Single-molecule analysis of DNA binding proteins using DNA array(Fostering Joint International Research)
| Project/Area Number |
16KK0157
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| Research Category |
Fund for the Promotion of Joint International Research (Fostering Joint International Research)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Biophysics
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| Research Institution | Tohoku University |
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Principal Investigator |
Kamagata Kiyoto 東北大学, 多元物質科学研究所, 准教授 (90432492)
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| Project Period (FY) |
2017 – 2019
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| Project Status |
Completed (Fiscal Year 2019)
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| Budget Amount *help |
¥15,210,000 (Direct Cost: ¥11,700,000、Indirect Cost: ¥3,510,000)
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| Keywords | DNA / DNA結合タンパク質 / 単分子蛍光顕微鏡 / スライディング / 拡散 / 障害物 / 単分子計測 / １分子計測(SMD) / 蛋白質 / 遺伝子 / 分子認識 / 生体分子 |
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| Outline of Final Research Achievements |
We analyzed the function of DNA-binding proteins using developed DNA aligned array and single-molecule fluorescence microscopy. We found that architectural DNA-binding proteins slide along DNA with continuous contacts to DNA. We identified the key residues to affect the sliding dynamics using mutation analysis. Although we expected that DNA-binding proteins bound to DNA block the movement by proteins along DNA, we found that an architectural DNA-binding protein can bypass other DNA-binding proteins along DNA.
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| Academic Significance and Societal Importance of the Research Achievements |
DNA結合タンパク質は、DNAの標的配列に結合し細胞の機能を制御することが知られている。本研究では、単分子顕微鏡を用いて、実際にDNA結合タンパク質がDNA上の動きを可視化することで、分子レベルでのメカニズムを解明した。また、DNA結合タンパク質の標的DNA配列への結合が阻害されると、様々な疾患になることも知られている。将来的に、本研究で明らかとなったDNA結合タンパク質の機能メカニズムを用いて、DNA結合タンパク質の関わる創薬研究が期待される。
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Report
(2 results)
Research Products
(23 results)
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[Journal Article] The mechanosensitive channel YbdG from Escherichia coli has a role in adaptation to osmotic up-shock.2019
Author(s)
Shun Amemiya, Hayato Toyoda, Mami Kimura, Hiromi Saito, Hiroshi Kobayashi, Kunio Ihara 3 , Kiyoto Kamagata 4 , Ryuji Kawabata 5 , Setsu Kato, Yutaka Nakashimada, Tadaomi Furuta, Shin Hamamoto, Nobuyuki Uozumi
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Journal Title
Journal of Biological Chemistry
Volume: 294 (33)
Issue: 33
Pages: 12281-12292
DOI
Related Report
Peer Reviewed
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