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Nucleic Acids Research Advance Access published online on March 6, 2007
Nucleic Acids Research, doi:10.1093/nar/gkl1113
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© 2007 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Molecular Biology

Involvement of chromatin and histone deacetylation in SV40 T antigen transcription regulation

Ester Valls1, Noemí Blanco-García1, Naiara Aquizu1, David Piedra2, Conchi Estarás1, Xavier de la Cruz2,3 and Marian A. Martínez-Balbás1,*

1Instituto de Biología Molecular de Barcelona. CID. Consejo Superior de Investigaciones Científicas (CSIC). Josep Samitier 1,5. Parc Cientific de Barcelona. E-08028 Barcelona. Spain, 2Institut de Recerca Biomédica-PCB. Josep Samitier 1, 5. E-08028 Barcelona, Spain and 3Institut Català per la Recerca i Estudis Avançats (ICREA). Passeig Lluís Companys, 23. E-08018 Barcelona, Spain

*To whom correspondance should be addressed. Tel: 34-93-4034961; Fax: 34-93-4034979; Email: mmbbmc{at}ibmb.csic.es

Received June 29, 2006. Revised December 5, 2006. Accepted December 6, 2006.

Simian Virus 40 (SV40) large T antigen (T Ag) is a multifunctional viral oncoprotein that regulates viral and cellular transcriptional activity. However, the mechanisms by which such regulation occurs remain unclear. Here we show that T antigen represses CBP-mediated transcriptional activity. This repression is concomitant with histone H3 deacetylation and is TSA sensitive. Moreover, our results demonstrate that T antigen interacts with HDAC1 in vitro in an Rb-independent manner. In addition, the overexpression of HDAC1 cooperates with T antigen to antagonize CBP transactivation function and correlates with chromatin deacetylation of the TK promoter. Finally, decreasing HDAC1 levels with small interfering RNA (siRNA) partially abolishes T antigen-induced repression. These findings highlight the importance of the histone acetylation/deacetylation balance in the cellular transformation mediated by oncoviral proteins.


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