How the load and the nucleotide state affect the actin filament binding mode of the molecular motor myosin V

Sergey V. Mikhailenko, Yusuke Oguchi, Takashi Ohki, Togo Shimozawa, Adrian O. Olivares, Enrique M. De La Cruz, Shin'ichi Ishiwata

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

The interaction between actin and myosin V has been probed by measuring the unbinding force of individual actomyosin complexes using optical tweezers. Surprisingly, we found that in both the nucleotide-free and ADP-bound states single- and double-headed binding occurs with approximately the same probability. Estimation of the spring constant of individual actomyosin complexes confirmed that in each of the nucleotide states two distinct populations exist. These results confirm that optical nanometry can be used to reliably study the mechanism of how cytoskeleton molecular motors interact with their associated polymer lattices under solution conditions more closely resembling the intracellular environment.

Original languageEnglish
Pages (from-to)1726-1730
Number of pages5
JournalJournal of the Korean Physical Society
Volume53
Issue number3
DOIs
Publication statusPublished - 2008 Sep

Keywords

  • Binding mode
  • Molecular motors
  • Myosin V
  • Processivity
  • Single-molecule

ASJC Scopus subject areas

  • Physics and Astronomy(all)

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