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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 ASEP0422977
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitleThe 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) RID
    Source TitleMolecular Biology of the Cell - ISSN 1059-1524
    Roč. 24, č. 22 (2013), s. 3557-3568
    Number of pages12 s.
    Languageeng - English
    CountryUS - United States
    KeywordsBrd2 ; alternative splicing ; chromatin
    Subject RIVEB - Genetics ; Molecular Biology
    Subject RIV - cooperationJ. Heyrovsky Institute of Physical Chemistry - Physical ; Theoretical Chemistry
    R&D ProjectsKAN200520801 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 supportUMG-J - RVO:68378050 ; UFCH-W - RVO:61388955
    UT WOS000328124600007
    DOI10.1091/mbc.E13-06-0303
    AnnotationBrd2 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.
    WorkplaceInstitute of Molecular Genetics
    ContactNikol Škňouřilová, nikol.sknourilova@img.cas.cz, Tel.: 241 063 217
    Year of Publishing2014
Number of the records: 1  

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