A CYTOPLASMIC CHAPERONIN THAT CATALYZES BETA-ACTIN FOLDING

被引：438

作者：

GAO, YJ

THOMAS, JO

CHOW, RL

LEE, GH

COWAN, NJ

机构：

[1] Department of Biochemistry New York University Medical Center New York

来源：

CELL | 1992年 / 69卷 / 06期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1016/0092-8674(92)90622-J

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We have isolated a cytoplasmic chaperonin based on its ability to catalyze the folding of denatured beta-actin. The cytoplasmic chaperonin is organized as a multisubunit toroid and requires Mg2+ and ATP for activity. The folding reaction proceeds via the rapid ATP-independent formation of a binary complex, followed by a slower ATP-dependent release of the native product. Electron microscopic observations reveal a striking structural change that occurs upon addition of Mg2+ and ATP. The eukaryotic cytoplasm thus contains a chaperonin that is functionally analagous to its prokaryotic, mitochondrial, and chloroplastic counter parts.

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页码：1043 / 1050

页数：8

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