TAILIEUCHUNG - Báo cáo khoa học: Molecular organization and force-generating mechanism of dynein

Dynein, which is a minus-end-directed microtubule motor, is crucial to a range of cellular processes. The mass of its motor domain is about 10 times that of kinesin, the other microtubule motor. Its large size and the diffi-culty of expressing and purifying mutants have hampered progress in dynein research. | IFEBS Journal MINIREVIEW Molecular organization and force-generating mechanism of dynein Hitoshi Sakakibara1 and Kazuhiro Oiwa1 2 1 National institute of Information and Communications Technology Kobe Japan 2 Graduate Schoolof Life Science University of Hyogo Japan Keywords dynein intracellular transport microtubules molecular motor processivity retrograde transport single-molecule nanometry Correspondence K. Oiwa National institute of Information and Communications Technology Advanced ICT Research Center 588-2 Iwaoka Nishi-ku Kobe 6512492 Japan Fax 81 78 969 2119 Tel 81 78 969 2110 E-mail oiwa@ Dynein which is a minus-end-directed microtubule motor is crucial to a range of cellular processes. The mass of its motor domain is about 10 times that of kinesin the other microtubule motor. Its large size and the difficulty of expressing and purifying mutants have hampered progress in dynein research. Recently however electron microscopy X-ray crystallography and single-molecule nanometry have shed light on several key unsolved questions concerning how the dynein molecule is organized what conformational changes in the molecule accompany ATP hydrolysis and whether two or three motor domains are coordinated in the movements of dynein. This minireview describes our current knowledge of the molecular organization and the force-generating mechanism of dynein with emphasis on findings from electron microscopy and single-molecule nanometry. Received 8 February 2011 revised 20 May 2011 accepted 1 July 2011 doi Introduction A high molecular weight ATPase extracted from Tetra-hymena cilia was the first microtubule-based force-generating ATPase to be discovered 1 . It was named dynein after the cgs unit of force the dyne 2 . Dynein is now known to consist of a functionally diverse family of proteins the members of which are involved in a wide variety of essential cellular functions in various cells. There are two major functional classes .

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