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

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F13%3A00424234" target="_blank" >RIV/61388971:_____/13:00424234 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61388955:_____/13:00422977 RIV/68378050:_____/13:00422977

Výsledek na webu

<a href="http://dx.doi.org/10.1091/mbc.E13-06-0303" target="_blank" >http://dx.doi.org/10.1091/mbc.E13-06-0303</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1091/mbc.E13-06-0303" target="_blank" >10.1091/mbc.E13-06-0303</a>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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, andthe 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 Brd2association 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 bromod

Název v anglickém jazyce

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

Popis výsledku anglicky

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, andthe 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 Brd2association 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 bromod

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

EE - Mikrobiologie, virologie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2013

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Molecular Biology of the Cell

ISSN

1059-1524

e-ISSN

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Svazek periodika

24

Číslo periodika v rámci svazku

22

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

12

Strana od-do

3557-3568

Kód UT WoS článku

000328124600007

EID výsledku v databázi Scopus

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