Myosin binding to actin. Structural analysis using myosin fragments

Loriana Castellani, Bruce W. Elliott, Donald A. Winkelmann, Peter Vibert, Carolyn Cohen

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The actin-binding property of the myosin head 20 K (K = 103 Mr) fragment has been examined by a structural assay. A new fragment is produced by digestion of scallop myosin synthetic filaments with a lysine-specific protease. This fragment consists of the rod together with two "nubs" corresponding to the 20 K fragment, which retain both the regulatory and essential light chains. Myosin filaments, digested for different lengths of time, were mixed with F-actin and visualized by electron microscopy after negative staining. When the head is cleaved, but the head fragments remain associated, the filaments bind actin in an ATP-sensitive manner. Filaments made primarily of the nub-containing fragments, however, bind actin very poorly. In addition, electron microscopic characterization of actin-binding by the isolated tryptic 20 K fragment from chicken myosin indicates that binding of this fragment to actin is probably non-specific. These results suggest that interactions between the 20 K region and the other peptides in the head are essential for actin-binding.

Original languageEnglish (US)
Pages (from-to)955-960
Number of pages6
JournalJournal of molecular biology
Issue number4
StatePublished - Aug 20 1987
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Molecular Biology


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