Abstract
The myosin molecule consists of two heads, each of which contains an enzymatic active site and an actin-binding site. The fundamental problem of whether the two heads function independently or cooperatively during muscle contraction has been studied by methods using an actomyosin thread1, superprecipitation2–4 and chemical modification of muscle fibres5. No clear conclusion has yet been reached. We have approached this question using an assay system in which sliding movements of fluorescently labelled single actin filaments along myosin filaments can be observed directly6,7. Here, we report direct measurement of the sliding of single actin filaments along one-headed myosin filaments in which the density of heads was varied over a wide range. Our results show that cooperative interaction between the two heads of myosin is not essential for inducing the sliding movement of actin filaments.
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Harada, Y., Noguchi, A., Kishino, A. et al. Sliding movement of single actin filaments on one-headed myosin filaments. Nature 326, 805–808 (1987). https://doi.org/10.1038/326805a0
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DOI: https://doi.org/10.1038/326805a0
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