A Dictyostelium myosin II lacking a proximal 58-kDa portion of the tail is functional in vitro and in vivo

E. W. Kubalek, T. Q.P. Uyeda, J. A. Spudich

研究成果: Article査読

34 被引用数 (Scopus)

抄録

We used molecular genetic approaches to delete 521 amino acid residues from the proximal portion of the Dictyostelium myosin II tail. The deletion encompasses ~40% of the tail, including the S2-LMM junction, a region that in muscle myosin II has been proposed to be important for contraction. The functions of the mutant myosin II are indistinguishable from the wild-type myosin II in our in vitro assays. It binds to actin in a typical rigor configuration in the absence of ATP and it forms filaments in a normal salt- dependent manner. In an in vitro motility assay, both monomeric and filamentous forms of the mutant myosin II translocate actin filaments at 2.4 μm/s at 30°C, similar to that of wild-type myosin II. The mutant myosin II is also functional in vivo. Cells expressing the mutant myosin II in place of the native myosin II perform myosin II-dependent activities such as cytokinesis and formation of fruiting bodies, albeit inefficiently. Growth of the mutant cells in suspension gives rise to many large multinucleated cells, demonstrating that cytokinesis often fails. The majority of the fruiting bodies are also morphologically abnormal. These results demonstrate that this region of the myosin II tail is not required for motile activities but its presence is necessary for optimum function in vivo.

本文言語English
ページ(範囲)1455-1462
ページ数8
ジャーナルMolecular biology of the cell
3
12
DOI
出版ステータスPublished - 1992
外部発表はい

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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