2019 Fiscal Year Annual Research Report
Single particle cryoEM of mammalian FoF1 ATP synthase
| Project/Area Number |
17H03647
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| Research Institution | Osaka University |
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Principal Investigator |
Gerle Christoph 大阪大学, 蛋白質研究所, 特任准教授(常勤) (10561970)
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| Co-Investigator(Kenkyū-buntansha) |
森本 幸生 京都大学, 複合原子力科学研究所, 教授 (80200450)
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| Project Period (FY) |
2017-04-01 – 2020-03-31
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| Keywords | F-ATP synthase / membrane protein / supercomplex / cryo-EM / protein structure / PTP / mitochondria / channel |
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| Outline of Annual Research Achievements |
In this project it was attempted to obtain atomic models of the mammalian F-ATP synthase. A fragile membrane supercomplex which has eluded high level structural description for now almost 60 years. This year we successfully applied our self-developed novel methods for the purification and in vitro membrane reconstitution for the comprehensive testing of the proposal that mitochondrial F-ATP synthase is the molecular identity of the mitochondrial permeability transition pore. Our confirmation of this surprising new channel function on the basis of the best functional data ever published on mammalian F-ATP synthase is less of surprise when considering that conventional purification methods for this fragile complex loose several subunits.
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| Research Progress Status |
令和元年度が最終年度であるため、記入しない。
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| Strategy for Future Research Activity |
令和元年度が最終年度であるため、記入しない。
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Research Products
(7 results)
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[Journal Article] The Dual Life of Mitochondrial F-ATP Synthase.2020
Author(s)
Paolo, B., Szabo, I., Lippe, G., Gerle, C., and Forte, M.A.
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Journal Title
Biophysical Journal
Volume: 118, 3
Pages: 16a-16a
DOI
Open Access / Int'l Joint Research
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[Journal Article] Purified F-ATP synthase forms a Ca2+-dependent high-conductance channel matching the mitochondrial permeability transition pore.2019
Author(s)
Urbani A, Giorgio V, Carrer A, Franchin C, Arrigoni G, Jiko C, Abe K, Maeda S, Shinzawa-Itoh K, Bogers JF, McMillan DG, Gerle, C.*, Szabo, I.*, Bernardi, P.*
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Journal Title
Nature communications
Volume: 10(1)
Pages: 1-11
DOI
Peer Reviewed / Open Access / Int'l Joint Research
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