A possible mechanism for determining the directionality of myosin molecular motors.
There is a large superfamily of myosins, which play various fundamental roles in cellular motility. In this superfamily, most of myosins, including myosins II and V, move to the barbed end of an actin filament, whereas myosin VI was found to move in the opposite direction to the pointed end. Although myosin VI has structural differences compared with the other myosins, the mechanism for the reversal of the directionality has not been satisfactorily explained by conventional theories for myosin motility, including the widely accepted lever-arm hypothesis. In this paper, a simple mechanism for determining the directionality is proposed. The mechanism assumes that the driving force for the power stroke is caused by elastic energy stored within a myosin molecule at the joint between the head and the neck. The elastic energy originates from the attractive force between myosin and actin, and accumulates during the docking process. The energy of ATP is used to reduce the attractive force between myosin and actin and to facilitate the dissociation of these molecules. Therefore, it is not directly engaged in the power stroke. With this mechanism, the directionality of the myosin motility is simply determined by the direction of the neck with respect to the head in the dissociated configuration. This structural difference is actually observed in myosin VI. The same mechanism also explains the behavior of a backward moving engineered myosin. Computer simulations demonstrated the feasibility of this working mechanism.
Masuda
Tadashi
T
Laboratory of Biosystem Modeling, School of Biomedical Science, Tokyo Medical and Dental University, 1-5-45 Yushima, Bunkyo-ku, Tokyo 103 8510, Japan. masuda.bsm@tmd.ac.jp
D008954:Models, Biological; D009218:Myosins / Q000737:chemistry* / Q000378:metabolism*
D009218:Myosins