Structural analysis of the axonemal dynein responsible for ciliary/flagellar beating
Project/Area Number |
26291014
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Research Category |
Grant-in-Aid for Scientific Research (B)
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Allocation Type | Partial Multi-year Fund |
Section | 一般 |
Research Field |
Structural biochemistry
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Research Institution | Osaka University |
Principal Investigator |
Kurisu Genji 大阪大学, たんぱく質研究所, 教授 (90294131)
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Project Period (FY) |
2014-04-01 – 2018-03-31
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Project Status |
Completed (Fiscal Year 2017)
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Budget Amount *help |
¥16,640,000 (Direct Cost: ¥12,800,000、Indirect Cost: ¥3,840,000)
Fiscal Year 2016: ¥5,200,000 (Direct Cost: ¥4,000,000、Indirect Cost: ¥1,200,000)
Fiscal Year 2015: ¥5,200,000 (Direct Cost: ¥4,000,000、Indirect Cost: ¥1,200,000)
Fiscal Year 2014: ¥6,240,000 (Direct Cost: ¥4,800,000、Indirect Cost: ¥1,440,000)
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Keywords | 生体運動 / 構造生物学 / 分子モーター / 構造解析 / 生物物理 / 蛋白質 / 生体分子 / X線結晶解析 |
Outline of Final Research Achievements |
Dynein motors are biologically important bio-nanomachines, and many atomic resolution structures of cytoplasmic dynein components from different organisms have been analyzed by X-ray crystallography, cryo-EM and NMR spectroscopy. However, atomic data are very much focused on cytoplasmic dyneins and remarkably less structural work on axonemal dyneins has been reported. This project provided structural studies of axonemal dynein including accessory proteins. My team performed mutational and structural studies of the interaction between the axonemal dynein light chain-1 (LC1) and the microtubule-binding domain (MTBD) of outer arm dynein gamma (OADγ), and tried to overexpress the axonemal dynein motor domain and crystallize the axonemal dynein stalk region. Based on the results mentioned above, we can discuss about the structural basis for the LC1-MTBD complex formation that might regulate the function of axonemal dynein heavy chain in different way from that of cytoplasmic dynein.
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Report
(5 results)
Research Products
(26 results)
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[Journal Article] Bacterial β-Glucosidase Reveals the Structural and Functional Basis of Genetic Defects in Human Glucocerebrosidase 2 (GBA2)2016
Author(s)
Charoenwattanasatien, R., Pengthaisong, S., Breen, I., Mutoh, R., Sansenya, S., Hua, Y., Tankrathok, A., Wu, L., Songsiriritthigul, C., Tanaka, H., Williams, S.J., Davies, G.J., Kurisu, G., Cairns, J.R.
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Journal Title
ACS Chem Biol.
Volume: 11
Issue: 7
Pages: 1891-1900
DOI
Related Report
Peer Reviewed / Open Access / Int'l Joint Research
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[Journal Article] A structural view of synthetic cofactor integration into [FeFe]-hydrogenases2016
Author(s)
Esselborn, J., Muraki, N., Klein, K., Engelbrecht, V., Metzler-Nolte, N., Apfel, U.P., Hofmann, E., Kurisu, G., Happe, T.
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Journal Title
Chemical Science
Volume: 7
Issue: 2
Pages: 959-968
DOI
Related Report
Peer Reviewed / Int'l Joint Research
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[Presentation] Structural insights into complex formation of the axonemal dynein light chain-1 and OADγ stalk2018
Author(s)
Toda, A., Tanaka, H., Nishikawa, Y., Yagi, T., Kurisu, G.
Organizer
62th Annual Meeting Biophysic Society, CA,USA
Related Report
Int'l Joint Research
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[Presentation] Structural insights into complex formation of the axonemal dynein light chain-1 and OADγ stalk2017
Author(s)
Toda, A., Tanaka, H., Nishikawa, Y., Yagi, T., Kurisu, G.
Organizer
International Workshop Dynein 2017, 淡路島市
Related Report
Int'l Joint Research
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