Document Detail


Structure of the histone chaperone CIA/ASF1-double bromodomain complex linking histone modifications and site-specific histone eviction.
MedLine Citation:
PMID:  20393127     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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).
Authors:
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:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2010-04-14
Journal Detail:
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:
Created Date:  2010-05-05     Completed Date:  2010-06-08     Revised Date:  2010-11-05    
Medline Journal Info:
Nlm Unique ID:  7505876     Medline TA:  Proc Natl Acad Sci U S A     Country:  United States    
Other Details:
Languages:  eng     Pagination:  8153-8     Citation Subset:  IM    
Affiliation:
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.:
PDB/3AAD
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MeSH Terms
Descriptor/Qualifier:
Cell Cycle Proteins / 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:
0/ASF1A protein, human; 0/Cell Cycle Proteins; 0/Histones

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