Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Acetylation
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Acetyltransferases / metabolism*
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Animals
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Antigens, Polyomavirus Transforming / metabolism
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Antigens, Polyomavirus Transforming / pharmacology*
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CREB-Binding Protein
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Cell Line
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Enzyme Activation
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Histone Acetyltransferases
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Histone Deacetylase Inhibitors
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Histones / metabolism
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Hydroxamic Acids / pharmacology
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Nuclear Proteins / metabolism*
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Saccharomyces cerevisiae Proteins / metabolism*
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Simian virus 40 / immunology
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Simian virus 40 / pathogenicity
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Trans-Activators / metabolism*
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Transcriptional Activation
Substances
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Antigens, Polyomavirus Transforming
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Histone Deacetylase Inhibitors
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Histones
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Hydroxamic Acids
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Nuclear Proteins
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Saccharomyces cerevisiae Proteins
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Trans-Activators
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trichostatin A
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Acetyltransferases
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CREB-Binding Protein
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Histone Acetyltransferases