Abstract
Essentially all nuclear eukaryotic gene transcription depends upon the function of the transcription factor TATA-binding protein (TBP). Here we show that the abundant, multifunctional DNA binding transcription factor repressor activator protein Rap1p interacts directly with TBP. TBP-Rap1p binding occurs efficiently in vivo at physiological expression levels, and in vitro analyses confirm that this is a direct interaction. The DNA binding domains of the two proteins mediate interaction between TBP and Rap1p. TBP-Rap1p complex formation inhibits TBP binding to TATA promoter DNA. Alterations in either Rap1p or TBP levels modulate mRNA gene transcription in vivo. We propose that Rap1p represents a heretofore unrecognized regulator of TBP.
Publication types
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Research Support, N.I.H., Extramural
MeSH terms
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DNA, Fungal / genetics
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DNA, Fungal / metabolism
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Gene Expression Regulation, Fungal*
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Models, Molecular
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Nucleic Acid Conformation
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Protein Binding
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Protein Structure, Quaternary
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Protein Structure, Tertiary
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RNA, Messenger / genetics
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RNA, Messenger / metabolism
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Saccharomyces cerevisiae / genetics*
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Saccharomyces cerevisiae / metabolism
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Saccharomyces cerevisiae Proteins / genetics
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Saccharomyces cerevisiae Proteins / metabolism*
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Shelterin Complex
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TATA-Box Binding Protein / chemistry
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TATA-Box Binding Protein / genetics
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TATA-Box Binding Protein / metabolism*
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Telomere-Binding Proteins / genetics
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Telomere-Binding Proteins / metabolism*
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Transcription Factors / genetics
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Transcription Factors / metabolism*
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Transcription, Genetic / genetics
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Up-Regulation
Substances
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DNA, Fungal
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RAP1 protein, S cerevisiae
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RNA, Messenger
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Saccharomyces cerevisiae Proteins
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Shelterin Complex
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TATA-Box Binding Protein
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Telomere-Binding Proteins
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Transcription Factors