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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Adenosine Diphosphate / metabolism
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Adenosine Triphosphate / metabolism
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Animals
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Chaperonin 10 / chemistry
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Chaperonin 10 / isolation & purification
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Chaperonin 10 / metabolism*
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Chaperonin 60 / chemistry
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Chaperonin 60 / isolation & purification
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Chaperonin 60 / metabolism*
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Chaperonins / metabolism*
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Cross-Linking Reagents
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Kinetics
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Macromolecular Substances
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Malate Dehydrogenase / chemistry
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Malate Dehydrogenase / metabolism
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Mitochondria, Heart / enzymology
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Protein Folding*
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
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Ribulose-Bisphosphate Carboxylase / chemistry
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Ribulose-Bisphosphate Carboxylase / metabolism
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Swine
Substances
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Chaperonin 10
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Chaperonin 60
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Cross-Linking Reagents
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Macromolecular Substances
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Recombinant Proteins
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Adenosine Diphosphate
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Adenosine Triphosphate
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Malate Dehydrogenase
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Chaperonins
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Ribulose-Bisphosphate Carboxylase