Direct and selective binding of an acidic transcriptional activation domain to the TATA-box factor TFIID

Nature. 1990 Jun 28;345(6278):783-6. doi: 10.1038/345783a0.


The potent transactivation domain of the herpes simplex virion protein VP16 was used as a column ligand for affinity chromatography. VP16 binds strongly and highly selectively to the human and yeast TATA box-binding factors. Our results imply that the principal target for acidic activation domains is the TATA-box factor TFIID.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Chromatography, Affinity
  • HeLa Cells
  • Herpes Simplex
  • Humans
  • Phosphoproteins / metabolism*
  • Phosphoproteins / ultrastructure
  • Protein Binding
  • RNA Polymerase II / metabolism
  • Regulatory Sequences, Nucleic Acid*
  • Saccharomyces cerevisiae / genetics
  • Trans-Activators / metabolism*
  • Trans-Activators / ultrastructure
  • Transcription Factors / metabolism*
  • Transcription Factors / ultrastructure


  • Phosphoproteins
  • Trans-Activators
  • Transcription Factors
  • RNA Polymerase II