Article: article from journal or magazin.
The protein-folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 heterooligomer.
Proceedings of the National Academy of Sciences of the United States of America
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.
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
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