Involvement of tail domains in regulation of Dictyostelium myosin II

Xiong Liu*, Kohji Ito, Randall J. Lee, Taro Q.P. Uyeda

*この研究の対応する著者

研究成果: Article査読

21 被引用数 (Scopus)

抄録

The actin-dependent ATPase activity of Dictyostelium myosin II filaments is regulated by phosphorylation of the regulatory light chain. Four deletion mutant myosins which lack different parts of subfragment 2 (S2) showed phosphorylation-independent elevations in their activities. Phosphorylation-independent elevation in the activity was also achieved by a double point mutation to replace conserved Glu932 and Glu933 in S2 with Lys. These results suggested that inhibitory interactions involving the head and S2 are required for efficient regulation. Regulation of wild-type myosin was not affected by copolymerization with a S2 deletion mutant myosin in the same filaments. Furthermore, the activity linearly correlated with the fraction of phosphorylated molecules in wild-type filaments. These latter two results suggest that the inhibitory head-tail interactions are primarily intramolecular. (C) 2000 Academic Press.

本文言語English
ページ(範囲)75-81
ページ数7
ジャーナルBiochemical and Biophysical Research Communications
271
1
DOI
出版ステータスPublished - 2000 4月 29
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

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