The protein-folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 heterooligomer.
Details
Serval ID
serval:BIB_D435AE9527B2
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
The protein-folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 heterooligomer.
Journal
Proceedings of the National Academy of Sciences of the United States of America
ISSN
0027-8424 (Print)
ISSN-L
0027-8424
Publication state
Published
Issued date
1995
Volume
92
Number
26
Pages
12021-12025
Language
english
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.
Keywords
Adenosine Diphosphate/metabolism, Adenosine Triphosphate/metabolism, Animals, Chaperonin 10/chemistry, Chaperonin 10/isolation & purification, Chaperonin 60/chemistry, Chaperonin 60/isolation & purification, Chaperonins/metabolism, Cross-Linking Reagents, Kinetics, Macromolecular Substances, Malate Dehydrogenase/chemistry, Malate Dehydrogenase/metabolism, Mitochondria, Heart/enzymology, Protein Folding, Recombinant Proteins/chemistry, Recombinant Proteins/metabolism, Ribulose-Bisphosphate Carboxylase/chemistry, Ribulose-Bisphosphate Carboxylase/metabolism, Swine
Pubmed
Web of science
Open Access
Yes
Create date
24/01/2008 21:02
Last modification date
20/08/2019 16:54