Noguchi, SusumuToyoshima, KazuyoshiYamamoto, SohMiyazaki, ToshioOtaka, MichiroWatanabe, SumioImai, KatsunoriSenoo, HarukiKobayashi, RyojiJikei, MitsutoshiKawata, YasushiKubota, HiroshiItoh, Hideaki2016-10-182016-10-182011-10American Journal of Molecular Biology, 2011, 1, 123-130http://dx.doi.org/10.4236/ajmb.2011.13013http://hdl.handle.net/123456789/973Cytosolic 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.enChaperoninMolecular ChaperoneProtein FoldingGtpArticle