DA-complex assembly activity required for VP16C transcriptional activation

Naoko Kobayashi, Peter J. Horn, Susan M. Sullivan, Steven J. Triezenberg, Thomas G. Boyer, Arnold J. Berk

Research output: Contribution to journalArticlepeer-review

43 Scopus citations

Abstract

One class of transcriptional activation domains stimulates the concerted binding of TFIIA and TFIID to promoter DNA. To test whether this DA-complex assembly activity contributes significantly to the overall mechanism of activation in vivo, we analyzed mutants of the 38-amino-acid residue VP16C activation subdomain from herpes simplex virus. An excellent correlation was observed between the in vivo activation function of these mutants and their in vitro DA-complex assembly activity. Mutants severely defective for in vivo activation also showed reduced in vitro binding to native TFIIA. No significant correlation between in vivo activation function and in vitro binding to human TATA binding protein, human TFIIB, or Drosophila melanogaster TAF11 40 was observed for this set of VP16C mutants. These results argue that the ability of VP16C to increase the rate and extent of DA-complex assembly makes a significant contribution to the overall mechanism of transcriptional activation in vivo.

Original languageEnglish (US)
Pages (from-to)4023-4031
Number of pages9
JournalMolecular and cellular biology
Volume18
Issue number7
DOIs
StatePublished - Jul 1998

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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