Abstract
RNA polymerases I, II, and III each use the TATA-binding protein (TBP). Regulators that target this shared factor may therefore provide a means to coordinate the activities of the three nuclear RNA polymerases. The repressor Dr1 binds to TBP and blocks the interaction of TBP with polymerase II- and polymerase III-specific factors. This enables Dr1 to coordinately regulate transcription by RNA polymerases II and III. Under the same conditions, Dr1 does not inhibit polymerase I transcription. By selectively repressing polymerases II and III, Dr1 may shift the physiological balance of transcriptional output in favor of polymerase I.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Base Sequence
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DNA-Binding Proteins / metabolism
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HeLa Cells
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Humans
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Molecular Sequence Data
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Phosphoproteins / metabolism
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Phosphoproteins / pharmacology*
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RNA Polymerase I / metabolism*
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RNA Polymerase II / metabolism*
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RNA Polymerase III / metabolism*
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Saccharomyces cerevisiae Proteins
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TATA Box
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TATA-Binding Protein Associated Factors
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TATA-Box Binding Protein
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Transcription Factor TFIIB
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Transcription Factor TFIIIB
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Transcription Factors / metabolism
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Transcription Factors / pharmacology*
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Transcription Factors, TFIII*
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Transcription, Genetic / drug effects*
Substances
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BRF1 protein, S cerevisiae
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BRF1 protein, human
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DNA-Binding Proteins
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Phosphoproteins
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Saccharomyces cerevisiae Proteins
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TATA-Binding Protein Associated Factors
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TATA-Box Binding Protein
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Transcription Factor TFIIB
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Transcription Factor TFIIIB
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Transcription Factors
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Transcription Factors, TFIII
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down-regulator of transcription 1
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transcription factor TFIIIC
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RNA Polymerase II
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RNA Polymerase I
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RNA Polymerase III