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Dual action of ATP hydrolysis couples lid closure to substrate release into the group II chaperonin chamber.


ABSTRACT: Group II chaperonins are ATP-dependent ring-shaped complexes that bind nonnative polypeptides and facilitate protein folding in archaea and eukaryotes. A built-in lid encapsulates substrate proteins within the central chaperonin chamber. Here, we describe the fate of the substrate during the nucleotide cycle of group II chaperonins. The chaperonin substrate-binding sites are exposed, and the lid is open in both the ATP-free and ATP-bound prehydrolysis states. ATP hydrolysis has a dual function in the folding cycle, triggering both lid closure and substrate release into the central chamber. Notably, substrate release can occur in the absence of a lid, and lid closure can occur without substrate release. However, productive folding requires both events, so that the polypeptide is released into the confined space of the closed chamber where it folds. Our results show that ATP hydrolysis coordinates the structural and functional determinants that trigger productive folding.

SUBMITTER: Douglas NR 

PROVIDER: S-EPMC3055171 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature

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Dual action of ATP hydrolysis couples lid closure to substrate release into the group II chaperonin chamber.

Douglas Nicholai R NR   Reissmann Stefanie S   Zhang Junjie J   Chen Bo B   Jakana Joanita J   Kumar Ramya R   Chiu Wah W   Frydman Judith J  

Cell 20110101 2


Group II chaperonins are ATP-dependent ring-shaped complexes that bind nonnative polypeptides and facilitate protein folding in archaea and eukaryotes. A built-in lid encapsulates substrate proteins within the central chaperonin chamber. Here, we describe the fate of the substrate during the nucleotide cycle of group II chaperonins. The chaperonin substrate-binding sites are exposed, and the lid is open in both the ATP-free and ATP-bound prehydrolysis states. ATP hydrolysis has a dual function i  ...[more]

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