Abstract
Transcriptional coactivators have been viewed as constitutively active components, using transcription factors mainly to localize their functions. Here, it is shown that PPARgamma coactivator-1 (PGC-1) promotes transcription through the assembly of a complex that includes the histone acetyltransferases steroid receptor coactivator-1 (SRC-1) and CREB binding protein (CBP)/p300. PGC-1 has a low inherent transcriptional activity when it is not bound to a transcription factor. The docking of PGC-1 to peroxisome proliferator-activated receptor gamma (PPARgamma) stimulates an apparent conformational change in PGC-1 that permits binding of SRC-1 and CBP/p300, resulting in a large increase in transcriptional activity. Thus, transcription factor docking switches on the activity of a coactivator protein.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Binding Sites
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COS Cells
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DNA-Binding Proteins / metabolism
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E1A-Associated p300 Protein
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Gene Expression Regulation
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Histone Acetyltransferases
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Mice
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Nuclear Proteins / chemistry
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Nuclear Proteins / metabolism*
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Nuclear Receptor Coactivator 1
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Nuclear Respiratory Factors
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Protein Binding
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Protein Conformation
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Receptors, Cytoplasmic and Nuclear / metabolism*
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Recombinant Fusion Proteins / metabolism
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Trans-Activators / chemistry
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Trans-Activators / metabolism*
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Transcription Factors / chemistry
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Transcription Factors / metabolism*
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Transcription, Genetic*
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Transfection
Substances
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DNA-Binding Proteins
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Nuclear Proteins
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Nuclear Respiratory Factors
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Receptors, Cytoplasmic and Nuclear
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Recombinant Fusion Proteins
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Trans-Activators
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Transcription Factors
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peroxisome-proliferator-activated receptor-gamma coactivator-1
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E1A-Associated p300 Protein
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Ep300 protein, mouse
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Histone Acetyltransferases
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Ncoa1 protein, mouse
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Nuclear Receptor Coactivator 1