The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding
NaturePublished 1 November 1993
Jörg Martin, Mark Mayhew, Thomas Langer, Ulrich Hartl
Citations291
SJR quartileQ1
SJR score18.29
SNIP10.16
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TL;DR
The reaction mechanism of protein folding by the chaperonin GroEL and its regulator GroES has been defined and partially folded protein rebinds to the chacheronin, thus perpetuating the cycle until folding is complete.
Abstract
The reaction mechanism of protein folding by the chaperonin GroEL and its regulator GroES has been defined. GroES and substrate protein counteract each other's effects on GroEL: whereas GroES stabilizes GroEL in the ADP-bound state, binding of unfolded polypeptide within the cavity of the GroEL cylinder triggers ADP and GroES release. Upon ADP-ATP exchange, GroES reassociates with GroEL and ATP hydrolysis discharges the bound protein for folding. Partially folded protein rebinds to the chaperonin, thus perpetuating the cycle until folding is complete.
Keywords
Materials ScienceBiochemistry, Genetics and Molecular Biology
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