Molecular chaperones: Inside a nd outside the Anfinsen cage

被引：38

作者：

Ellis, RJ ^{[1
]}

机构：

[1] Univ Warwick, Dept Biol Sci, Coventry CV4 7AL, W Midlands, England

来源：

CURRENT BIOLOGY | 2001年 / 11卷 / 24期

关键词：

D O I：

10.1016/S0960-9822(01)00620-0

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：

The GroEL/GroES chaperonin system acts as a passive anti-aggregation cage for refolding rubisco and rhodanese, and not as an active unfolding device. Refolding aconitase is too large to enter the cage but reversible binding to GroEL reduces its aggregration. Unexpectedly, confinement in the cage increases the rate of refolding of rubisco, but not rhodanese.

引用

页码：R1038 / R1040

页数：3

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