Axonemal dynein light chain-1 locates at the microtubule-binding domain of the γ heavy chain
-
- Muneyoshi Ichikawa
- Department of Life Sciences, Graduate School of Arts and Sciences, University of Tokyo, Tokyo 153-8902, Japan
-
- Kei Saito
- Department of Life Sciences, Graduate School of Arts and Sciences, University of Tokyo, Tokyo 153-8902, Japan
-
- Haru-aki Yanagisawa
- Department of Biological Sciences, Graduate School of Science, University of Tokyo, Tokyo 113-0033, Japan
-
- Toshiki Yagi
- Department of Biological Sciences, Graduate School of Science, University of Tokyo, Tokyo 113-0033, Japan
-
- Ritsu Kamiya
- Department of Biological Sciences, Graduate School of Science, University of Tokyo, Tokyo 113-0033, Japan
-
- Shin Yamaguchi
- Department of Life Sciences, Graduate School of Arts and Sciences, University of Tokyo, Tokyo 153-8902, Japan
-
- Junichiro Yajima
- Department of Life Sciences, Graduate School of Arts and Sciences, University of Tokyo, Tokyo 153-8902, Japan
-
- Yasuharu Kushida
- Graduate School of Life and Environmental Sciences, University of Tsukuba, Ibaraki 305-8572, Japan
-
- Kentaro Nakano
- Graduate School of Life and Environmental Sciences, University of Tsukuba, Ibaraki 305-8572, Japan
-
- Osamu Numata
- Graduate School of Life and Environmental Sciences, University of Tsukuba, Ibaraki 305-8572, Japan
-
- Yoko Y. Toyoshima
- Department of Life Sciences, Graduate School of Arts and Sciences, University of Tokyo, Tokyo 153-8902, Japan
-
- Samara Reck-Peterson
- editor
説明
<jats:p>The outer arm dynein (OAD) complex is the main propulsive force generator for ciliary/flagellar beating. In Chlamydomonas and Tetrahymena, the OAD complex comprises three heavy chains (α, β, and γ HCs) and >10 smaller subunits. Dynein light chain-1 (LC1) is an essential component of OAD. It is known to associate with the Chlamydomonas γ head domain, but its precise localization within the γ head and regulatory mechanism of the OAD complex remain unclear. Here Ni-NTA-nanogold labeling electron microscopy localized LC1 to the stalk tip of the γ head. Single-particle analysis detected an additional structure, most likely corresponding to LC1, near the microtubule-binding domain (MTBD), located at the stalk tip. Pull-down assays confirmed that LC1 bound specifically to the γ MTBD region. Together with observations that LC1 decreased the affinity of the γ MTBD for microtubules, we present a new model in which LC1 regulates OAD activity by modulating γ MTBD's affinity for the doublet microtubule.</jats:p>
収録刊行物
-
- Molecular Biology of the Cell
-
Molecular Biology of the Cell 26 (23), 4236-4247, 2015-11-15
American Society for Cell Biology (ASCB)
- Tweet
詳細情報 詳細情報について
-
- CRID
- 1360567184450105344
-
- ISSN
- 19394586
- 10591524
-
- データソース種別
-
- Crossref
- KAKEN