Abstract
Myosin V is a two-headed, actin-based molecular motor implicated in organelle transport. Previously, a single myosin V molecule has been shown to move processively along an actin filament in discrete ∼36 nm steps. However, 36nm is the helical repeat length of actin, and the geometry of the previous experiments may have forced the heads to bind to, or halt at, sites on one side of actin that are separated by 36 nm. To observe unconstrained motion, we suspended an actin filament in solution and attached a single myosin V molecule carrying a bead duplex. The duplex moved as a left-handed spiral around the filament, disregarding the right-handed actin helix. Our results indicate a stepwise walking mechanism in which myosin V positions and orients the unbound head such that the head will land at the 11th or 13th actin subunit on the opposing strand of the actin double helix.
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Acknowledgements
We thank R. Yasuda, H. Noji, T. Nishizaka, Y. Harada and T. Nishinaka for discussion; L.B. Roksana, K. Kawashima, K. Yogo, R. Shimo, J. Yamaguchi and H. Kubota for sample preparation; M. Shio for microscope setup and H. Umezawa for laboratory management. M.Y.A. was a research fellow of the Japan Society for the Promotion of Science. This work was supported in part by Grants-in-Aid from the Ministry of Education, Culture, Sports, Science, and Technology of Japan.
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Ali, M., Uemura, S., Adachi, K. et al. Myosin V is a left-handed spiral motor on the right-handed actin helix. Nat Struct Mol Biol 9, 464–467 (2002). https://doi.org/10.1038/nsb803
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DOI: https://doi.org/10.1038/nsb803
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