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Rivenzon-Segal, D., Wolf, S.G., Shimon, L., Willison. K.R. and Horovitz, A. (2005) Sequential ATP-induced allosteric transitions of the cytoplasmic chaperonin containing TCP-1 revealed by EM analysis. Nature Structural and Molecular Biologlogy, 12, 233-237. doi:10.1038/nsmb901

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• TITLE: Cytosolic chaperonin CCT possesses GTPase activity

  AUTHORS: Susumu Noguchi, Kazuyoshi Toyoshima, Soh Yamamoto, Toshio Miyazaki, Michiro Otaka, Sumio Watanabe, Katsunori Imai, Haruki Senoo, Ryoji Kobayashi, Mitsutoshi Jikei, Yasushi Kawata, Hiroshi Kubota, Hideaki Itoh

  KEYWORDS: Chaperonin; Molecular Chaperone; Protein Folding, Gtp

  JOURNAL NAME: American Journal of Molecular Biology, Vol.1 No.3, October 11, 2011

  ABSTRACT: Cytosolic chaperonin CCT (also known as TRiC) is a hetero-oligomeric cage-like molecular chaperone that assists in protein folding by ATPase cycle-dependent conformational changes. However, role of the nucleo-tide binding and hydrolysis in CCT-assisted protein folding is still poorly understood. We purified CCT by using ATP-Sepharose and other columns, and found that CCT possesses ability to hydrolyze GTP, with an activity level very similar to the ATPase activity. CCT was more resistant to proteinase K treatment in the presence of GTP or ATP. These results suggest that the GTPase activity of CCT may play a role in chaperone-assisted protein folding.