Control of extracytoplasmic stress responses by regulated intramembrane proteolysis
| Project/Area Number |
15370084
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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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 University, Institute for Virus Research, Associate Professor, ウイルス研究所, 助教授 (10192460)
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| Project Period (FY) |
2003 – 2004
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| Project Status |
Completed (Fiscal Year 2004)
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| Budget Amount *help |
¥12,700,000 (Direct Cost: ¥12,700,000)
Fiscal Year 2004: ¥4,800,000 (Direct Cost: ¥4,800,000)
Fiscal Year 2003: ¥7,900,000 (Direct Cost: ¥7,900,000)
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| Keywords | protease / membrane proteins / regulated intramembrane proteolysis / 表層ストレス応答 / 大腸菌 / タンパク質分解 / ストレス応答 / 膜プロテアーゼ |
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| Research Abstract |
E.coli σ^E is activated by extracytoplasmic stress-induced two step cleavages of the anti-σ^E protein, RseA (a type II single-spanning membrane protein). We showed that RseP (formerly YaeL), an E.coli homolog of the eukaryotic S2P protease, functions as a "RIP(regulated intramembrane proteolysis)" protease that introduces the second "intramembrane" cleavage into anti-σ^E protein (RseA) following the first cleavage on the periplasmic side by DegS. Our in vivo and in vitro results demonstrated that RseP directly catalyzes proteolysis within the transmembrane sequence of RseA. We also found that RseP can cleave transmembrane sequences of some model membrane proteins that are unrelated to RseA, provided that the transmembrane region contains residues of low helical propensity. We are now addressing the molecular mechanisms of the two-step proteolysis of RseA and its regulation using in vitro reaction system reconstituted from purified components.
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Report
(3 results)
Research Products
(8 results)
