Interaction Between Two Myosin Heads in Acto-Smooth Muscle Heavy Meromyosin Rigor Complex

  • Hirofumi Onishi
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 332)


Muscle contraction occurs as a result of the cyclic interaction between actin and myosin, coupled with the hydrolysis of ATP by the myosin heads1). A myosin molecule consists of two globular heads and a rod-shaped tail2). It is thought that each myosin head functions as a contractile machinery unit, because each head shows ATPase activity and binds to F-actin. A still unsolved question is whether or not the two heads of a myosin molecule interact with each other during their cyclic interaction with F-actin. Here we report that when chicken gizzard heavy meromyosin (HMM) in its rigor complex with F-actin is reacted with the zero-length cross-linker l-ethyl-3-[3-(dimethylamino)propyl] carbodiimide (EDC), the two heads of the HMM molecule are cross-linked. This result suggests that the two heads of smooth muscle myosin are in contact with each other when myosin is attached to F-actin. It is thus possible that the two myosin heads interact with each other when cross-bridges are formed.


Myosin Head Cyanogen Bromide Myosin Molecule Heavy Meromyosin Cyclic Interaction 
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  1. 1.
    Huxley, H.E. Science 164, 1356–1366 (1969).PubMedCrossRefGoogle Scholar
  2. 2.
    Lowey, S., Slayter, H. S., Weeds, A.G. & Baker, H. J. Mol. Biol. 42, 1–29 (1969).PubMedCrossRefGoogle Scholar
  3. 3.
    Onishi, H., Maita, T., Matsuda, G. & Fujiwara, K. Biochemistry 28, 1898–1904 (1989).PubMedCrossRefGoogle Scholar
  4. 4.
    Onishi, H., Maita, T., Matsuda, G. & Fujiwara, K. Biochemistry 28, 1905–1912 (1989).PubMedCrossRefGoogle Scholar
  5. 5.
    Onishi, H., Maita, T., Matsuda, G. & Fujiwara, K. J. Biol. Chem. 265, 19362–19368 (1990).PubMedGoogle Scholar
  6. 6.
    Onishi, H. & Fujiwara, K. Biochemistry 29, 3013–3023 (1990).PubMedCrossRefGoogle Scholar
  7. 7.
    Walker, J.E., Saraste, M., Runswick, M. J. & Gay, N.J. EMBO J. 1, 945–951 (1982).PubMedGoogle Scholar
  8. 8.
    Tokunaga, M., Sutoh, K., Toyoshima, C. & Wakabayashi, T. Nature 329, 635–638 (1987).PubMedCrossRefGoogle Scholar
  9. 9.
    Botts, J., Thomason, J.F. & Morales, M.F. Proc. Natl Acad. Sci. USA 86, 2204–2208 (1989)PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1993

Authors and Affiliations

  • Hirofumi Onishi
    • 1
  1. 1.Department of Structural AnalysisNational Cardiovascular Center Research InstituteSuita, OsakaJapan

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