Single particle cryoEM of mammalian FoF1 ATP synthase

2019 Fiscal Year Final Research Report

• Project/Area Number: 17H03647
• Research Category: Grant-in-Aid for Scientific Research (B)
• Allocation Type: Single-year Grants
• Section: 一般
• Research Field: Structural biochemistry
• Research Institution: Osaka University
• Principal Investigator: Gerle Christoph 大阪大学, 蛋白質研究所, 特任准教授(常勤) (10561970)
• 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)
• Project Period (FY): 2017-04-01 – 2020-03-31
• Keywords: mitochondria / F-ATP synthase / cryo-EM / membrane protein / super complex / cristae / membrane architecture / membrane transport

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.

Free Research Field

生物化学

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。