Synthesis of histone protein for the post-translationally modified protein library
| Project/Area Number |
15K05565
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Bio-related chemistry
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| Research Institution | Osaka University |
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Principal Investigator |
Kawakami Toru 大阪大学, たんぱく質研究所, 准教授 (70273711)
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| Co-Investigator(Renkei-kenkyūsha) |
SUETAKE Isao 甲子園大学, 栄養学部, 教授 (80304054)
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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 |
¥5,070,000 (Direct Cost: ¥3,900,000、Indirect Cost: ¥1,170,000)
Fiscal Year 2017: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2016: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2015: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
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| Keywords | ヒストン / 翻訳後修飾 / ペプチドライゲーション / イソペプチド / チイラン / ユビキチン / DNAメチル化 |
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| Outline of Final Research Achievements |
The site specific modification of proteins such as post-translational modification (PTM) is important for studies of protein functions. The PTMs of histones play an important role in the epigenetic regulation. In this research we aimed to develop the methods for preparation of the site specifically modified histones by using the CPE ligation method.
At first, a semi-synthetic method was developed, in which recombinant C-terminal peptides were ligated with the N-terminal site specifically modified CPE peptides, followed by desulfurized to produce trimethyl lysine containing histones H3 and H4. We also developed a convenient method for preparation of isopeptide mimetics by using a thiirane linker. Using this method, ubiquitinated histone H3 peptide and full length H3 were prepared, and these peptides were used for their structural and functional studies. In addition, in order to develop more convenient synthetic method for histones preliminary result of solid phase peptide ligation.
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Report
(4 results)
Research Products
(19 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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