TFIIA regulates TBP and TFIID dimers

Robert A. Coleman, Andrew K.P. Taggart, Sandeep Burma, John J. Chicca, B. Franklin Pugh

Research output: Contribution to journalArticlepeer-review

37 Scopus citations


Dimerization of the TATA-binding protein (TBP) through its DNA-binding domain blocks TBP from accessing DNA and prevents unregulated gene expression. TFIIA plays a central role in loading TBP and its multisubunit counterpart TFIID onto promoter DNA, and it is therefore a candidate for regulating TBP/TFIID dimerization. Here, we show that TFIIA promotes the dissociation of TBP dimers directly and in doing so accelerates the kinetics of DNA binding. TFIID dimer dissociation was found to be slow and rate limiting in DNA binding. TFIIA induced a rapid dissociation of TFIID dimers, allowing TFIID to readily load onto promoter DNA. Together, these results suggest a novel mechanism by which TFIIA assists in regulating gene expression.

Original languageEnglish (US)
Pages (from-to)451-457
Number of pages7
JournalMolecular Cell
Issue number3
StatePublished - Sep 1999
Externally publishedYes

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology


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