Assessing the permissiveness of transcriptional activator binding sites

Steven P. Rowe, Anna K. Mapp

Research output: Contribution to journalArticle

Abstract

Both genetic and biochemical data suggest that transcriptional activators with little sequence homology nevertheless function through interaction with a shared group of coactivators. Here we show that a series of peptidomimetic transcriptional activation domains interact under cell-free and cellular conditions with the metazoan coactivator CBP despite differences in the positioning and identity of the constituent functional groups. Taken together, these results suggest that a key activator binding site within CBP is permissive, accepting multiple arrangements of hydrophobic functional groups. Further, this permissiveness is also observed with a coactivator from S. cerevisiae. Thus, the design of small molecule mimics of transcriptional activation domains with broad function may be more straightforward than previously envisioned.

Original languageEnglish (US)
Pages (from-to)578-581
Number of pages4
JournalBiopolymers
Volume89
Issue number7
DOIs
StatePublished - Jul 1 2008
Externally publishedYes

Keywords

  • CBP
  • KIX domain
  • Med15
  • Transcriptional activator

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Biomaterials
  • Organic Chemistry

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