Graduate School of Frontier Biosciences, Osaka University

Japanese

A one-headed class V myosin molecule develops multiple large (approximately 32-nm) steps successively.

Journal Proc Natl Acad Sci USA 101, 9630-5 (2004)
Authors Watanabe TM, Tanaka H, Iwane AH, Maki-Yonekura S, Homma K, Inoue A, Ikebe R, Yanagida T, Ikebe M.
Title A one-headed class V myosin molecule develops multiple large (approximately 32-nm) steps successively.
PubMed 15208405
Laboratory
Abstract Class V myosin (myosin-V) was first found as a processive motor that moves along an actin filament with large ( approximately 36-nm) successive steps and plays an important role in cargo transport in cells. Subsequently, several other myosins have also been found to move processively. Because myosin-V has two heads with ATP- and actin-binding sites, the mechanism of successive movement has been generally explained based on the two-headed structure. However, the fundamental problem of whether the two-headed structure is essential for the successive movement has not been solved. Here, we measure motility of engineered myosin-V having only one head by optical trapping nanometry. The results show that a single one-headed myosin-V undergoes multiple successive large (approximately 32-nm) steps, suggesting that a novel mechanism is operating for successive myosin movement.