The core of the motor domain determines the direction of myosin movement
Biochemistry & Molecular Pharmacology
Medical Subject Headings
Animals; Calmodulin; Cell Line; Mice; Molecular Motor Proteins; Movement; Myosins; Protein Structure, Tertiary; Rabbits; Recombinant Fusion Proteins; Structure-Activity Relationship; Xenopus
Life Sciences | Medicine and Health Sciences
Myosins constitute a superfamily of at least 18 known classes of molecular motors that move along actin filaments. Myosins move towards the plus end of F-actin filaments; however, it was shown recently that a certain class of myosin, class VI myosin, moves towards the opposite end of F-actin, that is, in the minus direction. As there is a large, unique insertion in the myosin VI head domain between the motor domain and the light-chain-binding domain (the lever arm), it was thought that this insertion alters the angle of the lever-arm switch movement, thereby changing the direction of motility. Here we determine the direction of motility of chimaeric myosins that comprise the motor domain and the lever-arm domain (containing an insert) from myosins that have movement in the opposite direction. The results show that the motor core domain, but neither the large insert nor the converter domain, determines the direction of myosin motility.
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Citation: Nature. 2001 Aug 23;412(6849):831-4. Link to article on publisher's site
Homma, Kazuaki; Yoshimura, Misako; Saito, Junya; Ikebe, Reiko; and Ikebe, Mitsuo, "The core of the motor domain determines the direction of myosin movement" (2001). GSBS Student Publications. 537.