Single particle cryoEM of mammalian FoF1 ATP synthase
| Project/Area Number |
17H03647
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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 |
Structural biochemistry
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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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| Project Status |
Completed (Fiscal Year 2019)
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| Budget Amount *help |
¥17,810,000 (Direct Cost: ¥13,700,000、Indirect Cost: ¥4,110,000)
Fiscal Year 2019: ¥3,120,000 (Direct Cost: ¥2,400,000、Indirect Cost: ¥720,000)
Fiscal Year 2018: ¥4,160,000 (Direct Cost: ¥3,200,000、Indirect Cost: ¥960,000)
Fiscal Year 2017: ¥10,530,000 (Direct Cost: ¥8,100,000、Indirect Cost: ¥2,430,000)
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| Keywords | mitochondria / F-ATP synthase / cryo-EM / membrane protein / super complex / cristae / membrane architecture / membrane transport / supercomplex / protein structure / PTP / channel / 高分解能電子顕微鏡解析 / 膜タンパク質複合体 / クライオ電顕 / FoF1ATP合成酵素 / 膜蛋白質複合体 / FoF1ATP合成 / FoF1 ATP synthase / bioenergetics / single particle cryo-EM / structural biology / membrane biology / proton transport / rotary ATPase / 分子モータ / 蛋白質 / 電子顕微鏡 / 生体分子 |
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| Outline of Final Research Achievements |
All the cells in our body rely on the sufficient and well balanced energy supply in the form of the molecule ATP. Most ATP is produced by a large membrane supercomplex, the F-ATP synthase. How this very large protein complex achieves its energy transformation function is not very well understood yet. In this project we attempted to improve our understanding by inventing novel ways to purify fragile F-ATP synthase from cow heart muscle tissue and analyze its structure and function by cryo electron microscopy and other methods. We succeeded to find new ways to purifiy the protein complex that preserves it during isolation. All physiological functions of the F-ATP synthase could be preserved. We also invented novel ways to put the F-ATP synthase into artificial membranes, which was important to confirm new channel functions of F-ATP synthase. In summary, we have now established a firm basis for structure and function analysis in solution as well as in artificial membrane systems.
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| Academic Significance and Societal Importance of the Research Achievements |
哺乳類のF-ATP合成酵素は、ミトコンドリア疾患の鍵を握る存在として現在注目されている。今回のプロジェクトで得られた新しい調製法、膜の再構成、透過性遷移孔としての機能の発見は、F-ATP合成酵素の研究を前進させる上で重要な役割を果たすことが期待される。
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Report
(4 results)
Research Products
(22 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
DOI
Related Report
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, Sginzawa-Itoh K, Bogers JF, McMillan DG, Gerle C, Szabo I, Bernardi P
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Journal Title
Nat. Commun.
Volume: 4341
Pages: 1-11
DOI
Related Report
Peer Reviewed / Open Access / Int'l Joint Research
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[Journal Article] The cristae modulator Optic atrophy 1 requires mitochondrial ATP synthase oligomers to safeguard mitochondrial function.2018
Author(s)
Ruben Quintana-Cabrera, Charlotte Quirin, Christina Glytsou, Mauro Corrado, Andrea Urbani, Anna Pellattiero, Enrique Calvo, Jesus Vazquez, Jose; Antonio Enriquez, Christoph Gerle, Maria Eugenia Soriano, Paolo Bernardi & Luca Scorrano
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Journal Title
Nature communications
Volume: 9 (3399)
Pages: 1-13
DOI
Related Report
Peer Reviewed / Open Access / Int'l Joint Research
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[Journal Article] Protein assemblies ejected directly from native membranes yield complexes for mass spectrometry2018
Author(s)
Dror S Chorev, Lindsay A Baker, Di Wu, Victoria Beilsten-Edmands, Sarah L Rouse, Tzviya Zeev-Ben-Mordehai, Chimari Jiko, Firdaus Samsudin, Christoph Gerle, Syma Khalid, Alastair G Stewart, Stephen J Matthews, Kay Grunewald, Carol V Robinson
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Journal Title
Science
Volume: 362, 6416
Pages: 829-834
DOI
Related Report
Peer Reviewed / Int'l Joint Research
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