2014 Fiscal Year Final Research Report
A novel regulation mechanism of cellular functions by intramembrane proteolysis
| Project/Area Number |
24370054
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Partial Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Functional biochemistry
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| Research Institution | Kyoto University |
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Principal Investigator |
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| Co-Investigator(Kenkyū-buntansha) |
MORI Hiroyuki 京都大学, ウイルス研究所, 准教授 (10243271)
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| Project Period (FY) |
2012-04-01 – 2015-03-31
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| Keywords | 大腸菌 / 膜プロテアーゼ / 膜内タンパク質切断 / 表層ストレス応答 / S2Pプロテアーゼ |
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| Outline of Final Research Achievements |
The Escherichia coli σE extracytoplasmic stress response monitors and responds to folding stress in the cell envelope. A protease cascade directed at RseA, a membrane-spanning anti-σ that inhibits σE activity, controls this critical signal-transduction system. Stress cues activate DegS to cleave RseA; a second cleavage by RseP releases RseA from the membrane, enabling its rapid degradation.
We also analyzed the three-dimensional structure of the two tandemly arranged PDZ domains (PDZ tandem) present in the periplasmic region of RseP. Our results suggest that the PDZ tandem serves as a size-exclusion filter to accommodate the truncated form of RseA into the active center.
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| Free Research Field |
分子生物学
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