Abstract
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.
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Abbreviations
- actin-TM:
-
actin-tropomyosin filament
- F-actin:
-
filamentary actin
- RhPh-F-actin:
-
filamentary actin stained with phalloidin-tetramethylrhodamine
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Original Russian Text © G. V. Kopylova, D. V. Shchepkin, L. V. Nikitina, 2013, published in Biokhimiya, 2013, Vol. 78, No. 3, pp. 348–356.
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Kopylova, G.V., Shchepkin, D.V. & Nikitina, L.V. Study of regulatory effect of tropomyosin on actin-myosin interaction in skeletal muscle by in vitro motility assay. Biochemistry Moscow 78, 260–266 (2013). https://doi.org/10.1134/S0006297913030073
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DOI: https://doi.org/10.1134/S0006297913030073