The core of the motor domain determines the direction of myosin movement

Kazuaki Homma, Misako Yoshimura, Junya Saito, Reiko Ikebe and Mitsuo Ikebe
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Kazuaki Homma: University of Massachusetts Medical School
Misako Yoshimura: University of Massachusetts Medical School
Junya Saito: University of Massachusetts Medical School
Reiko Ikebe: University of Massachusetts Medical School
Mitsuo Ikebe: University of Massachusetts Medical School

Nature, 2001, vol. 412, issue 6849, 831-834

Abstract: Abstract Myosins constitute a superfamily of at least 18 known classes of molecular motors that move along actin filaments1,2,3. 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 direction4. 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 motility4. 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.

Date: 2001
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DOI: 10.1038/35090597

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