3AAD

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

Summary for 3AAD

• Entry DOI: 10.2210/pdb3aad/pdb
• Descriptor: Transcription initiation factor TFIID subunit 1, Histone chaperone ASF1A, SULFATE ION (3 entities in total)
• Functional Keywords: protein-protein complex, bromodomain, transcription, transcription regulation, chaperone, chromatin regulator, transcription-chaperone complex, transcription/chaperone
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus : P21675 Q9Y294
• Total number of polymer chains: 3
• Total formula weight: 70215.36

Authors

Akai, Y.,Adachi, N.,Hayashi, Y.,Eitoku, M.,Sano, N.,Natsume, R.,Kudo, N.,Tanokura, M.,Senda, T.,Horikoshi, M. (deposition date: 2009-11-16, release date: 2010-04-28, Last modification date: 2024-11-20)

Primary citation

Akai, Y.,Adachi, N.,Hayashi, Y.,Eitoku, M.,Sano, N.,Natsume, R.,Kudo, N.,Tanokura, M.,Senda, T.,Horikoshi, M.
Structure of the histone chaperone CIA/ASF1-double bromodomain complex linking histone modifications and site-specific histone eviction
Proc.Natl.Acad.Sci.USA, 107:8153-8158, 2010

PubMed 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. 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).

PubMed: 20393127
DOI: 10.1073/pnas.0912509107

Experimental method

X-RAY DIFFRACTION (3.3 Å)