Fluorescence-based analyses of the effects of full-length recombinant TAF130p on the interaction of TATA box-binding protein with TATA box DNA.

Banik U, Beechem JM, Klebanow E, Schroeder S, Weil PA
J Biol Chem. 2001 276 (52): 49100-9

PMID: 11677244 · DOI:10.1074/jbc.M109246200

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 (16)

DNA DNA-Binding Proteins Electrophoresis Fluorescence Polarization Macromolecular Substances Protein Binding Protein Subunits Recombinant Proteins Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins Spectrometry, Fluorescence TATA-Binding Protein Associated Factors TATA-Box Binding Protein TATA Box Transcription Factors Transcription Factor TFIID

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