globalchange  > 气候变化与战略
DOI: 10.1073/pnas.1810194115
论文题名:
Protein evolution speed depends on its stability and abundance and on chaperone concentrations
作者: Agozzino L.; Dill K.A.
刊名: Proceedings of the National Academy of Sciences of the United States of America
ISSN: 0027-8424
出版年: 2018
卷: 115, 期:37
起始页码: 9092
结束页码: 9097
语种: 英语
英文关键词: Adaptation ; Protein evolution ; Substitution rate
Scopus关键词: chaperone ; protein ; adaptation ; amino acid sequence ; Article ; cell activity ; conceptual framework ; hydrophobicity ; molecular dynamics ; molecular evolution ; molecular model ; prediction ; pressure ; priority journal ; protein aggregation ; protein folding ; protein function ; protein misfolding ; protein stability ; biological model ; chemistry ; genetics ; protein folding ; Evolution, Molecular ; Models, Genetic ; Protein Folding ; Proteins
英文摘要: Proteins evolve at different rates. What drives the speed of protein sequence changes? Two main factors are a protein’s folding stability and aggregation propensity. By combining the hydrophobic–polar (HP) model with the Zwanzig–Szabo–Bagchi rate theory, we find that: (i) Adaptation is strongly accelerated by selection pressure, explaining the broad variation from days to thousands of years over which organisms adapt to new environments. (ii) The proteins that adapt fastest are those that are not very stably folded, because their fitness landscapes are steepest. And because heating destabilizes folded proteins, we predict that cells should adapt faster when put into warmer rather than cooler environments. (iii) Increasing protein abundance slows down evolution (the substitution rate of the sequence) because a typical protein is not perfectly fit, so increasing its number of copies reduces the cell’s fitness. (iv) However, chaperones can mitigate this abundance effect and accelerate evolution (also called evolutionary capacitance) by effectively enhancing protein stability. This model explains key observations about protein evolution rates. © 2018 National Academy of Sciences. All Rights Reserved.
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资源类型: 期刊论文
标识符: http://119.78.100.158/handle/2HF3EXSE/163662
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作者单位: Agozzino, L., Laufer Center for Physical and Quantitative Biology, Stony Brook University, Stony Brook, NY 11794-5252, United States, Department of Physics and Astronomy, Stony Brook University, Stony Brook, NY 11794-3800, United States; Dill, K.A., Laufer Center for Physical and Quantitative Biology, Stony Brook University, Stony Brook, NY 11794-5252, United States, Department of Physics and Astronomy, Stony Brook University, Stony Brook, NY 11794-3800, United States, Department of Chemistry, Stony Brook University, Stony Brook, NY 11790-3400, United States

Recommended Citation:
Agozzino L.,Dill K.A.. Protein evolution speed depends on its stability and abundance and on chaperone concentrations[J]. Proceedings of the National Academy of Sciences of the United States of America,2018-01-01,115(37)
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