ArticleProceedings of the National Academy of Sciences of the United States of America2015
Mistranslation drives the evolution of robustness in TEM-1 β-lactamase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. 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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32 citing papers in PubMed, 59 citations in OpenAlex.
- Cost of Altered Translation Accuracy Shapes Adaptation to Antibiotics in E. coli.Molecular biology and evolution · 2025Article
- Effect of Mutations on the Evolution of Extended Spectrum β-lactamases (ESBL).The protein journal · 2025Review
- A direct experimental test of Ohno's hypothesis.eLife · 2025Article
- High temperature delays and low temperature accelerates evolution of a new protein phenotype.Nature communications · 2024Article
- Fitness Effects of Phenotypic Mutations at Proteome-Scale Reveal Optimality of Translation Machinery.Molecular biology and evolution · 2024Article
- Revisiting the hydrolysis of ampicillin catalyzed by Temoneira-1 β-lactamase, and the effect of Ni(II), Cd(II) and Hg(II).Protein science : a publication of the Protein Society · 2023Article
- Not Quite Lost in Translation: Mistranslation Alters Adaptive Landscape Topography and the Dynamics of Evolution.Molecular biology and evolution · 2023Article
- Genes Vary Greatly in Their Propensity for Collateral Fitness Effects of Mutations.Molecular biology and evolution · 2023Article
- Enhancement of tumor immunogenicity by the introduction of non- proteinogenic amino acid azetidine-2-carboxylic acid.Oncoimmunology · 2022Article
- Phenotypic mutations contribute to protein diversity and shape protein evolution.Protein science : a publication of the Protein Society · 2022Review
- Mechanisms of protein evolution.Protein science : a publication of the Protein Society · 2022Review
- Prediction of Antibiotic Resistance Evolution by Growth Measurement of All Proximal Mutants of Beta-Lactamase.Molecular biology and evolution · 2022Article
- Evolutionary Pathways and Trajectories in Antibiotic Resistance.Clinical microbiology reviews · 2021Article
- Mistranslation Reduces Mutation Load in Evolving Proteins through Negative Epistasis with DNA Mutations.Molecular biology and evolution · 2021Article
- Mistranslation can promote the exploration of alternative evolutionary trajectories in enzyme evolution.Journal of evolutionary biology · 2021Article
- Quantifying the Mutational Robustness of Protein-Coding Genes.Journal of molecular evolution · 2021Article
- Role of Synonymous Mutations in the Evolution of TEM β-Lactamase Genes.Antimicrobial agents and chemotherapy · 2021Article
- The impact of mistranslation on phenotypic variability and fitness.Evolution; international journal of organic evolution · 2021Article
- The Relationship between the Misfolding Avoidance Hypothesis and Protein Evolutionary Rates in the Light of Empirical Evidence.Genome biology and evolution · 2021Article
- The Boggarts of biology: how non-genetic changes influence the genotype.Current genetics · 2021Review
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
How biological systems such as proteins achieve robustness to ubiquitous perturbations is a fundamental biological question. Such perturbations include errors that introduce phenotypic mutations into nascent proteins during the translation of mRNA. These errors are remarkably frequent. They are also costly, because they reduce protein stability and help create toxic misfolded proteins. Adaptive evolution might reduce these costs of protein mistranslation by two principal mechanisms. The first increases the accuracy of translation via synonymous "high fidelity" codons at especially sensitive sites. The second increases the robustness of proteins to phenotypic errors via amino acids that increase protein stability. To study how these mechanisms are exploited by populations evolving in the laboratory, we evolved the antibiotic resistance gene TEM-1 in Escherichia coli hosts with either normal or high rates of mistranslation. We analyzed TEM-1 populations that evolved under relaxed and stringent selection for antibiotic resistance by single molecule real-time sequencing. Under relaxed selection, mistranslating populations reduce mistranslation costs by reducing TEM-1 expression. Under stringent selection, they efficiently purge destabilizing amino acid changes. More importantly, they accumulate stabilizing amino acid changes rather than synonymous changes that increase translational accuracy. In the large populations we study, and on short evolutionary timescales, the path of least resistance in TEM-1 evolution consists of reducing the consequences of translation errors rather than the errors themselves.
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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.