Cytosolic chaperonin CCT possesses GTPase activity

• 作者: Haruki Senoo Hideaki Itoh Hiroshi Kubota Katsunori Imai Kazuyoshi Toyoshima Michiro Otaka Mitsutoshi Jikei Ryoji Kobayashi Soh Yamamoto Sumio Watanabe Susumu Noguchi Toshio Miyazaki Yasushi Kawata
• 来源期刊: 美国分子生物学期刊(英文)
• 学科: 医学
• 关键词: CHAPERONIN Molecular CHAPERONE Protein FOLDING GTP
• 年，卷（期）: 2011,（3）
• 页码范围: 123-130
• 页数: 8页
• 分类号: R73

摘要

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.