Protein folding: Versatility of the cytosolic chaperonin TRIC/CCT

被引：105

作者：

Leroux, MR ^{[1
]}

Hartl, FU ^{[1
]}

机构：

[1] Max Planck Inst Biochem, Dept Cellular Biochem, D-82152 Martinsried, Germany

来源：

CURRENT BIOLOGY | 2000年 / 10卷 / 07期

关键词：

D O I：

10.1016/S0960-9822(00)00432-2

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：

Efficient de novo folding of actins and tubulins requires two molecular chaperones, the chaperonin TRiC (or CCT) and its novel cofactor GimC (or prefoldin). Recent studies indicate that TRiC is exquisitely adapted for this task, yet has the ability to interact with and assist the folding of numerous other cellular proteins. (C) 2000 Elsevier Science Ltd. All rights reserved.

引用

页码：R260 / R264

页数：5

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