An electromechanical model of myosin molecular motors.
There is a long-running debate on the working mechanism of myosin molecular motors, which, by interacting with actin filaments, convert the chemical energy of ATP into a variety of mechanical work. After the development of technologies for observing and manipulating individual working molecules, experimental results negating the widely accepted 'lever-arm hypothesis' have been reported. In this paper, based on the experimental results so far accumulated, an alternative hypothesis is proposed, in which motor molecules are modelled as electromechanical components that interact with each other through electrostatic force. Electrostatic attractive force between myosin and actin is assumed to cause a conformational change in the myosin head during the attachment process. An elastic energy resulting from the conformational change then produces the power stroke. The energy released at the ATP hydrolysis is mainly used to detach the myosin head from actin filaments. The mechanism presented in this paper is compatible with the experimental results contradictory to the previous theories. It also explains the behavior of myosins V and VI, which are engaged in cellular transport and move processively along actin filaments.
Masuda
Tadashi
T
School of Biomedical Science, Tokyo Medical and Dental University, Kanda Surugadai 2-3-10, Chiyoda-ku, 101-0062 Tokyo, Japan. masuda.bsm@mri.tmd.ac.jp
D008841:Actin Cytoskeleton / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D004734:Energy Metabolism; D008954:Models, Biological; D020409:Molecular Motor Proteins; D009218:Myosins / Q000378:metabolism*; D011487:Protein Conformation; D055672:Static Electricity
D020409:Molecular Motor Proteins; D000255:Adenosine Triphosphate; D009218:Myosins