| 研究課題/領域番号 |
17H03647
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| 研究機関 | 大阪大学 |
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研究代表者 |
Gerle Christoph 大阪大学, 蛋白質研究所, 特任准教授(常勤) (10561970)
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| 研究分担者 |
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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| 研究期間 (年度) |
2017-04-01 – 2020-03-31
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| キーワード | mitochondria / F-ATP synthase / cryo-EM / membrane protein / super complex / cristae / membrane architecture / membrane transport |
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| 研究実績の概要 |
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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| 現在までの達成度 (区分) |
現在までの達成度 (区分)
3: やや遅れている
理由
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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| 今後の研究の推進方策 |
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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