Počet záznamů: 1  

The C-terminal domain of Brd2 is important for chromatin interaction and regulation of transcription and alternative splicing

  1. 1.
    0422977 - UMG-J 2014 RIV US eng J - Článek v odborném periodiku
    Hnilicová, Jarmila - Hozeifi, Samira - Stejskalová, Eva - Dušková, Eva - Poser, I. - Humpolíčková, Jana - Hof, Martin - Staněk, David
    The C-terminal domain of Brd2 is important for chromatin interaction and regulation of transcription and alternative splicing.
    Molecular Biology of the Cell. Roč. 24, č. 22 (2013), s. 3557-3568. ISSN 1059-1524
    Grant CEP: GA AV ČR KAN200520801; GA ČR GAP305/10/0424; GA ČR GBP208/12/G016; GA ČR(CZ) GBP305/12/G034
    Institucionální podpora: RVO:68378050 ; RVO:61388955
    Klíčová slova: Brd2 * alternative splicing * chromatin
    Kód oboru RIV: EB - Genetika a molekulární biologie; CF - Fyzikální chemie a teoretická chemie (UFCH-W)
    Impakt faktor: 4.548, rok: 2013

    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.
    Trvalý link: http://hdl.handle.net/11104/0229180