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 language | English (US) |
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Pages (from-to) | 578-581 |
Number of pages | 4 |
Journal | Biopolymers |
Volume | 89 |
Issue number | 7 |
DOIs | |
State | Published - Jul 2008 |
Externally published | Yes |
Keywords
- CBP
- KIX domain
- Med15
- Transcriptional activator
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Biomaterials
- Organic Chemistry