NDLI: Coupling between protein folding and allostery in the GroE chaperonin system.

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Coupling between protein folding and allostery in the GroE chaperonin system.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Horovitz, A. Yifrach, O.
Description	Author Affiliation: Yifrach O ( Department of Structural Biology, Weizmann Institute of Science, Rehovot 76100, Israel.);
Abstract	GroEL is an allosteric protein that facilitates protein folding in an ATP-dependent manner. Herein, the relationship between cooperative ATP binding by GroEL and the kinetics of GroE-assisted folding of two substrates with different GroES dependence, mouse dihydrofolate reductase (mDHFR) and mitochondrial malate dehydrogenase, is examined by using cooperativity mutants of GroEL. Strong intra-ring positive cooperativity in ATP binding by GroEL decreases the rate of GroEL-assisted mDHFR folding owing to a slow rate of the ATP-induced transition from the protein-acceptor state to the protein-release state. Inter-ring negative cooperativity in ATP binding by GroEL is found to affect the kinetic partitioning of mDHFR, but not of mitochondrial malate dehydrogenase, between folding in solution and folding in the cavity underneath GroES. Our results show that protein folding by this 'two-stroke motor' is coupled to cooperative ATP binding.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	4
Volume Number	97
Language	English
Publisher	National Academy of Sciences
Publisher Date	2000-03-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Chaperonin 60 Chemistry Chaperonins Protein Folding Adenosine Triphosphate Metabolism Allosteric Regulation Animals Genetics Kinetics Malate Dehydrogenase Mice Mitochondria Enzymology Mutation Protein Binding Protein Conformation Tetrahydrofolate Dehydrogenase Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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