Slow dimer dissociation of the TATA binding protein dictates the kinetics of DNA binding

Robert A. Coleman, B. Franklin Pugh

Research output: Contribution to journalArticle

57 Scopus citations

Abstract

The association of the TATA binding protein (TBP) to eukaryotic promoters is a possible rate-limiting step in gene expression. Slow promoter binding might be related to TBP's ability to occlude its DNA binding domain through dimerization. Using a 'pull-down' based assay, we find that TBP dimers dissociate slowly (t( 1/4 ) = 6-10 min), and thus present a formidable kinetic barrier to TATA binding. At 10 nM, TBP appears to exist as a mixed population of monomers and dimers. In this state, TATA binding displays burst kinetics that appears to reflect rapid binding of monomers and slow dissociation of dimers. The kinetics of the slow phase is in excellent agreement with direct measurements of the kinetics of dimer dissociation.

Original languageEnglish (US)
Pages (from-to)7221-7226
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume94
Issue number14
DOIs
Publication statusPublished - Jul 8 1997
Externally publishedYes

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Keywords

  • DNA interactions
  • KINSIM
  • Protein
  • TFIID

ASJC Scopus subject areas

  • General

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