In Succharomyces cerevisiae the GCRl gene product is required for high-level expression o f genes encoding glycolytic enzymes. In this communication, we extend our analysis of the DNA binding properties of Gcrlp. The DNA-binding domain of Gcrlp binds DNA with high affinity. The apparent dissociation
Assessing the permissiveness of transcriptional activator binding sites
โ Scribed by Steven P. Rowe; Anna K. Mapp
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 2008
- Tongue
- English
- Weight
- 231 KB
- Volume
- 89
- Category
- Article
- ISSN
- 0006-3525
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โฆ Synopsis
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 cellโfiee 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. ยฉ 2008 Wiley Periodicals, Inc. Biopolymers 89: 578โ581, 2008.
This article was originally published online as an accepted preprint. The โPublished Onlineโ date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at [email protected]
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