Physiological functions and selective substrate-cleavage mechanism of E. coli intramembrane protease RseP
| Project/Area Number |
18H02404
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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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| Review Section |
Basic Section 43030:Functional biochemistry-related
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| Research Institution | Kyoto University |
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Principal Investigator |
Akiyama Yoshinori 京都大学, ウイルス・再生医科学研究所, 教授 (10192460)
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| Co-Investigator(Kenkyū-buntansha) |
檜作 洋平 京都大学, ウイルス・再生医科学研究所, 助教 (70568930)
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| Project Period (FY) |
2018-04-01 – 2021-03-31
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| Project Status |
Completed (Fiscal Year 2020)
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| Budget Amount *help |
¥17,420,000 (Direct Cost: ¥13,400,000、Indirect Cost: ¥4,020,000)
Fiscal Year 2020: ¥5,330,000 (Direct Cost: ¥4,100,000、Indirect Cost: ¥1,230,000)
Fiscal Year 2019: ¥5,330,000 (Direct Cost: ¥4,100,000、Indirect Cost: ¥1,230,000)
Fiscal Year 2018: ¥6,760,000 (Direct Cost: ¥5,200,000、Indirect Cost: ¥1,560,000)
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| Keywords | 膜内切断プロテアーゼ / 大腸菌 / 切断基質 / 膜内部でのタンパク質切断 / S2Pプロテアーゼ / Fecオペロン / 鉄取り込み / 蛍光ペプチド / 速度論的解析 / 小分子膜タンパク質 / RseP / Toxin-antitoxin / HokB / Persister / small membrane protein / FRET / 生体膜 / プロテアーゼ / 膜内切断 / 蛍光基質 |
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| Outline of Final Research Achievements |
Intramembrane cleaving proteases (I-CLiPs) are known to act in a variety of important cellular processes in diverse organisms. RseP, an Escherichia coli S2P family intramembrane cleaving protease, is involved in the regulation of the sigma E pathway extracytoplasmic stress response and membrane quality control through specific cleavage of substrates within the lipid bilayer. We have identified novel substrates of RseP and analyzed the physiological significance of their RseP-dependent cleavage. Also, we tried to construct an in vitro assay system that enables quantitative analysis of the RseP activity. These results would contribute to the elucidation of the cellular roles of and the mechanism underlying proteolysis by RseP.
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| Academic Significance and Societal Importance of the Research Achievements |
本研究は、申請者ら独自の発見・研究成果を直接踏まえ展開するもので、BepA機能解明を通じて、大腸菌等グラム陰性細菌の外膜形成・維持機構のみならず、protease制御機構に新たな知見を供し、基礎から応用まで広くインパクトを与えるだろう。本研究は、新奇発見に基づくアプローチによる独創性と、独自の成果を統合・発展させる着実性の、両面を兼ね備えたものである。
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Report
(4 results)
Research Products
(24 results)
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[Journal Article] Moving toward generalizable NZ-1 labeling for 3D structure determination with optimized epitope tag insertion.2021
Author(s)
Tamura-Sakaguchi, R., Aruga, R., Hirose, M., Ekimoto, T., Miyake, T., Hizukuri, Y., Oi, R., Kaneko, M. M., Kato, Y., Akiyama, Y., Ikeguchi, M., Iwasaki, K., and Nogi, T.
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Journal Title
Acta Crystallogr. D
Volume: -
NAID
Related Report
Peer Reviewed
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[Journal Article] Escherichia coli S2P family intramembrane protease RseP is engaged in the regulated sequential cleavages of FecR in the ferric citrate signaling.2021
Author(s)
Yokoyama, T., Niinae, T., Tsumagari, K., Imami, K., Ishihama, Y., Hizukuri, Y., and Akiyama, Y.
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Journal Title
Related Report
Peer Reviewed / Open Access
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[Journal Article] Identification of an Internal Cavity in the PhoQ Sensor Domain for PhoQ Activity and SafA-mediated Control2018
Author(s)
K. Yoshitani, E. Ishii, K. Taniguchi, H. Sugimoto, Y. Shiro, H. Mori, Y. Akiyama, A. Kato, R. Utsumi, Y. Eguchi
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Journal Title
Bioscience, Biotechnology, and Biochemistry
Volume: 83
Issue: 4
Pages: 684-694
DOI
Related Report
Peer Reviewed / Open Access
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