p300 functions as a coactivator for the peroxisome proliferator-activated receptor alpha.
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.
Mesh Terms:
Amino Acid Sequence, Animals, Carcinogens, DNA, Histone Acetyltransferases, Humans, Mice, Microbodies, Molecular Sequence Data, Nuclear Proteins, Nuclear Receptor Coactivator 1, Nuclear Receptor Coactivator 3, Pyrimidines, Receptors, Cytoplasmic and Nuclear, Receptors, Retinoic Acid, Retinoid X Receptors, Saccharomyces cerevisiae, Trans-Activators, Transcription Factors, Transcriptional Activation, Tumor Cells, Cultured
Amino Acid Sequence, Animals, Carcinogens, DNA, Histone Acetyltransferases, Humans, Mice, Microbodies, Molecular Sequence Data, Nuclear Proteins, Nuclear Receptor Coactivator 1, Nuclear Receptor Coactivator 3, Pyrimidines, Receptors, Cytoplasmic and Nuclear, Receptors, Retinoic Acid, Retinoid X Receptors, Saccharomyces cerevisiae, Trans-Activators, Transcription Factors, Transcriptional Activation, Tumor Cells, Cultured
J. Biol. Chem.
Date: Dec. 26, 1997
PubMed ID: 9407140
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