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    Cytosolic chaperonin CCT possesses GTPase activity

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    Date
    2011-10
    Author
    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
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    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.
    URI
    http://dx.doi.org/10.4236/ajmb.2011.13013
    http://hdl.handle.net/123456789/973
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    • Biology and Biotechnology [193]

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