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

研究成果: Article

3 引用 (Scopus)

抜粋

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.

元の言語English
ページ(範囲)1726-1730
ページ数5
ジャーナルJournal of the Korean Physical Society
53
発行部数3
DOI
出版物ステータスPublished - 2008 9

ASJC Scopus subject areas

  • Physics and Astronomy(all)

フィンガープリント How the load and the nucleotide state affect the actin filament binding mode of the molecular motor myosin V' の研究トピックを掘り下げます。これらはともに一意のフィンガープリントを構成します。

  • これを引用