Abstract
A yeast TBP mutant (N2-1) is described here that is defective specifically in responding to acidic activators in vivo. N2-1 does not support activation by Gal4, Ace1, and Gcn4, but appears unaffected for constitutive transcription, repression by the Cyc8-Tup1 and Not complexes, and transcription by polymerase I (Pol) and Pol III. In vitro, N2-1 fails to interact with TFIIA, but it associates normally with a TATA element, an acidic activation domain, and TFIIB. Fusion of the small subunit of TFIIA to N2-1 restores activation function in vivo. Thus, an efficient interaction between TBP and TFIIA is required for transcriptional activation in vivo.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Base Sequence
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DNA-Binding Proteins / genetics
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DNA-Binding Proteins / metabolism*
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DNA-Binding Proteins / physiology
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DNA-Directed RNA Polymerases / metabolism
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Fungal Proteins / physiology
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Hydrogen-Ion Concentration
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Immediate-Early Proteins / physiology
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Molecular Sequence Data
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Mutation
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Nuclear Proteins*
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Nuclear Receptor Subfamily 4, Group A, Member 2
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Protein Kinases / physiology
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Repressor Proteins*
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Saccharomyces cerevisiae / genetics*
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Saccharomyces cerevisiae / growth & development
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Saccharomyces cerevisiae Proteins*
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TATA Box*
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TATA-Box Binding Protein
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Trans-Activators / physiology*
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Transcription Factor TFIIA
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Transcription Factors / genetics
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Transcription Factors / metabolism*
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Transcription Factors / physiology
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Transcriptional Activation*
Substances
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CUP2 protein, S cerevisiae
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CYC8 protein, S cerevisiae
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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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Immediate-Early Proteins
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Nuclear Proteins
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Nuclear Receptor Subfamily 4, Group A, Member 2
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Repressor Proteins
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Saccharomyces cerevisiae Proteins
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TATA-Box Binding Protein
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TUP1 protein, S cerevisiae
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Trans-Activators
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Transcription Factor TFIIA
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Transcription Factors
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Protein Kinases
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DNA-Directed RNA Polymerases