A one-headed class V myosin molecule develops multiple large (approximately 32-nm) steps successively
Graduate School of Biomedical Sciences; Department of Physiology
Medical Subject Headings
Actins; Adenosine Triphosphate; Animals; Binding Sites; Chickens; Microfilaments; Models, Biological; *Movement; Myosin Type V; Protein Engineering; Protein Structure, Tertiary; Protein Transport; Rabbits; Xenopus laevis
Life Sciences | Medicine and Health Sciences
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.
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Citation: Proc Natl Acad Sci U S A. 2004 Jun 29;101(26):9630-5. Epub 2004 Jun 18. Link to article on publisher's site
Proceedings of the National Academy of Sciences of the United States of America
Watanabe, Tomonobu M.; Tanaka, Hiroto; Iwane, Atsuko Hikikoshi; Maki-Yonekura, Saori; Homma, Kazuaki; Inoue, Akira; Ikebe, Reiko; Yanagida, Toshio; and Ikebe, Mitsuo, "A one-headed class V myosin molecule develops multiple large (approximately 32-nm) steps successively" (2004). GSBS Student Publications. 1329.