The Protein-folding Activity of Chaperonins Correlates with the Symmetric GroEL14(GroES7)2 Heterooligomer

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 1995 Dec 19

PMID 8618836

Citations 34

Authors

A Azem

S Diamant

M Kessel

C Weiss

P Goloubinoff

Affiliations

Soon will be listed here.

Abstract

Chaperonins GroEL and GroES form, in the presence of ATP, two types of heterooligomers in solution: an asymmetric GroEL14GroES7 "bullet"-shaped particle and a symmetric GroEL14(GroES7)2 "football"-shaped particle. Under limiting concentrations of ATP or GroES, excess ADP, or in the presence of 5'-adenylyl imidodiphosphate, a correlation is seen between protein folding and the amount of symmetric GroEL14(GroES7)2 particles in a chaperonin solution, as detected by electron microscopy or by chemical crosslinking. Kinetic analysis suggests that protein folding is more efficient when carried out by a chaperonin solution populated with a majority of symmetric GroEL14(GroES7)2 particles than by a majority of asymmetric GroEL14GroES7 particles. The symmetric heterooligomer behaves as a highly efficient intermediate of the chaperonin protein folding cycle in vitro.

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