Heavy meromyosin induces sliding movements between antiparallel actin filaments.

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  • Author(s): Takiguchi K;Takiguchi K
  • Source:
    Journal of biochemistry [J Biochem] 1991 Apr; Vol. 109 (4), pp. 520-7.
  • Publication Type:
    Journal Article
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: Oxford University Press Country of Publication: England NLM ID: 0376600 Publication Model: Print Cited Medium: Print ISSN: 0021-924X (Print) Linking ISSN: 0021924X NLM ISO Abbreviation: J Biochem Subsets: MEDLINE
    • Publication Information:
      Publication: : Abingdon, UK : Oxford University Press
      Original Publication: Tokyo : Japanese Biochemical Society
    • Subject Terms:
      Actins/*physiology ; Myosin Subfragments/*physiology; Actins/ultrastructure ; Adenosine Triphosphate/metabolism ; Animals ; Microscopy, Electron ; Microscopy, Fluorescence ; Muscles/physiology ; Myosin Subfragments/ultrastructure ; Rabbits
    • Abstract:
      Suzuki et al. [Biochemistry 28, 6513-6518 (1989)] have shown that, when F-actin is mixed with inert high polymer, a large number of actin filaments closely align in parallel with overlaps to form a long and thick bundle. The bundle may be designated non-polar, as the constituent filaments are random in polarity (Suzuki et al. 1989). I prepared non-polar bundles of F-actin using methylcellulose (MC) as the high polymer, exposed them to heavy meromyosin (HMM) in the presence of ATP under a light microscope, and followed their morphological changes in the continuous presence of MC. It was found that bundles several tens of micrometers long contracted to about one-third the initial length, while becoming thicker, in half a minute after exposure to HMM. Subsequently, each bundle was split longitudinally into several bundles in a stepwise manner, while the newly formed ones remained associated together at one of the two ends. The product, an aster-like assembly of actin bundles, was morphologically quiescent; that is, individual bundles never contracted upon second exposure to HMM and ATP, although they were still longer than the F-actin used. Bundles in this state consisted of filaments with parallel polarity as examined by electron microscopy. This implies that non-polar bundles were transformed into assemblies of polar bundles with ATP hydrolysis by HMM. Importantly, myosin subfragment-1 caused neither contraction nor transformation. These results are interpreted as follows. In the presence of ATP, the two-headed HMM molecule was able to cross-bridge antiparallel actin filaments, as well as parallel ones.(ABSTRACT TRUNCATED AT 250 WORDS)
    • Accession Number:
      0 (Actins)
      0 (Myosin Subfragments)
      8L70Q75FXE (Adenosine Triphosphate)
    • Publication Date:
      Date Created: 19910401 Date Completed: 19910917 Latest Revision: 20190510
    • Publication Date:
      20231215
    • Accession Number:
      10.1093/oxfordjournals.jbchem.a123414
    • Accession Number:
      1869506