Chaperonin implicated in mitochondrial protein import andmacromolecular assembly. Together with Hsp10, facilitates the correctfolding of imported proteins. May also prevent misfolding and promotethe refolding and proper assembly of unfolded polypeptides generatedunder stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist ofheptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bindone unfolded substrate protein per ring, followed by the binding of ATPand association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the innercavity of Hsp60 where, for a certain period of time, it can foldundisturbed by other cell components. Synchronous hydrolysis of ATP inall Hsp60 subunits results in the dissociation of the chaperonin ringsand the release of ADP and the folded substrate protein. [1-3]

MLRLPTVFRQMRPVSRVLAPHLTRAYAKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTNEEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKEIGNIISDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSIQSIVPALEIANAHRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEGLTLNLEDVQPHDLGKVGEVIVTKDDAMLLKGKGDKAQIEKRIQEIIEQLDVTTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDALNATRAAVEEGIVLGGGCALLRCIPALDSLTPANEDQKIGIEIIKRTLKIPAMTIAKNAGVEGSLIVEKIMQSSSEVGYDAMAGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEVVVTEIPKEEKDPGMGAMGGMGGGMGGGMF