Abstract
IT is well established that muscle contraction results from the relative sliding of actin and myosin filaments. Both filaments have definite polarities and well-ordered structures. Thick filaments, however, are not vital for supporting movement in vitro1–4. Pre-viously we have demonstrated that actin filaments can move con-tinuously on myosin fragments (subfragment-1 or heavy meromyosin (HMM)) that are bound to a nitrocellulose surface3. Here we report that actin filaments can move in opposite directions on tracks of myosin heads formed when actin filaments decorated with HMM are placed on a nitrocellulose surface. The actin filaments always move forward, frequently changing the direction of the movement, but never move backward reversing the polarity of the movement. The direction of movement is therefore deter-mined by the polarity of the actin filament. These results indicate that myosin heads have considerable flexibility.
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Yano Toyoshima, Y., Toyoshima, C. & Spudich, J. Bidirectional movement of actin filaments along tracks of myosin heads. Nature 341, 154–156 (1989). https://doi.org/10.1038/341154a0
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DOI: https://doi.org/10.1038/341154a0
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