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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, J M; Klebanow, E; Schroeder, S; Weil, P A.
Afiliación
  • Banik U; Department of Molecular Physiology and Biophysics, Vanderbilt University, School of Medicine, Nashville, Tennessee 37232-0615, USA.
J Biol Chem ; 276(52): 49100-9, 2001 Dec 28.
Article en En | MEDLINE | ID: mdl-11677244
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.
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Factores de Transcripción / TATA Box / Factores Asociados con la Proteína de Unión a TATA / Factor de Transcripción TFIID / Proteínas de Unión al ADN Idioma: En Revista: J Biol Chem Año: 2001 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos
Buscar en Google
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Factores de Transcripción / TATA Box / Factores Asociados con la Proteína de Unión a TATA / Factor de Transcripción TFIID / Proteínas de Unión al ADN Idioma: En Revista: J Biol Chem Año: 2001 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos