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) |
|---|---|
| Pages (from-to) | 578-581 |
| Number of pages | 4 |
| Journal | Biopolymers |
| Volume | 89 |
| Issue number | 7 |
| DOIs | |
| State | Published - Jul 2008 |
| Externally published | Yes |
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Keywords
- CBP
- KIX domain
- Med15
- Transcriptional activator
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Biomaterials
- Organic Chemistry
- Biochemistry, Genetics and Molecular Biology(all)
Cite this
Assessing the permissiveness of transcriptional activator binding sites. / Rowe, Steven; Mapp, Anna K.
In: Biopolymers, Vol. 89, No. 7, 07.2008, p. 578-581.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Assessing the permissiveness of transcriptional activator binding sites
AU - Rowe, Steven
AU - Mapp, Anna K.
PY - 2008/7
Y1 - 2008/7
N2 - 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.
AB - 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.
KW - CBP
KW - KIX domain
KW - Med15
KW - Transcriptional activator
UR - http://www.scopus.com/inward/record.url?scp=49149106179&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=49149106179&partnerID=8YFLogxK
U2 - 10.1002/bip.20946
DO - 10.1002/bip.20946
M3 - Article
C2 - 18253946
AN - SCOPUS:49149106179
VL - 89
SP - 578
EP - 581
JO - Biopolymers
JF - Biopolymers
SN - 0006-3525
IS - 7
ER -