ArticlePLoS genetics2015
Methionine Mistranslation Bypasses the Restraint of the Genetic Code to Generate Mutant Proteins with Distinct Activities.
Article in PLoS genetics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 20 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
20 citing papers in PubMed, 25 citations in OpenAlex.
- Mistranslation from an endogenous tRNA variant in human pan-genome cell lines.Nucleic acids research · 2026Article
- Emerging Roles of Vitamin BInternational journal of molecular sciences · 2024Review
- Perseverance of protein homeostasis despite mistranslation of glycine codons with alanine.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023Article
- Regulating Expression of Mistranslating tRNAs by Readthrough RNA Polymerase II Transcription.ACS synthetic biology · 2021Article
- The Role of Methionine Residues in the Regulation of Liquid-Liquid Phase Separation.Biomolecules · 2021Review
- Transfer RNAs: diversity in form and function.RNA biology · 2021Review
- Chemical-Genetic Interactions with the Proline Analog L-Azetidine-2-Carboxylic Acid inG3 (Bethesda, Md.) · 2020Article
- Hijacking tRNAs From Translation: Regulatory Functions of tRNAs in Mammalian Cell Physiology.Frontiers in molecular biosciences · 2020Review
- Methionine in proteins: The Cinderella of the proteinogenic amino acids.Protein science : a publication of the Protein Society · 2019Review
- The Oxidized Protein Repair Enzymes Methionine Sulfoxide Reductases and Their Roles in Protecting against Oxidative Stress, in Ageing and in Regulating Protein Function.Antioxidants (Basel, Switzerland) · 2018Review
- Visualizing tRNA-dependent mistranslation in human cells.RNA biology · 2018Article
- Translational fidelity and mistranslation in the cellular response to stress.Nature microbiology · 2017Review
- tRNA Misacylation with Methionine in the Mouse Gut Microbiome in Situ.Microbial ecology · 2017Article
- Function and origin of mistranslation in distinct cellular contexts.Critical reviews in biochemistry and molecular biology · 2017Review
- Determining the fidelity of tRNA aminoacylation via microarrays.Methods (San Diego, Calif.) · 2017Article
- Global tRNA misacylation induced by anaerobiosis and antibiotic exposure broadly increases stress resistance in Escherichia coli.Nucleic acids research · 2016Article
- Evolutionary Gain of Alanine Mischarging to Noncognate tRNAs with a G4:U69 Base Pair.Journal of the American Chemical Society · 2016Article
- Interaction of tRNA with MEK2 in pancreatic cancer cells.Scientific reports · 2016Article
- Stress Beyond Translation: Poxviruses and More.Viruses · 2016Review
- Correction: Methionine Mistranslation Bypasses the Restraint of the Genetic Code to Generate Mutant Proteins with Distinct Activities.PLoS genetics · 2016Article
Corrections and comments
- Correction · 2016-01-25Duplication of/in Image · Error in Image ·
- Erratum issued
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Although mistranslation is commonly believed to be deleterious, recent evidence indicates that mistranslation can be actively regulated and be beneficial in stress response. Methionine mistranslation in mammalian cells is regulated by reactive oxygen species where cells deliberately alter the proteome through incorporating Met at non-Met positions to enhance oxidative stress response. However, it was not known whether specific, mistranslated mutant proteins have distinct activities from the wild-type protein whose sequence is restrained by the genetic code. Here, we show that Met mistranslation with and without Ca(2+) overload generates specific mutant Ca(2+)/calmodulin-dependent protein kinase II (CaMKII) proteins substituting non-Met with Met at multiple locations. Compared to the genetically encoded wild-type CaMKII, specific mutant CaMKIIs can have distinct activation profiles, intracellular localization and enhanced phenotypes. Our results demonstrate that Met-mistranslation, or "Met-scan" can indeed generate mutant proteins in cells that expand the activity profile of the wild-type protein, and provide a molecular mechanism for the role of regulated mistranslation.
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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.