Solubilization of aggregated proteins by ClpB/DnaK relies on the continuous extraction of unfolded polypeptides

被引：67

作者：

Schlieker, C

Tews, I

Bukau, B

Mogk, A

机构：

[1] Heidelberg Univ, D-69120 Heidelberg, Germany

[2] Heidelberg Univ, Biochem Zentrum, D-69120 Heidelberg, Germany

来源：

FEBS LETTERS | 2004年 / 578卷 / 03期

关键词：

protein disaggregation; chaperone; ClpB; DnaK; AAA plus protein;

D O I：

10.1016/j.febslet.2004.11.051

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 AAA+ chaperone ClpB solubilizes in cooperation with the DnaK chaperone system aggregated proteins. The mechanistic features of the protein disaggregation process are poorly understood. Here, we investigated the mechanism of ClpB/DnaK-dependent solubilization of heat-aggregated malate dehydrogenase (MDH) by following characteristics of MDH aggregates during the disaggregation reaction. We demonstrate that disaggregation is achieved by the continuous extraction of unfolded MDH molecules and not by fragmentation of large MDH aggregates. These findings support a ClpB-dependent threading mechanism as an integral part of the disaggregation reaction. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：351 / 356

页数：6

共 29 条

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