Development of methods for preparing histones with various modifications
| Project/Area Number |
15K14418
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Multi-year Fund |
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| Research Field |
Genome biology
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| Research Institution | Koshien University (2017-2018)
Osaka University (2015-2016) |
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Principal Investigator |
Suetake Isao 甲子園大学, 栄養学部, 教授 (80304054)
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| Co-Investigator(Kenkyū-buntansha) |
川上 徹 大阪大学, 蛋白質研究所, 准教授 (70273711)
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| Project Period (FY) |
2015-04-01 – 2019-03-31
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| Project Status |
Completed (Fiscal Year 2018)
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| Budget Amount *help |
¥3,900,000 (Direct Cost: ¥3,000,000、Indirect Cost: ¥900,000)
Fiscal Year 2017: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2016: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2015: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
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| Keywords | 修飾ヒストン / ヒストン / ユビキチン化 / 化学修飾 / ヒストン修飾 / 有機化学 |
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| Outline of Final Research Achievements |
Proteins are posttranlationally modified. Post-translational modifications are known to be essential mechanisms to diversify their protein functions and dynamically coordinate their signaling networks. To reveal the molecular mechanisms how the modifications function, we tried to chamically prepare modified proteins. As the molecular weight is small and various modifications are reported, we focused histone, which is nuclear protein. We established a method to prepare histone H3 carrying ubiquitin analogue at specific amino acid. By using the modified histone H3, we found new epigenetic regulation that ubiquitinated histone H3 stimulated maintenance DNA methylation activity, via direct interaction, in vitro.
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| Academic Significance and Societal Importance of the Research Achievements |
これまで修飾タンパク質を用意して、タンパク質修飾の機能を調べるという研究は少なかった。その理由は、修飾タンパク質（特に、低分子蛋白質が修飾として導入される場合）を作成するのが難しいことによる。本研究成果で、目的のアミノ酸にユビキチン化修飾を導入することができる。そのため、その修飾の生理機に迫ることができ、私が報告した以外の新制御系も見出すことが出来ると考えている。さらに、これまで導入が容易である修飾と同時に導入することにより、さらに複雑な制御系を明らかにできうる基盤的技術を準備できたため、今後の修飾研究が大きく進むと期待できる。
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Report
(5 results)
Research Products
(53 results)
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[Journal Article] RFTS-dependent negative regulation of Dnmt1 by nucleosome structure and histone tails.2017
Author(s)
Mishima Y, Brueckner L, Takahashi S, Kawakami T, Arita K, Oka S, Otani J, Hojo H, Shirakawa M, Shinohara A, Watanabe M, Suetake I
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Journal Title
FEBS J.
Volume: 284
Issue: 20
Pages: 3455-3469
DOI
NAID
Related Report
Peer Reviewed / Open Access / Int'l Joint Research
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[Journal Article] Structure of the Dnmt1 reader module complexed with a unique two-mono-ubiquitin mark on histone H3 reveals the basis for DNA methylation maintenance.2017
Author(s)
Ishiyama S, Nishiyama A, Saeki Y, Moritsugu K Morimoto D, Yamaguchi L, Arai N, Matsumura R, Kawakami T, Mishima Y, Hojo H, Shimamura S, Ishikawa F, Tajima S, Tanaka K, Ariyoshi M, Shirakawa M, Ikeguchi M, Kidera A, Suetake I, Arita K, Nakanishi M
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Journal Title
Mol Cell
Volume: 68
Issue: 2
Pages: 350-360
DOI
Related Report
Peer Reviewed / Open Access
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[Presentation] Isoform-specific binding properties of Heterochromatin protein 12016
Author(s)
Suetake I, Mishima Y, Watanabe S, Shimizu M, Takada S
Organizer
4th Awaji International Workshop on “Electron Spin Science & Technology Biological and Materials Science Oriented Applications
Place of Presentation
Awaji Yumebutai International Conference Center （Hyogo, Awaji)
Year and Date
2016-06-19
Related Report
Int'l Joint Research / Invited
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