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  1. Home
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Browsing by Author "Senoo, Haruki"

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    Cytosolic chaperonin CCT possesses GTPase activity
    (Scientific Research Publishing, 2011-10) Noguchi, Susumu; Toyoshima, Kazuyoshi; Yamamoto, Soh; Miyazaki, Toshio; Otaka, Michiro; Watanabe, Sumio; Imai, Katsunori; Senoo, Haruki; Kobayashi, Ryoji; Jikei, Mitsutoshi; Kawata, Yasushi; Kubota, Hiroshi; Itoh, Hideaki
    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.

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