Exploring protein fitness landscapes by directed evolution

被引：764

作者：

Romero, Philip A. ^{[1
]}

Arnold, Frances H. ^{[1
]}

机构：

[1] CALTECH, Div Chem & Chem Engn, Pasadena, CA 91125 USA

来源：

NATURE REVIEWS MOLECULAR CELL BIOLOGY | 2009年 / 10卷 / 12期

基金：

美国国家卫生研究院; 美国国家科学基金会;

关键词：

STRUCTURE-GUIDED RECOMBINATION; RED FLUORESCENT PROTEIN; IN-VITRO EVOLUTION; SEQUENCE SPACE; RNA ENZYME; SUBSTRATE SPECIFICITIES; COMPUTATIONAL DESIGN; LABORATORY EVOLUTION; METABOLIC PATHWAYS; CATALYTIC-ACTIVITY;

D O I：

10.1038/nrm2805

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Directed evolution circumvents our profound ignorance of how a protein's sequence encodes its function by using iterative rounds of random mutation and artificial selection to discover new and useful proteins. Proteins can be tuned to adapt to new functions or environments by simple adaptive walks involving small numbers of mutations. Directed evolution studies have shown how rapidly some proteins can evolve under strong selection pressures and, because the entire 'fossil record' of evolutionary intermediates is available for detailed study, they have provided new insight into the relationship between sequence and function. Directed evolution has also shown how mutations that are functionally neutral can set the stage for further adaptation.

引用

页码：866 / 876

页数：11

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