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

Tomonobu M. Watanabe, Hiroto Tanaka, Atsuko Hikikoshi Iwane, Saori Maki-Yonekura, Kazuaki Homma, Akira Inoue, Reiko Ikebe, Toshio Yanagida*, Mitsuo Ikebe

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

29 Scopus citations


Class V myosin (myosin-V) was first found as a processive motor that moves along an actin filament with large (≈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 (≈32-nm) steps, suggesting that a novel mechanism is operating for successive myosin movement.

Original languageEnglish (US)
Pages (from-to)9630-9635
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number26
StatePublished - Jun 29 2004

ASJC Scopus subject areas

  • General


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