Abstract
Muscle contraction is caused by relative sliding movement between interdigitating actin and myosin filaments. It has been thought that myosin heads protruding from the myosin filament rotate between two orientations, while they repeat detachment from and attachment to actin filament coupled to the ATP hydrolysis cycle and the rotation of the head may cause the sliding. Recently atomic structure obtained from X-ray crystallography supports the rotation of the myosin head relative to the actin filament. A small conformational change in the ATP binding domain is transmitted to a neck domain that connects a motor domain (head) and tail domain, depending on the chemical state of nucleotide bound. Thus the neck domain acts as a lever-arm that can cause a displacement of 5–10 nm for the muscle myosin. This lever-arm swinging model has been a paradigm not only for the muscle myosin but also for unconventional myosins. Large stepsize of unconventional processive myosin V motor can be explained by its large lever arm within the frame of the lever-arm swinging model.
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30.5. References
Galkin, V. E., VanLoock, M. S., Orlova, A., and Egelman, E. H., 2002. A new internal mode in F-actin helps explain the remarkable evolutionary conservation of actin’s sequence and structure. Curr. Biol. 12(7):570–575.
Harada, Y., Sakurada, Y., Aoki, T., Thomas, D. D., and Yanagida, T., 1990. Mechanochemmical coupling in actomyosin energy transduction studied by in vitro movement assay. J. Mol. Biol. 216:49–68.
Higuchi, H., and Goldman, Y. E., 1991, Sliding distance between actin and myosin filaments per ATP hydrolyzed in skinned muscle fibers. Nature 35:352–354.
Holmes, K. C., Angert, I., Kull, F. J., Jahn, W., and Schroder, R. R., 2003. Electron cryo-microscopy shoes how strong binding of myosin to actin releases nucleotide. Nature 425(6956):423–427.
Ishii, Y., Yoshida, T., Funatsu, T., Wazawa, T., and Yanagida, T., 1999. Fluorescence resonance energy transfer between single fluorophores attached to a coiled-coil protein in aqueous solution. Chem. Phys. 247:163–173.
Kitamura, K., Tokunaga, M., Esaki, S., Iwane, A. H., and Yanagida, T., 2005. Mechanism of mucle contraction based on stochastic properties of single actomyosin motors observed in vitro. Biophysics 1:1–19.
Kitamura, K., Tokunaga, M., Iwane, A. H., and Yanagida, T., 1999. Single myosin head moves alon an actin filament with regular steps of 5.3 nanometers. Nature 397:129.
Kozuka, J., Yokota, H., Arai, Y., Ishii, Y., and Yanagida, T., 2006. Dynamic polymorphism of single actin molecules in the actin filament. Nat. Chem. Biol. 2(2):83–86.
Otterbein, L. R., Graceffa, P., and Dominguez, R., 2001. The crystal structure of uncomplexed actin in the ADP state. Science 293(5530):708–711.
Prochniewicz, E., and Yanagida, T., 1990. Inhibition of sliding movement of F-actin by crosslinking emphasizes the role of actin structure in the mechanism of motility. J. Mol. Biol. 216(3):761–772.
Wakabayashi, K., Ueno, Y., Takezawa, Y., and Sugimoto, Y., 2001. Muscle contraction mechanism: Use of X-ray synchrotron radiation. Nature Encyclopedia of life science pp. 1–11.
Yanagida, T., Arata, T., and Oosawa, F., 1985. Sliding distance induced by a myosin crossbridge during one ATP hydrolysis cycle. Nature 316:366–369.
Yanagida, T., Esaki, S., Iwane, A. H., Inoue, Y., Ishijima, A., Kitamura, K., Tanaka, H., and Tokunaga, M., 2000. Single-motor mechanics and models of myosin motor. Phil. Trans. R. Soc. Lond. B 255:441–447.
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Yanagida, T. (2007). Muscle Contraction Mechanism Based on Actin Filament Rotation. In: Ebashi, S., Ohtsuki, I. (eds) Regulatory Mechanisms of Striated Muscle Contraction. Advances in Experimental Medicine and Biology, vol 592. Springer, Tokyo. https://doi.org/10.1007/978-4-431-38453-3_30
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DOI: https://doi.org/10.1007/978-4-431-38453-3_30
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