GSBS Student Publications

Title

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

UMMS Affiliation

Graduate School of Biomedical Sciences; Department of Physiology

Date

6-23-2004

Document Type

Article

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

Disciplines

Life Sciences | Medicine and Health Sciences

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.

Rights and Permissions

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

DOI of Published Version

10.1073/pnas.0402914101

Related Resources

Link to Article in PubMed

Journal Title

Proceedings of the National Academy of Sciences of the United States of America

PubMed ID

15208405