The Double Bromodomain Proteins Brd2 and Brd3 Couple Histone Acetylation to Transcription

Gary LeRoy, Brenden Rickards, S. J. Flint

Research output: Contribution to journalArticle

206 Scopus citations

Abstract

Posttranslational histone modifications are crucial for the modulation of chromatin structure and regulation of transcription. Bromodomains present in many chromatin-associated proteins recognize acetylated lysines in the unstructured N-terminal regions of histones. Here, we report that the double bromodomain proteins Brd2 and Brd3 associate preferentially in vivo with hyperacetylated chromatin along the entire lengths of transcribed genes. Brd2- and Brd3-associated chromatin is significantly enriched in H4K5, H4K12, and H3K14 acetylation and contains relatively little dimethylated H3K9. Both Brd2 and Brd3 allowed RNA polymerase II to transcribe through nucleosomes in a defined transcription system. Such activity depended on specific histone H4 modifications known to be recognized by the Brd proteins. We also demonstrate that Brd2 has intrinsic histone chaperone activity and is required for transcription of the cyclin D1 gene in vivo. These data identify proteins that render nucleosomes marked by acetylation permissive to the passage of elongating RNA polymerase II.

Original languageEnglish (US)
Pages (from-to)51-60
Number of pages10
JournalMolecular Cell
Volume30
Issue number1
DOIs
StatePublished - Apr 11 2008

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology

Keywords

  • DNA

Fingerprint Dive into the research topics of 'The Double Bromodomain Proteins Brd2 and Brd3 Couple Histone Acetylation to Transcription'. Together they form a unique fingerprint.

  • Cite this