The DOI matches its Crossref record; 12 of the 12 references it cites were found in a registry or an index.
Mistranslation-Induced Protein Misfolding as a Dominant Constraint on Coding-Sequence Evolution
Open accessAbstract
Summary The biological causes of selective pressures on coding-sequence evolution remain controversial, despite the surprising consistency of covariation between common measures of evolutionary change (substitution rates) and gene expression (mRNA levels, codon usage) across taxa. We carry out a unified analysis which reveals these conserved patterns in E. coli, yeast, worm, fly, mouse, and human, and suggests that all trends stem largely from a unified underlying selective pressure. In metazoans, these trends are strongest in tissues composed of neurons, whose structure and lifetime confer extreme sensitivity to protein misfolding. We propose, and demonstrate using a molecular-level evolutionary simulation, that selection against toxicity of misfolded proteins generated by ribosome errors suffices to create all the observed covariation. The mechanistic model of molecular evolution which emerges yields testable biochemical predictions, calls into question use of nonsynonymous-to-synonymous substitution ratios (Ka/Ks) to detect functional selection, and suggests how mistranslation may contribute to neurodegenerative disease.
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Cites
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Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
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Cited by
Biological and Chemical Approaches to Diseases of Proteostasis Deficiency
Powers, E. T., Morimoto, R. I., Dillin, A., Kelly, J. W., & Balch, W. E. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.052308.114844 · Cited by 1,149
Codon Optimality Is a Major Determinant of mRNA Stability
Presnyak, V., Alhusaini, N., Chen, Y.-H., Martin, S., Morris, N., Kline, N., Olson, S., Weinberg, D., Baker, K. E., Graveley, B. R., et al. (2015) · Cell · doi:10.1016/j.cell.2015.02.029 · Cited by 1,078
“Critically, optimal codons are postulated to be decoded faster and more accurately by the ribosome than non-optimal codons (Akashi, 1994; Drummond and Wilke, 2008), which are hypothesized to slow translation elongation (Novoa and Ribas de Pouplana, 2012; Tuller et al., 2010).”
BackgroundUnderstanding the contribution of synonymous mutations to human disease
Sauna, Z. E., & Kimchi-Sarfaty, C. (2011) · Nature Reviews Genetics · doi:10.1038/nrg3051 · Cited by 1,022
An evolutionarily conserved mechanism for controlling the efficiency of protein translation
Tuller, T., Carmi, A., Vestsigian, K., Navon, S., Dorfan, Y., Zaborske, J., Pan, T., Dahan, O., Furman, I., & Pilpel, Y. (2010) · Cell · doi:10.1016/j.cell.2010.03.031 · Cited by 874
Stability effects of mutations and protein evolvability
Tokuriki, N., & Tawfik, D. S. (2009) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2009.08.003 · Cited by 834
Metadata
- Authors
- Drummond, D. A., & Wilke, C. O.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2008-07
- Volume
- 134
- Issue
- 2
- Pages
- 341-352
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2039790548
- Cited by
- 1,053
- References
- 12
- FWCI
- 24.32
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Drummond, D. A., & Wilke, C. O. (2008). Mistranslation-Induced Protein Misfolding as a Dominant Constraint on Coding-Sequence Evolution. Cell. https://doi.org/10.1016/j.cell.2008.05.042
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