ArticleMolecular systems biology2010
Impact of translational error-induced and error-free misfolding on the rate of protein evolution.
Article in Molecular systems biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.
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77 citing papers in PubMed, 104 citations in OpenAlex.
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- Translational fidelity and longevity are genetically linked.Nature communications · 2025Article
- Cell Compartment is a Predictor of Protein Rate of Evolution, but not in the Manner Expected: Evidence Against the Extended Complexity Hypothesis.Genome biology and evolution · 2025Article
- Codon Usage Bias: A Potential Factor Affecting VGLUT Developmental Expression and Protein Evolution.Molecular neurobiology · 2025Article
- Protein Quality Control is a Master Modulator of Molecular Evolution in Bacteria.Genome biology and evolution · 2025Review
- Amino acid sequence encodes protein abundance shaped by protein stability at reduced synthesis cost.Protein science : a publication of the Protein Society · 2025Article
- Genome-wide impact of codon usage bias on translation optimization in Drosophila melanogaster.Nature communications · 2024Article
- Examining the Effects of Temperature on the Evolution of Bacterial tRNA Pools.Genome biology and evolution · 2024Article
- Evolution and expression patterns of the neo-sex chromosomes of the crested ibis.Nature communications · 2024Article
- Classical cadherins evolutionary constraints in primates is associated with their expression in the central nervous system.PloS one · 2024Article
- Genomic estimates of mutation and substitution rates contradict the evolutionary speed hypothesis of the latitudinal diversity gradient.Proceedings. Biological sciences · 2023Article
- Determining the effects of temperature on the evolution of bacterial tRNA pools.bioRxiv : the preprint server for biology · 2023Article
- Highly Abundant Proteins Are Highly Thermostable.Genome biology and evolution · 2023Article
- What Has Genomics Taught An Evolutionary Biologist?Genomics, proteomics & bioinformatics · 2023Review
- Purifying selection enduringly acts on the sequence evolution of highly expressed proteins in Escherichia coli.G3 (Bethesda, Md.) · 2022Article
- Low protein expression enhances phenotypic evolvability by intensifying selection on folding stability.Nature ecology & evolution · 2022Article
- Extracellular Domains of Transmembrane Proteins Defy the Expression Level-Evolutionary Rate Anticorrelation.Genome biology and evolution · 2022Article
- Expression level is a major modifier of the fitness landscape of a protein coding gene.Nature ecology & evolution · 2022Article
- Specificity of mRNA Folding and Its Association with Evolutionarily Adaptive mRNA Secondary Structures.Genomics, proteomics & bioinformatics · 2021Article
17 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
What determines the rate of protein evolution is a fundamental question in biology. Recent genomic studies revealed a surprisingly strong anticorrelation between the expression level of a protein and its rate of sequence evolution. This observation is currently explained by the translational robustness hypothesis in which the toxicity of translational error-induced protein misfolding selects for higher translational robustness of more abundant proteins, which constrains sequence evolution. However, the impact of error-free protein misfolding has not been evaluated. We estimate that a non-negligible fraction of misfolded proteins are error free and demonstrate by a molecular-level evolutionary simulation that selection against protein misfolding results in a greater reduction of error-free misfolding than error-induced misfolding. Thus, an overarching protein-misfolding-avoidance hypothesis that includes both sources of misfolding is superior to the translational robustness hypothesis. We show that misfolding-minimizing amino acids are preferentially used in highly abundant yeast proteins and that these residues are evolutionarily more conserved than other residues of the same proteins. These findings provide unambiguous support to the role of protein-misfolding-avoidance in determining the rate of protein sequence evolution.
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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.