Abstract
The incubation of chaperonins cpn60 (GroEL) and cpn10 (GroES) from E. coli in the presence of Mg-ATP and KCl generates the formation, as revealed by electron microscopy, of GroEL-GroES complexes with a symmetrical shape in which one toroidal GroES oligomer is bound to each end of the tetradecameric GroEL aggregate (1:2 GroEL:GroES oligomer molar ratio). The symmetrical complexes are not observed in the presence of ADP or the non-hydrolyzable ATP analog, ATP gamma S, where only asymmetrical complexes (1:1 GroEL:GroES oligomer molar ratio) are formed. These results suggest that ATP hydrolysis is required for the formation of symmetrical complexes.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Triphosphate / metabolism*
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Animals
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Bacterial Proteins / chemistry
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Bacterial Proteins / metabolism*
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Bacterial Proteins / ultrastructure
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Cattle
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Chaperonin 10
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Chaperonin 60
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Escherichia coli / metabolism*
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Heat-Shock Proteins / chemistry
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Heat-Shock Proteins / metabolism*
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Heat-Shock Proteins / ultrastructure
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Kinetics
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Liver / enzymology
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Microscopy, Electron
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Protein Binding
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Protein Denaturation
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Protein Folding
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Thiosulfate Sulfurtransferase / chemistry
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Thiosulfate Sulfurtransferase / metabolism
Substances
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Bacterial Proteins
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Chaperonin 10
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Chaperonin 60
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Heat-Shock Proteins
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Adenosine Triphosphate
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Thiosulfate Sulfurtransferase