A programmable DNA origami nanospring that reveals force-induced adjacent binding of myosin VI heads
M. Iwaki (),
S. F. Wickham,
K. Ikezaki,
T. Yanagida and
W. M. Shih
Additional contact information
M. Iwaki: Quantitative Biology Center, RIKEN
S. F. Wickham: Dana-Farber Cancer Institute
K. Ikezaki: School of Frontier Sciences, The University of Tokyo
T. Yanagida: Quantitative Biology Center, RIKEN
W. M. Shih: Dana-Farber Cancer Institute
Nature Communications, 2016, vol. 7, issue 1, 1-10
Abstract:
Abstract Mechanosensitive 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.
Date: 2016
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms13715
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DOI: 10.1038/ncomms13715
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