Structural basis of regulation of striated muscle using electron cryo-microscopy
| Project/Area Number |
15K07032
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Biophysics
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| Research Institution | Teikyo University |
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Principal Investigator |
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| Research Collaborator |
GOMIBUCHI Yuki 帝京大学, 理工学部, 研究員
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| Project Period (FY) |
2015-04-01 – 2018-03-31
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| Project Status |
Completed (Fiscal Year 2017)
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| Budget Amount *help |
¥4,550,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥1,050,000)
Fiscal Year 2017: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2016: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2015: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
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| Keywords | アクチン / トロポニン / トロポミオシン / カルシウム / 筋収縮制御 / クライオ電子顕微鏡 / 筋肉収縮制御 / 収縮制御 / 重合機構 / 三次元再構成 / カルシウム制御 / 筋肉収縮 / 家族性ヒト心筋症 |
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| Outline of Final Research Achievements |
The contraction of striated muscle is regulated by calcium concentration. The target of the calcium is troponin. The binding of calcium ions to troponin triggers the shifting of tropomyosin on the actin filaments and enables the muscle contraction. At low calcium ions concentration, a part of troponin named the mobile domain attaches firmly to the carboxyl-terminal region of actin molecule. To elucidate the structural basis of regulatory mechanism, the several thousand of cryo-electron micrographs of the ternary complex of troponin, tropomyosin, and actin were collected. A small portion of micrographs were analyzed by picking about 10,000 segments of the filaments. Two-dimensionally averaged images reached about 5 angstrom resolution. In the preliminary three-dimensional structure, the regions correspond to the regulatory proteins, i. e., troponin and/or tropomyosin, could be observed. The image analysis of total micrographs is in progress.
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Report
(4 results)
Research Products
(2 results)
