若林 憲一 所属 京都産業大学 生命科学部 産業生命科学科 職種 教授 |
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言語種別 | 英語 |
発行・発表の年月 | 2014/07 |
形態種別 | 研究論文 |
査読 | 査読あり |
標題 | Cooperative binding of the outer arm-docking complex underlies the regular arrangement of outer arm dynein in the axoneme |
執筆形態 | その他 |
掲載誌名 | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA |
出版社・発行元 | NATL ACAD SCIENCES |
巻・号・頁 | 111(26),pp.9461-9466 |
担当区分 | 責任著者 |
著者・共著者 | Mikito Owa,Akane Furuta,Jiro Usukura,Fumio Arisaka,Stephen M. King,George B. Witman,Ritsu Kamiya,Ken-ichi Wakabayashi |
概要 | Outer arm dynein (OAD) in cilia and flagella is bound to the outer doublet microtubules every 24 nm. Periodic binding of OADs at specific sites is important for efficient cilia/flagella beating; however, the molecular mechanism that specifies OAD arrangement remains elusive. Studies using the green alga Chlamydomonas reinhardtii have shown that the OAD-docking complex (ODA-DC), a heterotrimeric complex present at the OAD base, functions as the OAD docking site on the doublet. We find that the ODA-DC has an ellipsoidal shape similar to 24 nm in length. In mutant axonemes that lack OAD but retain the ODA-DC, ODA-DC molecules are aligned in an end-to-end manner along the outer doublets. When flagella of a mutant lacking ODA-DCs are supplied with ODA-DCs upon gamete fusion, ODA-DC molecules first bind to the mutant axonemes in the proximal region, and the occupied region gradually extends toward the tip, followed by binding of OADs. This and other results indicate that a cooperative association of the ODA-DC underlies its function as the OAD-docking site and is the determinant of the 24-nm periodicity. |
DOI | 10.1073/pnas.1403101111 |
ISSN | 0027-8424 |
PMID | 24979786 |