Abstract
The integrator protein, p300, was demonstrated to interact with mouse peroxisome proliferator-activated receptor alpha in a ligand-enhanced manner. The PPARalpha-interacting domain of p300 was mapped to amino acids 39-117 which interacted strongly with PPARalpha but did not interact with retinoic acid receptor-gamma or retinoid X receptor-alpha. Amino acids within the carboxyl terminus of PPARalpha as well as residues within the hinge region were required for ligand-dependent interaction with p300. p300 enhanced the transcriptional activation properties of PPARalpha and, therefore, can be considered a bona fide coactivator for this nuclear receptor. These observations extend the group of p300-interacting proteins to include mPPARalpha and further characterize the molecular mechanisms of PPARalpha-mediated transcriptional regulation.
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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Amino Acid Sequence
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Animals
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Carcinogens / pharmacology
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DNA / metabolism
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Histone Acetyltransferases
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Humans
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Mice
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Microbodies / metabolism*
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Molecular Sequence Data
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Nuclear Proteins / metabolism*
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Nuclear Receptor Coactivator 1
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Nuclear Receptor Coactivator 3
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Pyrimidines
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Receptors, Cytoplasmic and Nuclear / metabolism*
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Receptors, Retinoic Acid / metabolism
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Retinoid X Receptors
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Saccharomyces cerevisiae
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Trans-Activators / metabolism*
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Transcription Factors / metabolism*
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Transcriptional Activation
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Tumor Cells, Cultured
Substances
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Carcinogens
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Nuclear Proteins
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Pyrimidines
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Receptors, Cytoplasmic and Nuclear
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Receptors, Retinoic Acid
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Retinoid X Receptors
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Trans-Activators
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Transcription Factors
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pirinixic acid
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DNA
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Histone Acetyltransferases
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NCOA1 protein, human
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NCOA3 protein, human
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Ncoa1 protein, mouse
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Ncoa3 protein, mouse
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Nuclear Receptor Coactivator 1
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Nuclear Receptor Coactivator 3