Molecular mechanism of force generation by dynein, a molecular motor belonging to the AAA+ family.
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.
Numata
Naoki
N
Department of Life Sciences, University of Tokyo, Komaba 3-8-1, Meguro, Tokyo 153-8902, Japan. numata@bio.c.u-tokyo.ac.jp
Kon
Takahide
T
Shima
Tomohiro
T
Imamula
Kenji
K
Mogami
Toshifumi
T
Ohkura
Reiko
R
Sutoh
Keiko
K
Sutoh
Kazuo
K
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D001696:Biomechanical Phenomena; D004398:Dyneins / Q000737:chemistry / Q000378:metabolism*; D008666:Metalloendopeptidases / Q000737:chemistry / Q000378:metabolism*; D008870:Microtubules / Q000378:metabolism; D017434:Protein Structure, Tertiary
D000255:Adenosine Triphosphate; D008666:Metalloendopeptidases; C114583:m-AAA proteases; D004398:Dyneins