Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding - PubMed (original) (raw)
. 1995 Aug 11;269(5225):836-41.
doi: 10.1126/science.7638601.
Affiliations
- PMID: 7638601
- DOI: 10.1126/science.7638601
Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding
M K Hayer-Hartl et al. Science. 1995.
Abstract
The chaperonins GroEL and GroES of Escherichia coli facilitate protein folding in an adenosine triphosphate (ATP)-dependent reaction cycle. The kinetic parameters for the formation and dissociation of GroEL-GroES complexes were analyzed by surface plasmon resonance. Association of GroES and subsequent ATP hydrolysis in the interacting GroEL toroid resulted in the formation of a stable GroEL:ADP:GroES complex. The complex dissociated as a result of ATP hydrolysis in the opposite GroEL toroid, without formation of a symmetrical GroEL:(GroES)2 intermediate. Dissociation was accelerated by the addition of unfolded polypeptide. Thus, the functional chaperonin unit is an asymmetrical GroEL:GroES complex, and substrate protein plays an active role in modulating the chaperonin reaction cycle.
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