This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Obrdlik, A.
Right arrow Articles by Percipalle, P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Obrdlik, A.
Right arrow Articles by Percipalle, P.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, October 2008, p. 6342-6357, Vol. 28, No. 20
0270-7306/08/$08.00+0     doi:10.1128/MCB.00766-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

The Histone Acetyltransferase PCAF Associates with Actin and hnRNP U for RNA Polymerase II Transcription{triangledown}

Ales Obrdlik,1 Alexander Kukalev,1 Emilie Louvet,1 Ann-Kristin Östlund Farrants,2 Luca Caputo,1 and Piergiorgio Percipalle1*

Department of Cell and Molecular Biology, Medical Nobel Institute, Karolinska Institute, Box 285, Stockholm SE-171 77, Sweden,1 Institute of Cell Biology, Wenner-Gren Institute, Stockholm University, Stockholm SE-106 91, Sweden2

Received 13 May 2008/ Returned for modification 3 June 2008/ Accepted 12 August 2008

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.


* Corresponding author. Mailing address: Department of Cell and Molecular Biology, Medical Nobel Institute, Karolinska Institute, Box 285, Stockholm SE-171 77, Sweden. Phone: 46-8-52487546. Fax: 46-8-313529. E-mail: piergiorgio.percipalle{at}ki.se

{triangledown} Published ahead of print on 18 August 2008.


Molecular and Cellular Biology, October 2008, p. 6342-6357, Vol. 28, No. 20
0270-7306/08/$08.00+0     doi:10.1128/MCB.00766-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:

  • Fromm, G., de Vries, C., Byron, R., Fields, J., Fiering, S., Groudine, M., Bender, M. A., Palis, J., Bulger, M. (2009). Histone hyperacetylation within the {beta}-globin locus is context-dependent and precedes high-level gene expression. Blood 114: 3479-3488 [Abstract] [Full Text]