A KINETIC PARTITIONING MODEL OF SELECTIVE BINDING OF NONNATIVE PROTEINS BY THE BACTERIAL CHAPERONE SECB

被引：204

作者：

HARDY, SJS ^{[1
]}

RANDALL, LL ^{[1
]}

机构：

[1] WASHINGTON STATE UNIV,DEPT BIOCHEM & BIOPHYS,PULLMAN,WA 99164

来源：

SCIENCE | 1991年 / 251卷 / 4992期

关键词：

D O I：

10.1126/science.1989077

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

An in vitro assay for the interaction of SecB, a molecular chaperone from Escherichia coli, with polypeptide ligands was established based on the ability of SecB to block the refolding of denatured maltose-binding protein. Competition experiments show that SecB binds selectively to nonnative proteins with high affinity and without specificity for a particular sequence of amino acids. It is proposed that selectivity in binding is due to a kinetic partitioning of polypeptides between folding and association with SecB.

引用

页码：439 / 443

页数：5

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