Abstract
p300 and cAMP response element-binding protein (CREB)-binding protein (CBP) are members of a family of coactivators involved in the regulation of transcription and chromatin. We show that transcription factors of the nuclear factor of activated T cells (NFAT) family bind p300/CBP and recruit histone acetyltransferase activity from T cell nuclear extracts. The NH2-terminal transactivation domain of NFAT1 and the phospho-CREB- and E1A-binding sites of p300/CBP are involved in the interaction. The viral oncoprotein E1A inhibits NFAT-dependent transactivation in a p300-dependent manner. Recruitment of the coactivators p300/CBP by the transactivation domains of NFAT proteins is likely to play a critical role in NFAT-dependent gene expression during the immune response.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Acetyltransferases / metabolism*
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Adenovirus E1A Proteins
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CREB-Binding Protein
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Cell Cycle Proteins / metabolism*
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Cytokines / biosynthesis
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DNA-Binding Proteins / genetics
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DNA-Binding Proteins / metabolism*
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Histone Acetyltransferases
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NFATC Transcription Factors
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Nuclear Proteins / metabolism*
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Precipitin Tests
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Protein Binding
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Saccharomyces cerevisiae Proteins*
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Subcellular Fractions / metabolism
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T-Lymphocytes / immunology*
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T-Lymphocytes / metabolism
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Trans-Activators*
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Transcription Factors / genetics
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Transcription Factors / metabolism*
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Transcriptional Activation*
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p300-CBP Transcription Factors
Substances
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Adenovirus E1A Proteins
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Cell Cycle Proteins
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Cytokines
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DNA-Binding Proteins
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NFATC Transcription Factors
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Nuclear Proteins
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Saccharomyces cerevisiae Proteins
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Trans-Activators
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Transcription Factors
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Acetyltransferases
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CREB-Binding Protein
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Histone Acetyltransferases
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p300-CBP Transcription Factors
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p300-CBP-associated factor