期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 107, 期 18, 页码 8153-8158出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0912509107
关键词
chromatin; transcription; transcription factor IID; x-ray crystallography
资金
- JSPS
- New Energy and Industrial Technology Development Organization (NEDO) of Japan
- Ministry of Education, Culture, Sports, Science, and Technology of Japan
- Mitsubishi Foundation
- Uehara Memorial Foundation
- Japan Science and Technology Agency (JST)
- Grants-in-Aid for Scientific Research [21370052] Funding Source: KAKEN
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. Here, we determined at 3.3 angstrom 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 here is the initial structure-based model of the biological signaling from histone modifications to structural change of the nucleosome (hi-MOST model).
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