Abstract
The tumor suppressor protein p53 exerts its cell cycle-regulatory effects through its ability to function as a sequence-specific DNA-binding transcription factor. Herein, we show that p53 physically interacts with specific subregions of steroid receptor coactivator-1 (SRC-1) and its family members, p/CIP (p300/CBP interacting protein), xSRC-3, and AIB1 (amplified in breast cancer), originally isolated as transcription coactivators of nuclear receptors, as demonstrated by the yeast and mammalian two-hybrid tests as well as glutathione S-transferase pull-down assays. Interestingly, cotransfection of HeLa cells with SRC-1- or p/CIP expression vector potentiated the p53-mediated transactivation, whereas AIB1 and xSRC-3 were repressive. All of these SRC-1 members, however, similarly stimulated transactivation mediated by nuclear receptors and AP-1, as previously described. These results suggest that SRC-1 and its family members may differentially modulate the p53 transactivation in vivo.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Acetyltransferases
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism
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HeLa Cells / metabolism
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Histone Acetyltransferases
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Humans
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Nuclear Receptor Coactivator 1
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Nuclear Receptor Coactivator 3
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Oncogene Proteins
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Protein Isoforms
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Serine Endopeptidases / genetics
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Serine Endopeptidases / metabolism
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Trans-Activators / genetics
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Trans-Activators / metabolism
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Transcription Factors / genetics
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Transcription Factors / metabolism*
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Transcriptional Activation
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Transfection
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Tumor Suppressor Protein p53 / genetics
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Tumor Suppressor Protein p53 / metabolism*
Substances
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Bacterial Proteins
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LexA protein, Bacteria
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Oncogene Proteins
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Protein Isoforms
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Recombinant Proteins
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Trans-Activators
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Transcription Factors
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Tumor Suppressor Protein p53
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Acetyltransferases
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Histone Acetyltransferases
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NCOA1 protein, human
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NCOA3 protein, human
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Nuclear Receptor Coactivator 1
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Nuclear Receptor Coactivator 3
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Serine Endopeptidases