Molecular chaperone;
Chaperonin;
Protein folding;
GroEL;
GroES;
CRYSTAL-STRUCTURE;
CHAPERONIN GROEL;
ESCHERICHIA-COLI;
MOBILE LOOP;
HEAT-SHOCK;
POLYPEPTIDE;
SUBSTRATE;
BINDING;
D O I:
10.1016/j.febslet.2009.06.027
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 chaperonin GroEL contains two seven-subunit rings, and allosteric signals between them are required to complete the GroEL reaction cycle. For this reason SR1, a mutant of GroEL that forms only single rings, cannot function as a chaperone. Mutations in SR1 that restore chaperone function weaken its interaction with the cochaperonin GroES. We predicted that GroES mutants with reduced affinity for GroEL would also restore function to SR1. To test this, we mutated residues in GroES in and near its contact site with GroEL. Nearly half of the mutants showed partial function with SR1. Two mutants were confirmed to have reduced affinity for GroEL. Intriguingly, some GroES mutants were able to function with active single ring mutants of GroEL. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.