ArticleProceedings of the National Academy of Sciences of the United States of America2011
Naturally occurring aminoacyl-tRNA synthetases editing-domain mutations that cause mistranslation in Mycoplasma parasites.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.
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Who cites it
80 citing papers in PubMed, 111 citations in OpenAlex.
- Article
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- A metal ion mediated functional dichotomy encodes plasticity during translation quality control.Nature communications · 2025Article
- Surface protein glycosylation conserved in the human pathogen Mycoplasma genitalium and retained in the synthetic organism JCVI-Syn3A.PloS one · 2025Article
- Interplay between mistranslation and oxidative stress inArhiv za higijenu rada i toksikologiju · 2024Article
- The tRNA identity landscape for aminoacylation and beyond.Nucleic acids research · 2023Review
- Translational Fidelity during Bacterial Stresses and Host Interactions.Pathogens (Basel, Switzerland) · 2023Review
- Increase in Ribosomal Fidelity BenefitsGenes · 2022Article
- Integrated Metabolomics and Transcriptome Revealed the Effect of FermentedFrontiers in immunology · 2022Article
- Review
- Impact of alanyl-tRNA synthetase editing deficiency in yeast.Nucleic acids research · 2021Article
- Widespread ribosome stalling in a genome-reduced bacterium and the need for translational quality control.iScience · 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
- Sulfamethoxazole-Altered Transcriptomein Green AlgaFrontiers in microbiology · 2021Article
- Aminoacyl-tRNA synthetases.RNA (New York, N.Y.) · 2020Review
- Exploiting evolutionary trade-offs for posttreatment management of drug-resistant populations.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Genomic innovation of ATD alleviates mistranslation associated with multicellularity in Animalia.eLife · 2020Article
- 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 Synthetic Reporter for Probing Mistranslation in Living Cells.Frontiers in bioengineering and biotechnology · 2020Article
- Article
20 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
Abstract
Mycoplasma parasites escape host immune responses via mechanisms that depend on remarkable phenotypic plasticity. Identification of these mechanisms is of great current interest. The aminoacyl-tRNA synthetases (AARSs) attach amino acids to their cognate tRNAs, but occasionally make errors that substitute closely similar amino acids. AARS editing pathways clear errors to avoid mistranslation during protein synthesis. We show here that AARSs in Mycoplasma parasites have point mutations and deletions in their respective editing domains. The deleterious effect on editing was confirmed with a specific example studied in vitro. In vivo mistranslation was determined by mass spectrometric analysis of proteins produced in the parasite. These mistranslations are uniform cases where the predicted closely similar amino acid replaced the correct one. Thus, natural AARS editing-domain mutations in Mycoplasma parasites cause mistranslation. We raise the possibility that these mutations evolved as a mechanism for antigen diversity to escape host defense systems.
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