Biochemistry (Moscow)

, Volume 78, Issue 3, pp 260–266

Study of regulatory effect of tropomyosin on actin-myosin interaction in skeletal muscle by in vitro motility assay

  • G. V. Kopylova
  • D. V. Shchepkin
  • L. V. Nikitina


The interaction between myosin and actin in striated muscle tissue is regulated by Ca2+ via thin filament regulatory proteins. Skeletal muscle possesses a whole pattern of myosin and tropomyosin isoforms. The regulatory effect of tropomyosin on actin-myosin interaction was investigated by measuring the sliding velocity of both actin and actin-tropomyosin filaments over fast and slow skeletal myosins using the in vitro motility assay. The actin-tropomyosin filaments were reconstructed with tropomyosin isoforms from striated muscle tissue. It was found that tropomyosins with different content of α-, β-, and γ-chains added to actin filaments affect the sliding velocity of filaments in different ways. On the other hand, the sliding velocity of filaments with the same content of α-, β-, and Γ-chains depends on myosin isoforms of striated muscle. The reciprocal effects of myosin and tropomyosin on actin-myosin interaction in striated muscle may play a significant role in maintenance of effective work of striated muscle both during ontogenesis and under pathological conditions.

Key words

skeletal myosin isoforms tropomyosin isoforms in vitro motility assay 



actin-tropomyosin filament


filamentary actin


filamentary actin stained with phalloidin-tetramethylrhodamine


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Copyright information

© Pleiades Publishing, Ltd. 2013

Authors and Affiliations

  • G. V. Kopylova
    • 1
  • D. V. Shchepkin
    • 1
  • L. V. Nikitina
    • 1
  1. 1.Institute of Immunology and PhysiologyUral Division of the Russian Academy of SciencesEkaterinburgRussia

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