Supramolecular regulation of the actin-activated ATPase activity of filaments of Acanthamoeba Myosin II.

J. Kuznicki, J. P. Albanesi, G. P. Côté, E. D. Korn

Research output: Contribution to journalArticle

34 Scopus citations

Abstract

Acanthamoeba myosin II has three phosphorylation sites clustered near the end of the tail of each of its two heavy chains (six phosphorylation sites/molecule). Myosin II has little or no actin-activated ATPase activity when four to six of these sites are phosphorylated. Maximal actin-activated ATPase activity is obtained when all six sites are dephosphorylated. Under assay conditions, both phosphorylated and dephosphorylated myosin II form bipolar filaments. Filaments of dephosphorylated myosin II have larger sedimentation coefficients than filaments of phosphorylated myosin II but this difference does not explain the difference in their actin-activated ATPase activities. Heteropolymers, formed by mixing soluble dephosphorylated and phosphorylated myosins and then diluting the mixture into low ionic strength buffer containing MgCl2, have sedimentation coefficients close to those of the homopolymer of phosphorylated myosin. The actin-activated ATPase activities of heteropolymers are, under most conditions, lower than the equivalent mixtures of homopolymers of dephosphorylated and phosphorylated myosins. It is concluded, therefore, that the phosphorylation of myosin tails regulates the actin-activated ATPase activity of Acanthamoeba myosin II by affecting the myosin filament as a whole rather than specifically affecting the heads of the phosphorylated myosin molecules only.

Original languageEnglish (US)
Pages (from-to)6011-6014
Number of pages4
JournalJournal of Biological Chemistry
Volume258
Issue number10
StatePublished - May 25 1983

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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