Structure of the histone chaperone CIA/ASF1-double bromodomain complex linking histone modifications and site-specific histone eviction

Yusuke Akai, Naruhiko Adachi, Yohei Hayashi, Masamitsu Eitoku, Norihiko Sano, Ryo Natsume, Norio Kudo, Masaru Tanokura, Toshiya Senda, Masami Horikoshi

研究成果: Article査読

21 被引用数 (Scopus)

抄録

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 Å 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 fromhistone modifications to structural change of the nucleosome (hi-MOST model).

本文言語English
ページ(範囲)8153-8158
ページ数6
ジャーナルProceedings of the National Academy of Sciences of the United States of America
107
18
DOI
出版ステータスPublished - 2010 5月 4
外部発表はい

ASJC Scopus subject areas

  • 一般

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