Molecular mechanisms of a multifunctional AAA protein, p97
| Project/Area Number |
20770106
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Functional biochemistry
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| Research Institution | Kumamoto University |
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Principal Investigator |
ESAKI Masatoshi Kumamoto University, 発生医学研究所, 助教 (70437911)
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| Project Period (FY) |
2008 – 2009
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| Project Status |
Completed (Fiscal Year 2009)
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| Budget Amount *help |
¥4,160,000 (Direct Cost: ¥3,200,000、Indirect Cost: ¥960,000)
Fiscal Year 2009: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2008: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
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| Keywords | AAA / ATPase / 分子シャペロン / 出芽酵母 / AAAタンパク / p97 / ミトコンドリア / 協同性 / AAAタンパク質 |
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| Research Abstract |
P97 is an essential AAA ATPase that is required for many cellular processes, and is identified as a causative gene for an autosomal dominant human disorder, inclusion body myopathy associated with Paget's disease of the bone and frontotemporal dementia. P97 possesses two AAA domains, in which disease-related mutations are mostly found in the N-terminal half. In this study, effects of mutations defective in ATPase activity in each AAA domain on the function of yeast p97 were analyzed. In this result, it is found that the C-terminal AAA domain is essential for p97 functions, which is modulated by the N-terminal AAA domain.
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Report
(3 results)
Research Products
(28 results)
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[Journal Article] Roles of TOM70 in import of presequence-containing mitochondrial proteins2009
Author(s)
Hayashi Yamamoto, Kenji Fukui, Hisashi Takahashi, Shingo Kitamura, Takuya Shiota, Kayoko Terao, Mayumi Uchida, Masatoshi Esaki, Shuh-ichi Nishikawa, Tohru Yoshihisa, Koji Yamano, Toshiya Endo*
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Journal Title
J. Biol. Chem. 284
Pages: 31635-31646
Related Report
Peer Reviewed
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