Molecular mechanism of force generation by dynein, a molecular motor belonging to the AAA+ family
-
- Naoki Numata
- Department of Life Sciences, University of Tokyo, Komaba 3-8-1, Meguro, Tokyo 153-8902, Japan
-
- Takahide Kon
- Department of Life Sciences, University of Tokyo, Komaba 3-8-1, Meguro, Tokyo 153-8902, Japan
-
- Tomohiro Shima
- Department of Life Sciences, University of Tokyo, Komaba 3-8-1, Meguro, Tokyo 153-8902, Japan
-
- Kenji Imamula
- Department of Life Sciences, University of Tokyo, Komaba 3-8-1, Meguro, Tokyo 153-8902, Japan
-
- Toshifumi Mogami
- Department of Life Sciences, University of Tokyo, Komaba 3-8-1, Meguro, Tokyo 153-8902, Japan
-
- Reiko Ohkura
- Department of Life Sciences, University of Tokyo, Komaba 3-8-1, Meguro, Tokyo 153-8902, Japan
-
- Keiko Sutoh
- Department of Life Sciences, University of Tokyo, Komaba 3-8-1, Meguro, Tokyo 153-8902, Japan
-
- Kazuo Sutoh
- Department of Life Sciences, University of Tokyo, Komaba 3-8-1, Meguro, Tokyo 153-8902, Japan
この論文をさがす
説明
<jats:p>Dynein is an AAA+ (ATPase associated with various cellular activities)-type motor complex that utilizes ATP hydrolysis to actively drive microtubule sliding. The dynein heavy chain (molecular mass >500 kDa) contains six tandemly linked AAA+ modules and exhibits full motor activities. Detailed molecular dissection of this motor with unique architecture was hampered by the lack of an expression system for the recombinant heavy chain, as a result of its large size. However, the recent success of recombinant protein expression with full motor activities has provided a method for advances in structure–function studies in order to elucidate the molecular mechanism of force generation.</jats:p>
収録刊行物
-
- Biochemical Society Transactions
-
Biochemical Society Transactions 36 (1), 131-135, 2008-01-22
Portland Press Ltd.
