2018 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 | mitochondria / F-ATP synthase / cryo-EM / membrane protein / super complex / cristae / membrane architecture / membrane transport |
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| Outline of Annual Research Achievements |
In this project it is the aim to deepen our understanding of energy transformation at the inner mitochondrial membrane with a special emphasis on the structure determination of the mammalian F-ATP synthase. Mitochondrial energy transformation has proven to be central to human health and much more dynamic than previously imagined. Together with our colleagues in Italy at the University of Padova and in England at Oxford University we were able to further significantly our understanding of cristae re-modelling and the influence of lipids on the structure-function relationship of mitochondrial membrane complexes. Our during this project developed expertise in isolation and handling of mitochondrial complexes was crucial to these advances.
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| Current Status of Research Progress |
Current Status of Research Progress
3: Progress in research has been slightly delayed.
Reason
Though a lot of progress has been achieved and we can already use our isolation procdures for F-ATP synthase from the inner mitochondrial membrane for important studies (Quintana-Cabrera et al., Nature communications, 2018; Chorev et al., Science, 2018) the establishment of a column free, "perfect" purification method is still challenging. Nevertheless, I am confident that the pace of progress is sufficient to achieve our goals soon.
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| Strategy for Future Research Activity |
The firm basis for our project is the establishment of a column free isolation procedure for mammalian F-ATP synthase that preserves not only all its subunits, but also its full functionallity as will have to be proven by a 100% coupled proton pumping capability and 100% oligomycin sensitivity. At the same time the complex has to be isolated in a pure oligomeric state, that is either monomer, dimer or tetramer, and in the absence of contamination. Of course this is a very ambitious aim, however, after 60 years of research it is very clear that without such a purification procedure a full understanding of mammalian F-ATP synthase will stay elusive.
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Research Products
(8 results)
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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
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
Peer Reviewed / Int'l Joint Research
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