Elucidation of the mechanism of nucleosomal structural change mediated by histone modifications
| Project/Area Number |
21370052
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Functional biochemistry
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| Research Institution | The University of Tokyo |
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Principal Investigator |
HORIKOSHI Masami 東京大学, 分子細胞生物学研究所, 准教授 (70242089)
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| Project Period (FY) |
2009 – 2011
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| Project Status |
Completed (Fiscal Year 2011)
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| Budget Amount *help |
¥18,980,000 (Direct Cost: ¥14,600,000、Indirect Cost: ¥4,380,000)
Fiscal Year 2011: ¥4,550,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥1,050,000)
Fiscal Year 2010: ¥6,370,000 (Direct Cost: ¥4,900,000、Indirect Cost: ¥1,470,000)
Fiscal Year 2009: ¥8,060,000 (Direct Cost: ¥6,200,000、Indirect Cost: ¥1,860,000)
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| Keywords | 遺伝子の情報発現と複製 / 遺伝子 / 酵素 / 生体分子 / 構造変換 / 蛋白質 / 発現制御 |
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| Research Abstract |
Nucleosomes around the promoter region are disassembled for transcription in response to various signals, such as acetylation and methylation of histones. Although the interactions between histone-acetylation- recognizing bromodomains and factors involved in nucleosome disassembly have been reported, no structural basis connecting histone modifications and nucleosome disassembly has been obtained. We determined at 3.3 A resolution the crystal structure of histone chaperone cell cycle gene 1 (CCG1) interacting factor A/antisilencing function 1 (CIA/ASF1) in complex with the double bromodomain in the CCG1/TAF1/TAF(II)250 subunit of transcription factor IID. Structural, biochemical, and biological studies suggested that interaction between double bromodomain and CIA/ASF1 is required for their colocalization, histone eviction, and pol II entry at active promoter regions. Furthermore, the present crystal structure has characteristics that can connect histone acetylation and CIA/ASF1-mediated histone eviction. These findings suggest that the molecular complex between CIA/ASF1 and the double bromodomain plays a key role in site-specific histone eviction at active promoter regions. The model we propose in this study is the initial structure-based model of the biological signaling fromhistone modifications to structural change of the nucleosome (hi-MOST model).
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Report
(4 results)
Research Products
(33 results)
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[Journal Article] The histone chaperone FACT maintains replication fork rates2011
Author(s)
T.Abe, K.Sugimura, Y.Hosono, Y.Takami, M.Akita, A.Yoshimura, S.Tada, T.Nakayama, H.Murofushi, K.Okumura, S.Takeda, M.Horikoshi, M.Seki & T.Enomoto
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Journal Title
J.Biol.Chem.
Volume: 286
Issue: 35
Pages: 30504-30512
DOI
Related Report
Peer Reviewed
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