Study on the motile mechanisms for processive myosins with short legs using high-speed atomic force microscopy
| Project/Area Number |
24770149
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Biophysics
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| Research Institution | Kanazawa University |
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Principal Investigator |
KODERA Noriyuki 金沢大学, バイオAFM先端研究センター, 准教授 (30584635)
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| Project Period (FY) |
2012-04-01 – 2015-03-31
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| Project Status |
Completed (Fiscal Year 2014)
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| Budget Amount *help |
¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000)
Fiscal Year 2014: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2013: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2012: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
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| Keywords | ミオシン / アクチン / モータータンパク質 / 一分子計測・走査 / 原子間力顕微鏡 / 一分子計測・操作 / 生物物理学 / 1分子計測・操作 |
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| Outline of Final Research Achievements |
Myosin 6 and 10 are two-headed molecular motors that move along actin filaments. Intriguingly, it is known that these motors move with a large stride than that expended from their leg length. However, their functional mechanisms have not been elucidated yet, due to the lack of structural evidence. Here, we applied high-speed atomic force microscopy to directly observe their structural dynamics at high spatiotemporal resolution. Net wiggly processive movements with large and small strides performed by these myosins were directly visualized. The large stride was made by a lever-arm extension in their tail domain. The direct evidence obtained here should lead to better understanding the functional mechanism of these myosins.
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Report
(4 results)
Research Products
(76 results)
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[Journal Article] Multiple Interactions of the Intrinsically Disordered Region between the N-terminal Helicase and C-terminal Nuclease Domains2014
Author(s)
S. Ishino, T. Yamagami, M. Kitamura, N. Kodera, T. Mori, S. Sugiyama, T. Ando, N. Goda, T. Tenno, H. Hiroaki, and Y. Ishino
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Journal Title
J. Biol. Chem.
Volume: 289
Issue: 31
Pages: 21627-21639
DOI
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Peer Reviewed
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[Journal Article] Nano-scale alignment of proteins on a nexible DNA back-bone2012
Author(s)
Nojima, T.*, Konno, H., Kodera, N., Seio, K, Taguchi, H., Yoshida, M.
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Journal Title
PLoS One
Volume: 7
Issue: 12
Pages: 52534-52534
DOI
Related Report
Peer Reviewed
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[Presentation] Cofilin-induced unidirectional cooperative conformational changes of actin filaments visualized by high speed atomic force microscopy2014
Author(s)
Ngo, KX., Kodera, N., Katayama, E., Nagasaki, A., Ando, T., and Uyeda, TQP.
Organizer
第52回日本生物物理学会年会
Place of Presentation
札幌コンベンションセンター
Year and Date
2014-09-25 – 2014-09-27
Related Report
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[Presentation] An analysis of cooperative binding of myosin to F-actin using high-speed atomic force microscope and fluorescence microscopy2014
Author(s)
Ueno, H., Nishikawa, Y., Ainai, A., Hirakawa, R., Yoshino, A., Kodera, N., Uyeda, TQP., and Tokuraku, K.
Organizer
第52回日本生物物理学会年会
Place of Presentation
札幌コンベンションセンター
Year and Date
2014-09-25 – 2014-09-27
Related Report
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[Presentation] Real-Time Observation of DNA Digestion by RecBCD with High-Speed Atomic Force Microscopy2014
Author(s)
Zhao, W., Handa, N., Moriguchi, Y., Kowalczykowski, S., Kodera, N., and Ando, T.
Organizer
第52回日本生物物理学会年会
Place of Presentation
札幌コンベンションセンター
Year and Date
2014-09-25 – 2014-09-27
Related Report
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[Presentation] ATP-less movement of myosin V2014
Author(s)
Kodera, N., Uchihashi, T., and Ando, T.
Organizer
Gordon Research Conferences, Muscle & Molecular Motors, Resolving the Molecular Mechanisms of Contractile Biology
Place of Presentation
Mount Snow Resort, West Dover, VT, USA
Year and Date
2014-07-06 – 2014-07-16
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[Book] Atomic Force Microscopy in Liquid2012
Author(s)
Ando, T., Uchihashi, T., Kodera, N., Shibata, M., Yamamoto, D., and Yamashita, H.
Total Pages
402
Publisher
Wiley-VCH
Related Report
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