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

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

Abstract

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.

Keywords

Myosin Head Cyanogen Bromide Myosin Molecule Heavy Meromyosin Cyclic Interaction 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  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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