Three-dimensional image analysis of the complex of thin filaments and myosin molecules from skeletal muscle. III. The multi-domain structure of actin-heavy meromyosin complex

J Biochem. 1981 Sep;90(3):703-14. doi: 10.1093/oxfordjournals.jbchem.a133524.

Abstract

Heavy meromyosin (HMM) prepared by chymotryptic digestion retains DTNB light chain and subfragment-2 (S2) in addition to the two subfragment-1 (S1) moieties. The electron micrograph of negatively stained rigor complex of HMM and actin showed some different features as compared with that of S1 and actin. The three-dimensional image reconstructed from the electron micrograph of actin-HMM gave additional domains other than those observed in actin-S1 (Wakabayashi and Toyoshima, 1981). The differences between the images of actin-HMM and actin-S1 were attributed to the differences in protein composition. Further, the structural characteristics of actin-HMM are discussed in comparison with those of the actin-S1.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins*
  • Animals
  • Cytoskeleton / ultrastructure*
  • Macromolecular Substances
  • Microscopy, Electron
  • Models, Molecular
  • Muscles / ultrastructure*
  • Myosin Subfragments*
  • Peptide Fragments*
  • Rabbits

Substances

  • Actins
  • Macromolecular Substances
  • Myosin Subfragments
  • Peptide Fragments
  • actin subfragments