TY - JOUR
T1 - Involvement of chromatin and histone deacetylation in SV40T antigen transcription regulation
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
Y1 - 2007/3
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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U2 - 10.1093/nar/gkl1113
DO - 10.1093/nar/gkl1113
M3 - Article
C2 - 17341466
SN - 0305-1048
VL - 35
SP - 1958
EP - 1968
JO - Nucleic Acids Research
JF - Nucleic Acids Research
IS - 6
ER -