The neck domain of myosin II primarily regulates the actomyosin kinetics, not the stepsize

Atsuko Hikikoshi Iwane, Hiroto Tanaka, Sayuri Morimoto, Akihiko Ishijima, Toshio Yanagida

研究成果: Article査読

5 被引用数 (Scopus)

抄録

In order to study the role of the neck domain of myosin in muscle contraction, we measured the steps of individual myosin II molecules engineered to have no neck domain (light chain-binding domain) by optical trapping nanometry. The actin filament and myosin cofilaments interacted on a glass surface to minimize the angle between them, and to minimize the interaction between myosin and the glass surface. The results showed that the average myosin stepsize did not change much when the neck domain was removed, but the sliding velocity decreased ∼fivefold. Furthermore, the duration of steps for neckless myosin was several times longer at saturated ATP concentration, indicating that the slower velocity was due to a slower dissociation rate of myosin heads from actin. From these data, we conclude that the neck domain of myosin-II primarily regulates the actomyosin kinetics, not the mechanics.

本文言語English
ページ(範囲)213-221
ページ数9
ジャーナルJournal of Molecular Biology
353
2
DOI
出版ステータスPublished - 2005 10月 21
外部発表はい

ASJC Scopus subject areas

  • 構造生物学
  • 分子生物学

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