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The C-terminal domain of Brd2 is important for chromatin interaction and regulation of transcription and alternative splicing
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SYSNO ASEP 0422977 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title The C-terminal domain of Brd2 is important for chromatin interaction and regulation of transcription and alternative splicing Author(s) Hnilicová, Jarmila (UMG-J)
Hozeifi, Samira (UMG-J)
Stejskalová, Eva (UMG-J)
Dušková, Eva (UMG-J)
Poser, I. (DE)
Humpolíčková, Jana (UFCH-W) RID
Hof, Martin (UFCH-W) RID, ORCID
Staněk, David (UMG-J) RIDSource Title Molecular Biology of the Cell - ISSN 1059-1524
Roč. 24, č. 22 (2013), s. 3557-3568Number of pages 12 s. Language eng - English Country US - United States Keywords Brd2 ; alternative splicing ; chromatin Subject RIV EB - Genetics ; Molecular Biology Subject RIV - cooperation J. Heyrovsky Institute of Physical Chemistry - Physical ; Theoretical Chemistry R&D Projects KAN200520801 GA AV ČR - Academy of Sciences of the Czech Republic (AV ČR) GAP305/10/0424 GA ČR - Czech Science Foundation (CSF) GBP208/12/G016 GA ČR - Czech Science Foundation (CSF) GBP305/12/G034 GA ČR - Czech Science Foundation (CSF) Institutional support UMG-J - RVO:68378050 ; UFCH-W - RVO:61388955 UT WOS 000328124600007 DOI 10.1091/mbc.E13-06-0303 Annotation Brd2 is a member of the bromodomain extra terminal (BET) protein family, which consists of four chromatin-interacting proteins that regulate gene expression. Each BET protein contains two N-terminal bromodomains, which recognize acetylated histones, and the C-terminal protein-protein interaction domain. Using a genome-wide screen, we identify 1450 genes whose transcription is regulated by Brd2. In addition, almost 290 genes change their alternative splicing pattern upon Brd2 depletion. Brd2 is specifically localized at promoters of target genes, and our data show that Brd2 interaction with chromatin cannot be explained solely by histone acetylation. Using coimmunoprecipitation and live-cell imaging, we show that the C-terminal part is crucial for Brd2 association with chromatin. Live-cell microscopy also allows us to map the average binding time of Brd2 to chromatin and quantify the contributions of individual Brd2 domains to the interaction with chromatin. Finally, we show that bromodomains and the C-terminal domain are equally important for transcription and splicing regulation, which correlates with the role of these domains in Brd2 binding to chromatin. Workplace Institute of Molecular Genetics Contact Nikol Škňouřilová, nikol.sknourilova@img.cas.cz, Tel.: 241 063 217 Year of Publishing 2014
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