journal article Open Access Dec 12, 2016

A programmable DNA origami nanospring that reveals force-induced adjacent binding of myosin VI heads

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Abstract
AbstractMechanosensitive biological nanomachines such as motor proteins and ion channels regulate diverse cellular behaviour. Combined optical trapping with single-molecule fluorescence imaging provides a powerful methodology to clearly characterize the mechanoresponse, structural dynamics and stability of such nanomachines. However, this system requires complicated experimental geometry, preparation and optics, and is limited by low data-acquisition efficiency. Here we develop a programmable DNA origami nanospring that overcomes these issues. We apply our nanospring to human myosin VI, a mechanosensory motor protein, and demonstrate nanometre-precision single-molecule fluorescence imaging of the individual motor domains (heads) under force. We observe force-induced transitions of myosin VI heads from non-adjacent to adjacent binding, which correspond to adapted roles for low-load and high-load transport, respectively. Our technique extends single-molecule studies under force and clarifies the effect of force on biological processes.
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Published
Dec 12, 2016
Vol/Issue
7(1)
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Cite This Article
M. Iwaki, S. F. Wickham, K. Ikezaki, et al. (2016). A programmable DNA origami nanospring that reveals force-induced adjacent binding of myosin VI heads. Nature Communications, 7(1). https://doi.org/10.1038/ncomms13715
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