| Project/Area Number |
09680691
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Cell biology
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| Research Institution | KYOTO UNIVERSITY |
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Principal Investigator |
AKIYAMA Yoshinori Kyoto Univ., Inst.Virus.Res., Instructor, ウイルス研究所, 助手 (10192460)
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| Co-Investigator(Kenkyū-buntansha) |
MORI Hiroyuki Kyoto Univ., Inst.Virus.Res., Instructor, ウイルス研究所, 助手 (10243271)
ITO Koreaki Kyoto Univ., Inst.Virus.Res., Professor, ウイルス研究所, 教授 (90027334)
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| Project Period (FY) |
1997 – 1998
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| Project Status |
Completed (Fiscal Year 1998)
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| Budget Amount *help |
¥3,400,000 (Direct Cost: ¥3,400,000)
Fiscal Year 1998: ¥2,000,000 (Direct Cost: ¥2,000,000)
Fiscal Year 1997: ¥1,400,000 (Direct Cost: ¥1,400,000)
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| Keywords | FtsH / stop tranfer / membrane proteins / FtsH / SecY / prlA |
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| Research Abstract |
(1st year) We constructed a model membrane protein, proOmpAl65-LacY(TM12)-PhoA, and analyzed the roles of SecY in its integration into the membrane. We found that this model protein was less stably integrated into the membrane as a result of inefficient strop transfer reaction in the secY125 mutant strain than in the wild type strain. On the other hand, the stop transfer reaction occurred with the enhanced efficiency in the prIA(secY) 4-1 mutant strain. These results strongly suggest that SecY is directly involved in the stop transfer process in biogenesis of membrane proteins.
(2nd year) We suggested previously that FtsH is involved in the stop transfer process. We found that, 1) FtsH has affinity to a denatured alkaline phosphatase, 2) the binding of FtsH to a denatured alkaline phosphatase is independent of ATP, 3) FtsH is unable to degrade bound alkaline phosphatase. This denatured protein binding activity of FtsH may have some role in the biogenesis of membrane proteins, especially the stop transfer process.
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