Abstract
The p53 tumor suppressor protein functions as an activator and also as a repressor of gene transcription. Currently, the mechanism of transcriptional repression by p53 remains poorly understood. To help clarify this mechanism, we carried out studies designed to identify the minimal repression domain that inhibits p53 transcriptional activities. We found only eight amino acids (339) of the COOH-terminal domain (termed P53MRD) that possess activities of repression. The exact location of this minimal domain is on the E6-binding region, and it lacks the ability of tetramerization. P53MRD is able to repress the transcription of p53 while not affecting VP16. The mutants (amino acids M340P and F341D) of native p53 also lost transcriptional repression of the thymidine kinase chloramphenicol acetyltransferase promoter. These results suggest that this eight-amino acid element is required for the repression of p53.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Binding Sites
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Chloramphenicol O-Acetyltransferase / genetics
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Chloramphenicol O-Acetyltransferase / metabolism
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DNA-Binding Proteins / genetics
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Fungal Proteins / genetics
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Genes, Reporter
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Herpes Simplex Virus Protein Vmw65 / genetics
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Humans
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Peptide Fragments / metabolism
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Recombinant Fusion Proteins / metabolism
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Repressor Proteins / metabolism*
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Saccharomyces cerevisiae Proteins*
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Thymidine Kinase / genetics
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Transcription Factors / genetics
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Transcription, Genetic
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Transcriptional Activation
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Transfection
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Tumor Cells, Cultured
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Tumor Suppressor Protein p53 / chemistry*
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Tumor Suppressor Protein p53 / genetics
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Tumor Suppressor Protein p53 / metabolism*
Substances
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DNA-Binding Proteins
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Fungal Proteins
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GAL4 protein, S cerevisiae
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Herpes Simplex Virus Protein Vmw65
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Peptide Fragments
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Recombinant Fusion Proteins
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Repressor Proteins
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Saccharomyces cerevisiae Proteins
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Transcription Factors
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Tumor Suppressor Protein p53
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Chloramphenicol O-Acetyltransferase
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Thymidine Kinase