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Molecular engineering of a backwards-moving myosin motor

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Tsiavaliaris,  Georgios
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Fujita-Becker,  Setsuko
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Manstein,  Dietmar J.
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Tsiavaliaris, G., Fujita-Becker, S., & Manstein, D. J. (2004). Molecular engineering of a backwards-moving myosin motor. Nature, 427(6974), 558-561. doi:10.1038/nature02303.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002A-5E04-F
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 movement. 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 arm. Myosins move on polarized actin filaments either forwards to the barbed (+) or backwards to the pointed (-) end. 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 alpha-actinin repeats. Our results prove that reverse-direction movement of myosins can be achieved simply by rotating the direction of the lever arm 180 degrees.