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Molecular engineering of a backwards-moving myosin motor

Author

Listed:
  • Georgios Tsiavaliaris

    (Institut für Biophysikalische Chemie, Medizinische Hochschule Hannover
    Abteilung Biophysik, Max-Planck-Institut für Medizinische Forschung)

  • Setsuko Fujita-Becker

    (Abteilung Biophysik, Max-Planck-Institut für Medizinische Forschung)

  • Dietmar J. Manstein

    (Institut für Biophysikalische Chemie, Medizinische Hochschule Hannover
    Abteilung Biophysik, Max-Planck-Institut für Medizinische Forschung)

Abstract

All members of the diverse myosin superfamily have a highly conserved globular motor domain that contains the actin- and nucleotide-binding sites and produces force and movement1,2. The light-chain-binding domain connects the motor domain to a variety of functionally specialized tail domains and amplifies small structural changes in the motor domain through rotation of a lever arm3,4. Myosins move on polarized actin filaments either forwards to the barbed (+ ) or backwards to the pointed (- ) end5,6. Here, we describe the engineering of an artificial backwards-moving myosin from three pre-existing molecular building blocks. These blocks are: a forward-moving class I myosin motor domain, a directional inverter formed by a four-helix bundle segment of human guanylate-binding protein-1 and an artificial lever arm formed by two α-actinin repeats. Our results prove that reverse-direction movement of myosins can be achieved simply by rotating the direction of the lever arm 180°.

Suggested Citation

  • Georgios Tsiavaliaris & Setsuko Fujita-Becker & Dietmar J. Manstein, 2004. "Molecular engineering of a backwards-moving myosin motor," Nature, Nature, vol. 427(6974), pages 558-561, February.
    • Handle: RePEc:nat:nature:v:427:y:2004:i:6974:d:10.1038_nature02303
    DOI: 10.1038/nature02303
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