Putting a lid on protein folding: Structure and function of the co-chaperonin, GroES

被引：17

作者：

Fenton, WA ^{[1
]}

Weissman, JS ^{[1
]}

Horwich, AL ^{[1
]}

机构：

[1] YALE UNIV,SCH MED,HOWARD HUGHES MED INST,NEW HAVEN,CT 06520

来源：

CHEMISTRY & BIOLOGY | 1996年 / 3卷 / 03期

关键词：

D O I：

10.1016/S1074-5521(96)90257-4

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 co-chaperonin GroES is an essential partner in protein folding mediated by the chaperonin, GroEL. Two recent crystal structures of GroES provide a structural basis to understand how GroES forms the lid on the folding-active cis ternary complex, and how the GroEL-GroES complex enhances folding.

引用

页码：157 / 161

页数：5

共 37 条

[1] The protein-folding activity of chaperonins correlates with the symmetric GroEL(14)(GroES(7))(2) heterooligomer [J].

Azem, A ;

Diamant, S ;

Kessel, M ;

Weiss, C ;

Goloubinoff, P .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1995, 92 (26) :12021-12025

[2]

BOCHKAREVA ES, 1992, J BIOL CHEM, V267, P6796

[3]

BOCHKAREVA ES, 1992, J BIOL CHEM, V267, P25672

[4] 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

[5] A POLYPEPTIDE BOUND BY THE CHAPERONIN GROEL IS LOCALIZED WITHIN A CENTRAL CAVITY [J].

BRAIG, K ;

SIMON, M ;

FURUYA, F ;

HAINFELD, JF ;

HORWICH, AL .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1993, 90 (09) :3978-3982

[6] THE ORIGINS AND CONSEQUENCES OF ASYMMETRY IN THE CHAPERONIN REACTION CYCLE [J].

BURSTON, SG ;

RANSON, NA ;

CLARKE, AR .

JOURNAL OF MOLECULAR BIOLOGY, 1995, 249 (01) :138-152

[7] LOCATION OF A FOLDING PROTEIN AND SHAPE CHANGES IN GROEL-GROES COMPLEXES IMAGED BY CRYOELECTRON MICROSCOPY [J].

CHEN, S ;

ROSEMAN, AM ;

HUNTER, AS ;

WOOD, SP ;

BURSTON, SG ;

RANSON, NA ;

CLARKE, AR ;

SAIBIL, HR .

NATURE, 1994, 371 (6494) :261-264

[8] THE GROES AND GROEL HEAT-SHOCK GENE-PRODUCTS OF ESCHERICHIA-COLI ARE ESSENTIAL FOR BACTERIAL-GROWTH AT ALL TEMPERATURES [J].

FAYET, O ;

ZIEGELHOFFER, T ;

GEORGOPOULOS, C .

JOURNAL OF BACTERIOLOGY, 1989, 171 (03) :1379-1385

[9] RESIDUES IN CHAPERONIN GROEL REQUIRED FOR POLYPEPTIDE BINDING AND RELEASE [J].

FENTON, WA ;

KASHI, Y ;

FURTAK, K ;

HORWICH, AL .

NATURE, 1994, 371 (6498) :614-619

[10] PROTEIN FOLDING IN THE CELL [J].

GETHING, MJ ;

SAMBROOK, J .

NATURE, 1992, 355 (6355) :33-45

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