气候变化领域集成服务门户(CCPortal): Protein evolution speed depends on its stability and abundance and on chaperone concentrations

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DOI	10.1073/pnas.1810194115
	Protein evolution speed depends on its stability and abundance and on chaperone concentrations
	Agozzino L.; Dill K.A.
发表日期	2018
ISSN	0027-8424
起始页码	9092
结束页码	9097
卷号	115 期号:37
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.
英文关键词	Adaptation; Protein evolution; Substitution rate
语种	英语
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
来源期刊	Proceedings of the National Academy of Sciences of the United States of America
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/160466
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
推荐引用方式 GB/T 7714	Agozzino L.,Dill K.A.. Protein evolution speed depends on its stability and abundance and on chaperone concentrations[J],2018,115(37).
APA	Agozzino L.,&Dill K.A..(2018).Protein evolution speed depends on its stability and abundance and on chaperone concentrations.Proceedings of the National Academy of Sciences of the United States of America,115(37).
MLA	Agozzino L.,et al."Protein evolution speed depends on its stability and abundance and on chaperone concentrations".Proceedings of the National Academy of Sciences of the United States of America 115.37(2018).