The histone acetyltransferase PCAF associates with actin and hnRNP U for RNA polymerase II transcription

Ales Obrdlik, Alexander Kukalev, Emilie Louvet, Ann Kristin Östlund Farrants, Luca Caputo, Piergiorgio Percipalle

Research output: Contribution to journalArticlepeer-review

Abstract

Actin is a key regulator of RNA polymerase (pol) II transcription. In complex with specific hnRNPs, it has been proposed that actin functions to recruit pol II coactivators during the elongation of nascent transcripts. Here, we show by affinity chromatography, protein-protein interaction assays, and biochemical fractionation of nuclear extracts that the histone acetyltransferase (HAT) PCAF associates with actin and hnRNP U. PCAF and the nuclear actin-associated HAT activity detected in the DNase I-bound protein fraction could be released by disruption of the actin-hnRNP U complex. In addition, actin, hnRNP U, and PCAF were found to be associated with the Ser2/5- and Ser2-phosphorylated pol II carboxy-terminal domain construct. Chromatin and RNA immunoprecipitation assays demonstrated that actin, hnRNP U, and PCAF are present at the promoters and coding regions of constitutively expressed pol II genes and that they are associated with ribonucleoprotein complexes. Finally, disruption of the actin-hnRNP U interaction repressed bromouridine triphosphate incorporation in living cells, suggesting that actin and hnRNP U cooperate with PCAF in the regulation of pol II transcription elongation.

Original languageEnglish (US)
Pages (from-to)6342-6357
Number of pages16
JournalMolecular and cellular biology
Volume28
Issue number20
DOIs
StatePublished - Oct 2008

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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