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Corrales FJ, Fersht AR. Toward a mechanism for GroEL.GroES chaperone activity: an ATPase-gated and -pulsed folding and annealing cage. Proc Natl Acad Sci U S A. 1996;93(9):4509-12doi: 10.1073/pnas.93.9.4509.
Corrales, F. J., & Fersht, A. R. (1996). Toward a mechanism for GroEL.GroES chaperone activity: an ATPase-gated and -pulsed folding and annealing cage. Proceedings of the National Academy of Sciences of the United States of America, 93(9), 4509-12. https://doi.org/10.1073/pnas.93.9.4509
Corrales, F J, and Fersht, A R. "Toward a mechanism for GroEL.GroES chaperone activity: an ATPase-gated and -pulsed folding and annealing cage." Proceedings of the National Academy of Sciences of the United States of America vol. 93,9 (1996): 4509-12. doi: https://doi.org/10.1073/pnas.93.9.4509
Corrales FJ, Fersht AR. Toward a mechanism for GroEL.GroES chaperone activity: an ATPase-gated and -pulsed folding and annealing cage. Proc Natl Acad Sci U S A. 1996 Apr 30;93(9):4509-12. doi: 10.1073/pnas.93.9.4509. PMID: 8633099; PMCID: PMC39569.
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Proc Natl Acad Sci U S A. 1996 Apr 30;93(9):4509-12. doi: 10.1073/pnas.93.9.4509.

Toward a mechanism for GroEL.GroES chaperone activity: an ATPase-gated and -pulsed folding and annealing cage.

Proceedings of the National Academy of Sciences of the United States of America

F J Corrales, A R Fersht

Affiliations

  1. Medical Research Council Unit for Protein Function and Design, University of Cambridge, United Kingdom.

PMID: 8633099 PMCID: PMC39569 DOI: 10.1073/pnas.93.9.4509
Free PMC Article

Abstract

Free GroEL binds denatured proteins very tightly: it retards the folding of barnase 400-fold and catalyzes unfolding fluctuations in native barnase and its folding intermediate. GroEL undergoes an allosteric transition from its tight-binding T-state to a weaker binding R-state on the cooperative binding of nucleotides (ATP/ADP) and GroES. The preformed GroEL.GroES.nucleotide complex retards the folding of barnase by only a factor of 4, and the folding rate is much higher than the ATPase activity that releases GroES from the complex. Binding of GroES and nucleotides to a preformed GroEL.denatured-barnase complex forms an intermediately fast-folding complex. We propose the following mechanism for the molecular chaperone. Denatured proteins bind to the resting GroEL.GroES.nucleotide complex. Fast-folding proteins are ejected as native structures before ATP hydrolysis. Slow-folding proteins enter chaperoning cycles of annealing and folding after the initial ATP hydrolysis. This step causes transient release of GroES and formation of the GroEL.denatured-protein complexes with higher annealing potential. The intermediately fast-folding complex is formed on subsequent rebinding of GroES. The ATPase activity of GroEL.GroES is thus the gatekeeper that selects for initial entry of slow-folding proteins to the chaperone action and then pumps successive transitions from the faster-folding R-states to the tighter-binding/stronger annealing T-states. The molecular chaperone acts as a combination of folding cage and an annealing machine.

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