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-Structure paper
タイトル | Structure and function of outer dynein arm intermediate and light chain complex. |
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ジャーナル・号・ページ | Mol Biol Cell, Vol. 27, Issue 7, Page 1051-1059, Year 2016 |
掲載日 | 2016年4月1日 |
著者 | Toshiyuki Oda / Tatsuki Abe / Haruaki Yanagisawa / Masahide Kikkawa / |
PubMed 要旨 | The outer dynein arm (ODA) is a molecular complex that drives the beating motion of cilia/flagella. Chlamydomonas ODA is composed of three heavy chains (HCs), two ICs, and 11 light chains (LCs). ...The outer dynein arm (ODA) is a molecular complex that drives the beating motion of cilia/flagella. Chlamydomonas ODA is composed of three heavy chains (HCs), two ICs, and 11 light chains (LCs). Although the three-dimensional (3D) structure of the whole ODA complex has been investigated, the 3D configurations of the ICs and LCs are largely unknown. Here we identified the 3D positions of the two ICs and three LCs using cryo-electron tomography and structural labeling. We found that these ICs and LCs were all localized at the root of the outer-inner dynein (OID) linker, designated the ODA-Beak complex. Of interest, the coiled-coil domain of IC2 extended from the ODA-Beak to the outer surface of ODA. Furthermore, we investigated the molecular mechanisms of how the OID linker transmits signals to the ODA-Beak, by manipulating the interaction within the OID linker using a chemically induced dimerization system. We showed that the cross-linking of the OID linker strongly suppresses flagellar motility in vivo. These results suggest that the ICs and LCs of the ODA form the ODA-Beak, which may be involved in mechanosignaling from the OID linker to the HCs. |
リンク | Mol Biol Cell / PubMed:26864626 / PubMed Central |
手法 | EM (サブトモグラム平均) |
解像度 | 46.0 - 48.0 Å |
構造データ | EMDB-6515: EMDB-6516: EMDB-6517: EMDB-6518: EMDB-6519: EMDB-6520: EMDB-6521: EMDB-6522: EMDB-6523: EMDB-6524: |
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