Author(s)

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

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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.

Chaperonin; Molecular Chaperone; Protein Folding, Gtp

Noguchi, S. , Toyoshima, K. , Yamamoto, S. , Miyazaki, T. , Otaka, M. , Watanabe, S. , Imai, K. , Senoo, H. , Kobayashi, R. , Jikei, M. , Kawata, Y. , Kubota, H. and Itoh, H. (2011) Cytosolic chaperonin CCT possesses GTPase activity. American Journal of Molecular Biology, 1, 123-130. doi: 10.4236/ajmb.2011.13013.