The SV40 T antigen modulates CBP histone acetyltransferase activity.
Histone acetyltransferases (HATs) play a key role in transcription control, cell proliferation and differentiation by modulating chromatin structure; however, little is known about their own regulation. Here we show that expression of the viral oncoprotein SV40 T antigen increases histone acetylation and global cellular HAT activities. In addition, it enhances CREB-binding protein HAT activity and modulates its transcriptional activity. Finally, we show that inhibition of cellular histone deacetylases by trichostatin A increases the SV40 infectivity rate. These findings highlight the importance of histone acetylation in the regulation of the cell cycle by oncoviral proteins.
Valls
Ester
E
Instituto de Biología Molecular de Barcelona, CID, Consejo Superior de Investigaciones Científicas, Jordi Girona 18-26, E-08034 Barcelona, Spain.
de la Cruz
Xavier
X
Martínez-Balbás
Marian A
MA
D000107:Acetylation; D000123:Acetyltransferases / Q000378:metabolism*; D000818:Animals; D000952:Antigens, Polyomavirus Transforming / Q000378:metabolism / Q000494:pharmacology*; D050882:CREB-Binding Protein; D002460:Cell Line; D004789:Enzyme Activation; D051548:Histone Acetyltransferases; D056572:Histone Deacetylase Inhibitors; D006657:Histones / Q000378:metabolism; D006877:Hydroxamic Acids / Q000494:pharmacology; D009687:Nuclear Proteins / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism*; D013539:Simian virus 40 / Q000276:immunology / Q000472:pathogenicity; D015534:Trans-Activators / Q000378:metabolism*; D015533:Transcriptional Activation
D000952:Antigens, Polyomavirus Transforming; D056572:Histone Deacetylase Inhibitors; D006657:Histones; D006877:Hydroxamic Acids; D009687:Nuclear Proteins; D029701:Saccharomyces cerevisiae Proteins; D015534:Trans-Activators; C012589:trichostatin A; D000123:Acetyltransferases; D050882:CREB-Binding Protein; D051548:Histone Acetyltransferases