Molecular chaperones: containers and surfaces for folding, stabilising or unfolding proteins

被引：97

作者：

Saibil, H ^{[1
]}

机构：

[1] Univ London Birkbeck Coll, Dept Crystallog, London WC1E 7HX, England

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2000年 / 10卷 / 02期

关键词：

D O I：

10.1016/S0959-440X(00)00074-9

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：

Newly solved chaperone structures include the thermosome, a group II chaperonin, and a small heat-shock protein. Novel ideas on chaperone mechanism are presented in the forced unfolding hypothesis of GroEL action. Structures of chaperone-pilin complexes reveal the mechanism of chaperone interaction in bacterial pilus assembly and there have been major advances in understanding the structure and function of Hsp 100 unfoldases.

引用

页码：251 / 258

页数：8

共 63 条

[51] HSP100/Clp proteins: A common mechanism explains diverse functions [J].

Schirmer, EC ;

Glover, JR ;

Singer, MA ;

Lindquist, S .

TRENDS IN BIOCHEMICAL SCIENCES, 1996, 21 (08) :289-296

[52] Three conformations of an archaeal chaperonin, TF55 from Sulfolobus shibatae [J].

Schoehn, G ;

Quaite-Randall, E ;

Jiménez, JL ;

Joachimiak, A ;

Saibil, HR .

JOURNAL OF MOLECULAR BIOLOGY, 2000, 296 (03) :813-819

[53] Chaperonin function: Folding by forced unfolding [J].

Shtilerman, M ;

Lorimer, GH ;

Englander, SW .

SCIENCE, 1999, 284 (5415) :822-825

[54] Structure and function in GroEL-mediated protein folding [J].

Sigler, PB ;

Xu, ZH ;

Rye, HS ;

Burston, SG ;

Fenton, WA ;

Horwich, AL .

ANNUAL REVIEW OF BIOCHEMISTRY, 1998, 67 :581-608

[55] DYNAMICS OF THE CHAPERONIN ATPASE CYCLE - IMPLICATIONS FOR FACILITATED PROTEIN-FOLDING [J].

TODD, MJ ;

VIITANEN, PV ;

LORIMER, GH .

SCIENCE, 1994, 265 (5172) :659-666

[56] Global unfolding of a substrate protein by the Hsp100 chaperone ClpA [J].

Weber-Ban, EU ;

Reid, BG ;

Miranker, AD ;

Horwich, AL .

NATURE, 1999, 401 (6748) :90-93

[57] GROEL-MEDIATED PROTEIN-FOLDING PROCEEDS BY MULTIPLE ROUNDS OF BINDING AND RELEASE OF NONNATIVE FORMS [J].

WEISSMAN, JS ;

KASHI, Y ;

FENTON, WA ;

HORWICH, AL .

CELL, 1994, 78 (04) :693-702

[58] The crystal structure of the asymmetric GroEL-GroES-(ADP)(7) chaperonin complex [J].

Xu, ZH ;

Horwich, AL ;

Sigler, PB .

NATURE, 1997, 388 (6644) :741-750

[59] Transient kinetic analysis of adenosine 5′-triphosphate binding-induced conformational changes in the allosteric chaperonin GroEL [J].

Yifrach, O ;

Horovitz, A .

BIOCHEMISTRY, 1998, 37 (20) :7083-7088

[60] NESTED COOPERATIVITY IN THE ATPASE ACTIVITY OF THE OLIGOMERIC CHAPERONIN GROEL [J].

YIFRACH, O ;

HOROVITZ, A .

BIOCHEMISTRY, 1995, 34 (16) :5303-5308

← 1 2 3 4 5 6 7 →