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XB-ART-3390
Proc Natl Acad Sci U S A 2004 Jun 29;10126:9630-5. doi: 10.1073/pnas.0402914101.
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A one-headed class V myosin molecule develops multiple large (approximately 32-nm) steps successively.

Watanabe TM , Tanaka H , Iwane AH , Maki-Yonekura S , Homma K , Inoue A , Ikebe R , Yanagida T , Ikebe M .


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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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Species referenced: Xenopus laevis
Genes referenced: actl6a

References [+] :
Ali, Unconstrained steps of myosin VI appear longest among known molecular motors. 2004, Pubmed