2017 Fiscal Year Final Research Report
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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Keywords | 生体運動 / 構造生物学 / 分子モーター |
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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Free Research Field |
構造生物化学
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