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Inter-ring communication is dispensable in the reaction cycle of group II chaperonins.

Journal of molecular biology (2014-05-27)
Yohei Y Yamamoto, Yuki Abe, Kazuki Moriya, Mayuno Arita, Keiichi Noguchi, Noriyuki Ishii, Hiroshi Sekiguchi, Yuji C Sasaki, Masafumi Yohda
ABSTRACT

Chaperonins are ubiquitous molecular chaperones with the subunit molecular mass of 60kDa. They exist as double-ring oligomers with central cavities. An ATP-dependent conformational change of the cavity induces the folding of an unfolded protein that is captured in the cavity. In the group I chaperonins, which are present in eubacteria and eukaryotic organelles, inter-ring communication takes important role for the reaction cycle. However, there has been limited study on the inter-ring communication in the group II chaperonins that exist in archaea and the eukaryotic cytosol. In this study, we have constructed the asymmetric ring complex of a group II chaperonin using circular permutated covalent mutants. Although one ring of the asymmetric ring complex lacks ATPase or ATP binding activity, the other wild-type ring undergoes an ATP-dependent conformational change and maintains protein-folding activity. The results clearly demonstrate that inter-ring communication is dispensable in the reaction cycle of group II chaperonins.

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