The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding
- 1 November 1993
- journal article
- Published by Springer Nature in Nature
- Vol. 366 (6452) , 228-233
- https://doi.org/10.1038/366228a0
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
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