Involvement of chromatin and histone deacetylation in SV40T antigen transcription regulation

Ester Valls; Noemí Blanco-García; Naiara Aquizu; David Piedra; Conchi Estarás; Xavier de la Cruz; Marian A. Martínez-Balbás

doi:10.1093/nar/gkl1113

Involvement of chromatin and histone deacetylation in SV40T antigen transcription regulation

Ester Valls
, Noemí Blanco-García
, Naiara Aquizu
, David Piedra
, Conchi Estarás
, Xavier de la Cruz
, Marian A. Martínez-Balbás

University of Barcelona
Institute for Research in Biomedicine
ICREA

Research output: Contribution to journal › Article › peer-review

22 Scopus citations

Abstract

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.

Original language	English
Pages (from-to)	1958-1968
Number of pages	11
Journal	Nucleic Acids Research
Volume	35
Issue number	6
DOIs	https://doi.org/10.1093/nar/gkl1113
State	Published - Mar 2007
Externally published	Yes

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title = "Involvement of chromatin and histone deacetylation in SV40T antigen transcription regulation",

abstract = "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.",

author = "Ester Valls and Noem{\'i} Blanco-Garc{\'i}a and Naiara Aquizu and David Piedra and Conchi Estar{\'a}s and \{de la Cruz\}, Xavier and Mart{\'i}nez-Balb{\'a}s, \{Marian A.\}",

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AU - Valls, Ester

AU - Blanco-García, Noemí

AU - Aquizu, Naiara

AU - Piedra, David

AU - Estarás, Conchi

AU - de la Cruz, Xavier

AU - Martínez-Balbás, Marian A.

PY - 2007/3

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N2 - 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.

AB - 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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Involvement of chromatin and histone deacetylation in SV40T antigen transcription regulation

Abstract

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