Force-generating domain of myosin motor

Shinji Itakura, Hisashi Yamakawa, Yoko Yano Toyoshima, Akihiko Ishijima, Takaaki Kojima, Yoshie Harada, Toshio Yanagida, Takeyuki Wakabayashi, Kazuo Sutoh

研究成果: Article査読

107 被引用数 (Scopus)

抄録

To understand the underlying mechanism of force generation by myosin motor, it is crucial to know which part of the molecule is essential for the process. Recent structure determination of myosin motor domain at atomic resolution has revealed that the domain comprises two smaller domains, the "ATPase domain" consisting of only an N-terminal segment of the heavy chain and the "neck domain" consisting of a long α-helix of the heavy chain and two light chains. This atomic structure begs the question of whether both domains are required for force generation. To answer it, we genetically truncated the head to generate a recombinant fragment composed of the "ATPase domain" alone. The truncated head drove sliding movement of actin filaments and generated force in a novel in vitro assay system, which allows us to hold a specific site of the head on a glass surface. These results indicate that the compact ATPase domain functions as a force-generating machinery of the myosin motor.

本文言語English
ページ(範囲)1504-1510
ページ数7
ジャーナルBiochemical and biophysical research communications
196
3
DOI
出版ステータスPublished - 1993 11 15
外部発表はい

ASJC Scopus subject areas

  • 生物理学
  • 生化学
  • 分子生物学
  • 細胞生物学

フィンガープリント

「Force-generating domain of myosin motor」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。

引用スタイル