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Light-chain movement and regulation in scallop myosin

Nature volume 301, pages 478–482 (1983)Cite this article

Abstract

Photo-cross-linking techniques show that when scallop myosin or myofibrils are subjected to experimental conditions that cause relaxed muscles to go into rigor, the N-terminal portion of the regulatory light chain of myosin moves towards the essential light chain while the C-terminal portion stays in place. These changes occur on the myosin before combination with actin. Cross-linking of the N-terminal region to the essential light chain in rigor locks the myosin into a conformation such that calcium sensitivity of the actin-activated Mg-ATPase is lost.

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Authors and Affiliations

  1. Department of Biology, Brandeis University, Waltham, Massachusetts, 02254, USA

    Peter M. D. Hardwicke & Andrew G. Szent-Györgyi

  2. ETH Eidgenossische Technische Hochschule, Institut für Zellbiologie, Honggerberg, CH-8093, Zürich, Switzerland

    Theo Wallimann

Authors
  1. Peter M. D. Hardwicke
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  2. Theo Wallimann
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  3. Andrew G. Szent-Györgyi
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Hardwicke, P., Wallimann, T. & Szent-Györgyi, A. Light-chain movement and regulation in scallop myosin. Nature 301, 478–482 (1983). https://doi.org/10.1038/301478a0

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  • DOI: https://doi.org/10.1038/301478a0

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