Nanometer localization of single fluorescent proteins: Evidence that myosin V walks hand-over-hand via telemark configuration

Gregory E. Snyder, Takeshi Sakamoto, John A. Hammer, James R. Sellers, Paul R. Selvin

Research output: Contribution to journalArticle

Abstract

Myosin V is a homodimeric motor protein involved in trafficking of vesicles in the cell. It walks bipedally along actin filaments, moving cargo ∼37 nm per step. We have measured the step size of individual myosin heads by fusing an enhanced green fluorescent protein (eGFP) to the N-terminus of one head of the myosin dimer and following the motion with nanometer precision and subsecond resolution. We find the average step size to be 74.1 nm with 9.4 nm (SD) and 0.3 nm (SE). Our measurements demonstrate nanometer localization of single eGFPs, confirm the hand-over-hand model of myosin V procession, and when combined with previous data, suggest that there is a kink in the leading lever arm in the waiting state of myosin V. This kink, or "telemark skier" configuration, may cause strain, which, when released, leads to the powerstroke of myosin, throwing the rear head forward and leading to unidirectional motion.

Original languageEnglish (US)
Pages (from-to)1776-1783
Number of pages8
JournalBiophysical journal
Volume87
Issue number3
DOIs
StatePublished - Sep 2004

ASJC Scopus subject areas

  • Biophysics

Fingerprint Dive into the research topics of 'Nanometer localization of single fluorescent proteins: Evidence that myosin V walks hand-over-hand via telemark configuration'. Together they form a unique fingerprint.

  • Cite this