The affinity of the GroEL/GroES complex for peptides under conditions of protein folding.
The affinity of four short peptides for the Escherichia coli molecular chaperone GroEL was studied in the presence of the co-chaperone GroES and nucleotides. Our data show that binding of GroES to one ring enhances the interaction of the peptides with the opposite GroEL ring, a finding that was related to the structural readjustments in GroEL following GroES binding. We further report that the GroEL/GroES complex has a high affinity for peptides during ATP hydrolysis when protein substrates would undergo repeated cycles of assisted folding. Although we could not determine at which step(s) during the cycle our peptides interacted with GroEL, we propose that successive state changes in GroEL during ATP hydrolysis may create high affinity complexes and ensure maximum efficiency of the chaperone machinery under conditions of protein folding.
Preuss
M
M
Imperial College Genetic Therapies Centre, Department of Chemistry, Imperial College of Science, Technology and Medicine, South Kensington, London, UK.
Miller
A D
AD
D000244:Adenosine Diphosphate / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D018835:Chaperonin 10 / Q000737:chemistry / Q000378:metabolism*; D018834:Chaperonin 60 / Q000737:chemistry / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism; D006868:Hydrolysis; D046911:Macromolecular Substances; D008954:Models, Biological; D010455:Peptides / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D017510:Protein Folding
D018835:Chaperonin 10; D018834:Chaperonin 60; D046911:Macromolecular Substances; D010455:Peptides; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate