The ClpB/Hsp104 molecular chaperone - a protein disaggregating machine

被引：76

作者：

Lee, S ^{[1
]}

Sowa, ME ^{[1
]}

Choi, JM ^{[1
]}

Tsai, FTF ^{[1
]}

机构：

[1] Baylor Coll Med, Verna & Marrs McLean Dept Biochem & Mol Biol, Houston, TX 77030 USA

来源：

JOURNAL OF STRUCTURAL BIOLOGY | 2004年 / 146卷 / 1-2期

关键词：

AAA(+) ClpB; Hsp104; molecular chaperone; protein disaggregation;

D O I：

10.1016/j.jsb.2003.11.016

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：

ClpB and Hsp104 (ClpB/Hsp104) are essential proteins of the heat-shock response and belong to the class 1 family of Clp/Hsp100 AAA(+) ATPases. Members of this family form large ring structures and contain two AAA(+) modules, which consist of a RecA-like nucleotide-binding domain (NBD) and an alpha-helical domain. Furthermore, ClpB/Hsp104 has a longer middle region, the ClpB/ Hsp104-linker, which is essential for chaperone activity. Unlike other Clp/Hsp100 proteins, however, ClpB/Hspl04 neither associates with a cellular protease nor directs the degradation of its substrate proteins. Rather, ClpB/Hsp104 is a bona fide molecular chaperone.. which has the remarkable ability to rescue proteins from an aggregated state. The full recovery of these proteins requires the assistance of the cognate DnaK/Hsp70 chaperone system. The mechanism of this "bi-chaperone" network, however, remains elusive. Here we review the current understanding of the structure-function relationship of the ClpB/Hsp104 molecular chaperone and its role in protein disaggregation. (C) 2003 Elsevier Inc. All rights reserved.

引用

页码：99 / 105

页数：7

共 55 条

[1] Structure and activity of ClpB from Escherichia coli -: Role of the amino- and carboxyl-terminal domains [J].

Barnett, ME ;

Zolkiewska, A ;

Zolkiewski, M .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (48) :37565-37571

[2] The N terminus of C1pB from Thermus thermophilus is not essential for the chaperone activity [J].

Beinker, P ;

Schlee, S ;

Groemping, Y ;

Seidel, R ;

Reinstein, J .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (49) :47160-47166

[3] At sixes and sevens: Characterization of the symmetry mismatch of the ClpAP chaperone-assisted protease [J].

Beuron, F ;

Maurizi, MR ;

Belnap, DM ;

Kocsis, E ;

Booy, FP ;

Kessel, M ;

Steven, AC .

JOURNAL OF STRUCTURAL BIOLOGY, 1998, 123 (03) :248-259

[4] The structures of HsIU and ATP-dependent protease HsIU-HsIV [J].

Bochtler, M ;

Hartmann, C ;

Song, HK ;

Bourenkov, GP ;

Bartunik, HD ;

Huber, R .

NATURE, 2000, 403 (6771) :800-805

[5] Defining a pathway of communication from the C-terminal peptide binding domain to the N-terminal ATPase domain in a AAA protein [J].

Cashikar, AG ;

Schirmer, EC ;

Hattendorf, DA ;

Glover, R ;

Ramakrishnan, MS ;

Ware, DM ;

Lindquist, SL .

MOLECULAR CELL, 2002, 9 (04) :751-760

[6] The truncated form of the bacterial heat shock protein ClpB/HSP100 contributes to development of thermotolerance in the cyanobacterium Synechococcus sp strain PCC 7942 [J].

Clarke, AK ;

Eriksson, MJ .

JOURNAL OF BACTERIOLOGY, 2000, 182 (24) :7092-7096

[7] Complete structure of p97/valosin-containing protein reveals communication between nucleotide domains [J].

DeLaBarre, B ;

Brunger, AT .

NATURE STRUCTURAL BIOLOGY, 2003, 10 (10) :856-863

[8] Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machinery [J].

Diamant, S ;

Ben-Zvi, AP ;

Bukau, B ;

Goloubinoff, P .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (28) :21107-21113

[9] Protein folding and degradation in bacteria: To degrade or not to degrade? That is the question [J].

Dougan, DA ;

Mogk, A ;

Bukau, B .

CELLULAR AND MOLECULAR LIFE SCIENCES, 2002, 59 (10) :1607-1616

[10] AAA plus proteins and substrate recognition, it all depends on their partner in crime [J].

Dougan, DA ;

Mogk, A ;

Zeth, K ;

Turgay, K ;

Bukau, B .

FEBS LETTERS, 2002, 529 (01) :6-10

← 1 2 3 4 5 6 →