Fluorescence-based analyses of the effects of full-length recombinant TAF130p on the interaction of TATA box-binding protein with TATA box DNA.
We have used a combination of fluorescence anisotropy spectroscopy and fluorescence-based native gel electrophoresis methods to examine the effects of the transcription factor IID-specific subunit TAF130p (TAF145p) upon the TATA box DNA binding properties of TATA box-binding protein (TBP). Purified full-length recombinant TAF130p decreases TBP-TATA DNA complex formation at equilibrium ... by competing directly with DNA for binding to TBP. Interestingly, we have found that full-length TAF130p is capable of binding multiple molecules of TBP with nanomolar binding affinity. The biological implications of these findings are discussed.
Mesh Terms:
DNA, DNA-Binding Proteins, Electrophoresis, Fluorescence Polarization, Macromolecular Substances, Protein Binding, Protein Subunits, Recombinant Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Spectrometry, Fluorescence, TATA Box, TATA-Binding Protein Associated Factors, TATA-Box Binding Protein, Transcription Factor TFIID, Transcription Factors
DNA, DNA-Binding Proteins, Electrophoresis, Fluorescence Polarization, Macromolecular Substances, Protein Binding, Protein Subunits, Recombinant Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Spectrometry, Fluorescence, TATA Box, TATA-Binding Protein Associated Factors, TATA-Box Binding Protein, Transcription Factor TFIID, Transcription Factors
J. Biol. Chem.
Date: Dec. 28, 2001
PubMed ID: 11677244
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