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A programmable DNA origami nanospring that reveals force-induced adjacent binding of myosin VI heads
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...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5159853/ https://www.ncbi.nlm.nih.gov/pubmed/27941751 http://dx.doi.org/10.1038/ncomms13715 |
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author | Iwaki, M. Wickham, S. F. Ikezaki, K. Yanagida, T. Shih, W. M. |
author_facet | Iwaki, M. Wickham, S. F. Ikezaki, K. Yanagida, T. Shih, W. M. |
author_sort | Iwaki, M. |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-5159853 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-51598532016-12-20 A programmable DNA origami nanospring that reveals force-induced adjacent binding of myosin VI heads Iwaki, M. Wickham, S. F. Ikezaki, K. Yanagida, T. Shih, W. M. Nat Commun Article 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. Nature Publishing Group 2016-12-12 /pmc/articles/PMC5159853/ /pubmed/27941751 http://dx.doi.org/10.1038/ncomms13715 Text en Copyright © 2016, The Author(s) http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Article Iwaki, M. Wickham, S. F. Ikezaki, K. Yanagida, T. Shih, W. M. A programmable DNA origami nanospring that reveals force-induced adjacent binding of myosin VI heads |
title | A programmable DNA origami nanospring that reveals force-induced adjacent binding of myosin VI heads |
title_full | A programmable DNA origami nanospring that reveals force-induced adjacent binding of myosin VI heads |
title_fullStr | A programmable DNA origami nanospring that reveals force-induced adjacent binding of myosin VI heads |
title_full_unstemmed | A programmable DNA origami nanospring that reveals force-induced adjacent binding of myosin VI heads |
title_short | A programmable DNA origami nanospring that reveals force-induced adjacent binding of myosin VI heads |
title_sort | programmable dna origami nanospring that reveals force-induced adjacent binding of myosin vi heads |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5159853/ https://www.ncbi.nlm.nih.gov/pubmed/27941751 http://dx.doi.org/10.1038/ncomms13715 |
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