| Structure of the histone chaperone CIA/ASF1-double bromodomain complex linking histone modifications and site-specific histone eviction. | |
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MedLine Citation:
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PMID: 20393127 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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 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 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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Authors:
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Yusuke Akai; Naruhiko Adachi; Yohei Hayashi; Masamitsu Eitoku; Norihiko Sano; Ryo Natsume; Norio Kudo; Masaru Tanokura; Toshiya Senda; Masami Horikoshi |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2010-04-14 |
Journal Detail:
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Title: Proceedings of the National Academy of Sciences of the United States of America Volume: 107 ISSN: 1091-6490 ISO Abbreviation: Proc. Natl. Acad. Sci. U.S.A. Publication Date: 2010 May |
Date Detail:
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Created Date: 2010-05-05 Completed Date: 2010-06-08 Revised Date: 2010-11-05 |
Medline Journal Info:
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Nlm Unique ID: 7505876 Medline TA: Proc Natl Acad Sci U S A Country: United States |
Other Details:
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Languages: eng Pagination: 8153-8 Citation Subset: IM |
Affiliation:
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Biomedicinal Information Research Center, National Institute of Advanced Industrial Science and Technology, 2-4-7 Aomi, Koto-ku, Tokyo 135-0064, Japan. |
| Data Bank Information | |
Bank Name/Acc. No.:
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PDB/3AAD |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Cell Cycle Proteins
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chemistry*,
genetics,
metabolism Crystallography, X-Ray Histones / chemistry*, metabolism Humans Models, Molecular Mutation Promoter Regions, Genetic Protein Binding Protein Structure, Quaternary Protein Structure, Tertiary |
| Chemical | |
Reg. No./Substance:
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0/ASF1A protein, human; 0/Cell Cycle Proteins; 0/Histones |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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