About: The C-terminal domain of Brd2 is important for chromatin interaction and regulation of transcription and alternative splicing     Goto   Sponge   NotDistinct   Permalink

An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

AttributesValues
rdf:type
Description
  • 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.
  • 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. (en)
Title
  • The C-terminal domain of Brd2 is important for chromatin interaction and regulation of transcription and alternative splicing
  • The C-terminal domain of Brd2 is important for chromatin interaction and regulation of transcription and alternative splicing (en)
skos:prefLabel
  • The C-terminal domain of Brd2 is important for chromatin interaction and regulation of transcription and alternative splicing
  • The C-terminal domain of Brd2 is important for chromatin interaction and regulation of transcription and alternative splicing (en)
skos:notation
  • RIV/68378050:_____/13:00422977!RIV14-GA0-68378050
http://linked.open...avai/predkladatel
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • I, P(GAP305/10/0424), P(GBP208/12/G016), P(GBP305/12/G034), P(KAN200520801)
http://linked.open...iv/cisloPeriodika
  • 22
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
http://linked.open.../riv/druhVysledku
http://linked.open...iv/duvernostUdaju
http://linked.open...titaPredkladatele
http://linked.open...dnocenehoVysledku
  • 67447
http://linked.open...ai/riv/idVysledku
  • RIV/68378050:_____/13:00422977
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • Brd2; alternative splicing; chromatin (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • US - Spojené státy americké
http://linked.open...ontrolniKodProRIV
  • [B8C134D51C65]
http://linked.open...i/riv/nazevZdroje
  • Molecular Biology of the Cell
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...vavai/riv/projekt
http://linked.open...UplatneniVysledku
http://linked.open...v/svazekPeriodika
  • 24
http://linked.open...iv/tvurceVysledku
  • Hof, Martin
  • Stejskalová, Eva
  • Humpolíčková, Jana
  • Dušková, Eva
  • Hnilicová, Jarmila
  • Hozeifi, Samira
  • Staněk, David
  • Poser, I.
http://linked.open...ain/vavai/riv/wos
  • 000328124600007
issn
  • 1059-1524
number of pages
http://bibframe.org/vocab/doi
  • 10.1091/mbc.E13-06-0303
Faceted Search & Find service v1.16.118 as of Jun 21 2024


Alternative Linked Data Documents: ODE     Content Formats:   [cxml] [csv]     RDF   [text] [turtle] [ld+json] [rdf+json] [rdf+xml]     ODATA   [atom+xml] [odata+json]     Microdata   [microdata+json] [html]    About   
This material is Open Knowledge   W3C Semantic Web Technology [RDF Data] Valid XHTML + RDFa
OpenLink Virtuoso version 07.20.3240 as of Jun 21 2024, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (126 GB total memory, 48 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software