Development of variable-temperature high-speed AFM and its application to temperature-dependent ATPases
Project/Area Number |
15H03540
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Research Category |
Grant-in-Aid for Scientific Research (B)
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Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Nanobioscience
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Research Institution | Nagoya University (2017) Kanazawa University (2015-2016) |
Principal Investigator |
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Co-Investigator(Renkei-kenkyūsha) |
IMADA KATSUMI 大阪大学, 理学研究科, 教授 (40346143)
YOKOYAMA KEN 京都産業大学, 総合生命科学部, 教授 (70271377)
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Project Period (FY) |
2015-04-01 – 2018-03-31
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Project Status |
Completed (Fiscal Year 2017)
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Budget Amount *help |
¥16,770,000 (Direct Cost: ¥12,900,000、Indirect Cost: ¥3,870,000)
Fiscal Year 2017: ¥3,900,000 (Direct Cost: ¥3,000,000、Indirect Cost: ¥900,000)
Fiscal Year 2016: ¥5,850,000 (Direct Cost: ¥4,500,000、Indirect Cost: ¥1,350,000)
Fiscal Year 2015: ¥7,020,000 (Direct Cost: ¥5,400,000、Indirect Cost: ¥1,620,000)
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Keywords | 高速原子間力顕微鏡 / タンパク質 / 一分子計測 / ATP加水分解酵素 / 時計タンパク質 / 温度制御 / 1分子計測(SMD / 走査プローブ顕微鏡 / ナノバイオ / 蛋白質 / 一分子イメージング・ナノ計測 / 走査型プローブ顕微鏡 / 1分子イメージング・ナノ計測 |
Outline of Final Research Achievements |
We have developed variable-temperature high-speed atomic force microscopy (VT-HS-AFM) with which the experimental temperature can be controlled ranging from a room temperature to around 40 ℃. The performance of VT-HS-AFM was confirmed by observation of fluidity of DPPC lipid bilayer with the phase-transition temperature of 41℃ from gel phase to liquid crystal phase. We applied the VT-HS-AFM system to observation of a flagellar protein, FliI, which is an ATPase with the activity optimum temperature over 40℃. HS-AFM images captured oligomerization processes of the FliI monomers to the hexamer and also conformational changes of the oligomers. Also we observed temperature dependent interaction between KaiC and KaiA which are proteins responsible to the circadian rhythm of Cyanobacteria.
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Report
(4 results)
Research Products
(76 results)
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[Journal Article] Rate constants, processivity, and productive binding ratio of chitinase A revealed by single- molecule analysis2018
Author(s)
Akihiko Nakamura, Tomoyuki Tasaki, Yasuko Okuni, Chihong Song, Kazuyoshi Murata, Toshiya Kozai, Mayu Hara, Hayuki Sugimoto, Kazushi Suzuki, Takeshi Watanabe, Takayuki Uchihashi, Hiroyuki Noji and Ryota Iino
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Journal Title
Phys. Chem. Chem. Phys.
Volume: 20
Issue: 5
Pages: 3010-3018
DOI
Related Report
Peer Reviewed / Open Access
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[Journal Article] Conversion of functionally undefined homopentameric protein PbaA into a proteasome activator by mutational modification of its C-terminal segment conformation2018
Author(s)
M. Yagi-Utsumi, A. Sikdar, T. Kozai, R. Inoue, M. Sugiyama, T. Uchihashi, H. Yagi, T. Satoh, and K. Kato
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Journal Title
Protein Engineering, Design, and Selection
Volume: 31
Issue: 1
Pages: 29-36
DOI
Related Report
Peer Reviewed / Open Access
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[Journal Article] Dynamic clustering of dynamin-amphiphysin helices regulates membrane constriction and fission coupled with GTP hydrolysis2018
Author(s)
Tetsuya Takeda, Toshiya Kozai, Huiran Yang, Daiki Ishikuro, Kaho Seyama, Yusuke Kumagai, Tadashi Abe, Hiroshi Yamada, Takayuki Uchihashi, Toshio Ando, Kohji Takei
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Journal Title
eLife
Volume: 7
Pages: 1-19
DOI
NAID
Related Report
Peer Reviewed / Open Access
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[Journal Article] A natural light-driven inward proton pump2016
Author(s)
Keiichi Inoue, Shota Ito, Yoshitaka Kato, Yurika Nomura, Mikihiro Shibata, Takayuki Uchihashi, Satoshi P. Tsunoda and Hideki Kandori
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Journal Title
Nature Communications
Volume: 7
Issue: 1
Pages: 13415-13415
DOI
Related Report
Peer Reviewed / Open Access
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[Presentation] Dynamic remodeling of Dynamin complexes during membrane fission2017
Author(s)
Tetsuya Takeda, Daiki Ishikuro, Huiran Yang, Toshiya Kozai, Kaho Seyama, Yusuke Kumagai, Hiroshi Yamada, Takayuki Uchihashi, Toshio Ando, Kohji Takei
Organizer
日本生物物理学会第55回年会, シンポジウム "Biophysics of molecular assembly and biological membrane"
Related Report
Int'l Joint Research / Invited
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