GroEL-GroES-mediated protein folding

被引:209
作者
Horwich, Arthur L.
Farr, George W.
Fenton, Wayne A.
机构
[1] Yale Univ, Sch Med, Dept Genet, Boyer Ctr, New Haven, CT 06510 USA
[2] Yale Univ, Sch Med, Boyer Ctr, Howard Hughes Med Inst, New Haven, CT 06510 USA
[3] Scripps Res Inst, La Jolla, CA 92037 USA
关键词
D O I
10.1021/cr040435v
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
A review of the mechanism of protein refolding by GroEL-GroES machine is presented. Topics discussed include: chaperonins, specifically the establishment of a role on mediating protein folding in the cell; structural states of GroEL and the GroEL-GroES reaction cycle; and triggering productive folding. Under the second topic, focus is on the architecture of GroEL and GroES, polypeptide binding to a GroEL ring, and rigid body movements of GroEL during the reaction cycle. For the third topic, emphasis is on cis ternary complexes formation, GroEL-GroES formation, nature of the polypeptide load, and the polypeptide-GroEL-GroES-ADP complex as representative collision state.
引用
收藏
页码:1917 / 1930
页数:14
相关论文
共 95 条
[1]   PRINCIPLES THAT GOVERN FOLDING OF PROTEIN CHAINS [J].
ANFINSEN, CB .
SCIENCE, 1973, 181 (4096) :223-230
[2]   PROTEIN-SYNTHESIS IN CHLOROPLASTS .9. ASSEMBLY OF NEWLY-SYNTHESIZED LARGE SUBUNITS INTO RIBULOSE BISPHOSPHATE CARBOXYLASE IN ISOLATED INTACT PEA-CHLOROPLASTS [J].
BARRACLOUGH, R ;
ELLIS, RJ .
BIOCHIMICA ET BIOPHYSICA ACTA, 1980, 608 (01) :19-31
[3]   GroEL channels the folding of thioredoxin along one kinetic route [J].
Bhutani, N ;
Udgaonkar, JB .
JOURNAL OF MOLECULAR BIOLOGY, 2001, 314 (05) :1167-1179
[4]   FLUORIDE COMPLEXES OF ALUMINUM OR BERYLLIUM ACT ON G-PROTEINS AS REVERSIBLY BOUND ANALOGS OF THE GAMMA-PHOSPHATE OF GTP [J].
BIGAY, J ;
DETERRE, P ;
PFISTER, C ;
CHABRE, M .
EMBO JOURNAL, 1987, 6 (10) :2907-2913
[5]  
BOCHKAREVA ES, 1992, J BIOL CHEM, V267, P6796
[6]   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
[7]   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
[8]   Dual function of protein confinement in chaperonin-assisted protein folding [J].
Brinker, A ;
Pfeifer, G ;
Kerner, MJ ;
Naylor, DJ ;
Hartl, FU ;
Hayer-Hartl, M .
CELL, 2001, 107 (02) :223-233
[9]   A structural model for GroEL-polypeptide recognition [J].
Buckle, AM ;
Zahn, R ;
Fersht, AR .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1997, 94 (08) :3571-3575
[10]   A CARBOXY-TERMINAL DELETION IMPAIRS THE ASSEMBLY OF GROEL AND CONFERS A PLEIOTROPIC PHENOTYPE IN ESCHERICHIA-COLI K-12 [J].
BURNETT, BP ;
HORWICH, AL ;
LOW, KB .
JOURNAL OF BACTERIOLOGY, 1994, 176 (22) :6980-6985