptation Mediated by Amino Acid Misincorporation during Protein Synthesis.Advances in nutrition (Bethesda, Md.) · 2016Review
- Homologous trans-editing factors with broad tRNA specificity prevent mistranslation caused by serine/threonine misactivation.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Bacterial transfer RNAs.FEMS microbiology reviews · 2015Review
- Ancestral AlaX editing enzymes for control of genetic code fidelity are not tRNA-specific.The Journal of biological chemistry · 2015Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
Aminoacyl tRNA synthetases are ancient proteins that interpret the genetic material in all life forms. They are thought to have appeared during the transition from the RNA world to the theatre of proteins. During translation, they establish the rules of the genetic code, whereby each amino acid is attached to a tRNA that is cognate to the amino acid. Mistranslation occurs when an amino acid is attached to the wrong tRNA and subsequently is misplaced in a nascent protein. Mistranslation can be toxic to bacteria and mammalian cells, and can lead to heritable mutations. The great challenge for nature appears to be serine-for-alanine mistranslation, where even small amounts of this mistranslation cause severe neuropathologies in the mouse. To minimize serine-for-alanine mistranslation, powerful selective pressures developed to prevent mistranslation through a special editing activity imbedded within alanyl-tRNA synthetases (AlaRSs). However, serine-for-alanine mistranslation is so challenging that a separate, genome-encoded fragment of the editing domain of AlaRS is distributed throughout the Tree of Life to redundantly prevent serine-to-alanine mistranslation. Detailed X-ray structural and functional analysis shed light on why serine-for-alanine mistranslation is a universal problem, and on the selective pressures that engendered the appearance of AlaXps at the base of the Tree of Life.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.