Cooperativity between two heads of Dictyostelium myosin II in in vitro motility and ATP hydrolysis

Kohji Ito, Xiong Liu, Eisaku Katayama, Taro Q.P. Uyeda*

*この研究の対応する著者

研究成果: Article査読

30 被引用数 (Scopus)

抄録

To elucidate the significance of the two-headed structure of myosin II, we have engineered and characterized recombinant single-headed myosin II. A tail segment of a myosin II heavy chain fused with a His-tag was expressed in wild-type Dictyostelium cells. Single-headed myosin, which consists of a full length myosin heavy chain and a tagged tail, was isolated on the basis of the affinities for Nickel agarose and actin. Actin sliding velocity by the single-headed myosin was about half of the two-headed, whereas the minimum density of the heads to support continuous movement was twofold higher. Actin-activated MgATPase activity of the single-headed myosin in solution in the presence of 24 μM actin was less than half of the two headed. This decrease is primarily because of fourfold-elevated Kapp for actin and secondary to 40% lower Vmax. These results suggest that the two heads of a Dictyostelium myosin II molecule act cooperatively on an actin filament. We propose a mechanism by which two heads move actin efficiently based on the cooperativity.

本文言語English
ページ(範囲)985-992
ページ数8
ジャーナルBiophysical Journal
76
2
DOI
出版ステータスPublished - 1999
外部発表はい

ASJC Scopus subject areas

  • 生物理学

フィンガープリント

「Cooperativity between two heads of Dictyostelium myosin II in in vitro motility and ATP hydrolysis」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