Cytosolic chaperonin CCT possesses GTPase activity

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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DOI: 10.4236/ajmb.2011.13013                

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.

Keywords

Chaperonin; Molecular Chaperone; Protein Folding, Gtp

Conflicts of Interest

The authors declare no conflicts of interest.

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