Gymnastics of Molecular Chaperones

被引:279
作者
Mayer, Matthias P. [1 ]
机构
[1] Univ Heidelberg ZMBH, Zentrum Mol Biol, DKFZ ZMBH Allianz, D-69120 Heidelberg, Germany
关键词
HSP70 NUCLEOTIDE EXCHANGE; ESCHERICHIA-COLI HSP90; CRYSTAL-STRUCTURE; ATP HYDROLYSIS; IN-VIVO; STRUCTURAL BASIS; CONFORMATIONAL DYNAMICS; EUKARYOTIC CHAPERONIN; ALLOSTERIC REGULATION; SUBSTRATE-BINDING;
D O I
10.1016/j.molcel.2010.07.012
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
Molecular chaperones assist folding processes and conformational changes in many proteins. In order to do so, they progress through complex conformational cycles themselves. In this review, I discuss the diverse conformational dynamics of the ATP-dependent chaperones of the Hsp60, Hsp70, Hsp90, and Hsp100 families. © 2010 Elsevier Inc.
引用
收藏
页码:321 / 331
页数:11
相关论文
共 83 条
[1]   Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex [J].
Ali, MMU ;
Roe, SM ;
Vaughan, CK ;
Meyer, P ;
Panaretou, B ;
Piper, PW ;
Prodromou, C ;
Pearl, LH .
NATURE, 2006, 440 (7087) :1013-1017
[2]   Chaperoning checkpoint kinase 1 (Chk1), an Hsp90 client, with purified chaperones [J].
Arlander, SJH ;
Felts, SJ ;
Wagner, JM ;
Stensgard, B ;
Toft, DO ;
Karnitz, LM .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2006, 281 (05) :2989-2998
[3]   Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate [J].
Bertelsen, Eric B. ;
Chang, Lyra ;
Gestwicki, Jason E. ;
Zuiderweg, Erik R. P. .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2009, 106 (21) :8471-8476
[4]   Allostery in Hsp70 Chaperones Is Transduced by Subdomain Rotations [J].
Bhattacharya, Akash ;
Kurochkin, Alexander V. ;
Yip, Grover N. B. ;
Zhang, Yongbo ;
Bertelsen, Eric B. ;
Zuiderweg, Erik R. P. .
JOURNAL OF MOLECULAR BIOLOGY, 2009, 388 (03) :475-490
[5]   Cooperativity in the thermosome [J].
Bigotti, MG ;
Clarke, AR .
JOURNAL OF MOLECULAR BIOLOGY, 2005, 348 (01) :13-26
[6]   Mechanism of lid closure in the eukaryotic chaperonin TRiC/CCT [J].
Booth, Christopher R. ;
Meyer, Anne S. ;
Cong, Yao ;
Topf, Maya ;
Sali, Andrej ;
Ludtke, Steven J. ;
Chiu, Wah ;
Frydman, Judith .
NATURE STRUCTURAL & MOLECULAR BIOLOGY, 2008, 15 (07) :746-753
[7]   THE CRYSTAL-STRUCTURE OF THE BACTERIAL CHAPERONIN GROEL AT 2.8-ANGSTROM [J].
BRAIG, K ;
OTWINOWSKI, Z ;
HEGDE, R ;
BOISVERT, DC ;
JOACHIMIAK, A ;
HORWICH, AL ;
SIGLER, PB .
NATURE, 1994, 371 (6498) :578-586
[8]   Tuning of chaperone activity of Hsp70 proteins by modulation of nucleotide exchange [J].
Brehmer, D ;
Rüdiger, S ;
Gässler, CS ;
Klostermeier, D ;
Packschies, L ;
Reinstein, J ;
Mayer, MP ;
Bukau, B .
NATURE STRUCTURAL BIOLOGY, 2001, 8 (05) :427-432
[9]   Multiple states of a nucleotide-bound group 2 chaperonin [J].
Clare, Daniel K. ;
Stagg, Scott ;
Quispe, Joel ;
Farr, George W. ;
Horwich, Arthur L. ;
Saibil, Helen R. .
STRUCTURE, 2008, 16 (04) :528-534
[10]   Structures of GRP94-Nucleotide complexes reveal mechanistic differences between the hsp90 chaperones [J].
Dollins, D. Eric ;
Warren, Joshua J. ;
Immormino, Robert M. ;
Gewirth, Daniel T. .
MOLECULAR CELL, 2007, 28 (01) :41-56