Abstract
Actomyosin, a complex of actin filaments and myosin motor proteins, is responsible for force generation during muscle contraction. To resolve the individual mechanical events of force generation by actomyosin, we have developed a new instrument with which we can capture and directly manipulate individual myosin subfragment-1 molecules using a scanning probe. Single subfragment-1 molecules can be visualized by using a fluorescent label. The data that we obtain using this technique are consistent with myosin moving along an actin filament with single mechanical steps of approximately 5.3 nanometres; groups of two to five rapid steps in succession often produce displacements of 11 to 30 nanometres. This multiple stepping is produced by a single myosin head during just one biochemical cycle of ATP hydrolysis.
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Acknowledgements
We thank T. Funatsu, K. Saito, H. Higuchi, A. Ishijima and H. Kojima for technical suggestions; Y. Ishii and other colleagues of the ERATO project and Osaka University for valuable discussions; A. F. Huxley, Y. E. Goldman, F. Brozovich, C. R. Bagshaw, J. E. Molloy, A. D. Mehta, R. D. Vale and J. West for critically reading the manuscript; S. Kimura for instructions on preparing α-actinin; M. Taniguchi for advice on statistical analysis; and M. Kitano, H. Kado and H. Ogawa for the gift of the ZnO whiskers. This work was partially supported by JSPS Research Fellowships for Young Scientists (K.K.).
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Kitamura, K., Tokunaga, M., Iwane, A. et al. A single myosin head moves along an actin filament with regular steps of 5.3 nanometres. Nature 397, 129–134 (1999). https://doi.org/10.1038/16403
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DOI: https://doi.org/10.1038/16403
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