A functional recombinant myosin II lacking a regulatory light chain-binding site

Taro Q.P. Uyeda, James A. Spudich*

*この研究の対応する著者

研究成果: Article査読

103 被引用数 (Scopus)

抄録

Myosin II, which converts the energy of adenosine triphosphate hydrolysis into the movement of actin filaments, is a hexamer of two heavy chains, two essential light chains, and two regulatory light chains (RLCs). Dictyostelium myosin II is known to be regulated in vitro by phosphorylation of the RLC. Cells in which the wild-type myosin II heavy chain was replaced with a recombinant form that lacks the binding site for RLC carried out cytokinesis and almost normal development, processes known to be dependent on functional myosin II. Characterization of the purified recombinant protein suggests that a complex of RLC and the RLC binding site of the heavy chain plays an inhibitory role for adenosine triphosphatase activity and a structural role for the movement of myosin along actin.

本文言語English
ページ(範囲)1867-1870
ページ数4
ジャーナルScience
262
5141
DOI
出版ステータスPublished - 1993
外部発表はい

ASJC Scopus subject areas

  • 一般

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