Assessing the permissiveness of transcriptional activator binding sites Export

@article{citeulike:3025276, 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-fiee 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. {\copyright} 2008 Wiley Periodicals, Inc. Biopolymers 89: 578-581, 2008.This article was originally published online as an accepted preprint. The ldquoPublished Onlinerdquo date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com}, address = {Department of Chemistry, University of Michigan, Ann Arbor, MI; Department of Medicinal Chemistry, University of Michigan, Ann Arbor, MI}, author = {Rowe, Steven P. and Mapp, Anna K.}, citeulike-article-id = {3025276}, citeulike-linkout-0 = {http://dx.doi.org/10.1002/bip.20946}, citeulike-linkout-1 = {http://www3.interscience.wiley.com/cgi-bin/abstract/117906882/ABSTRACT}, doi = {10.1002/bip.20946}, journal = {Biopolymers}, keywords = {activator, b-peptides, binding-study, kix, peptides, peptoids, transcription}, number = {7}, pages = {578--581}, posted-at = {2008-07-21 20:43:44}, priority = {2}, title = {Assessing the permissiveness of transcriptional activator binding sites}, url = {http://dx.doi.org/10.1002/bip.20946}, volume = {89}, year = {2008} }

TY - JOUR ID - citeulike:3025276 L3 - citeulike-article-id:3025276 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-fiee 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. © 2008 Wiley Periodicals, Inc. Biopolymers 89: 578-581, 2008.This article was originally published online as an accepted preprint. The ldquoPublished Onlinerdquo date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com IS - 7 JF - Biopolymers AD - Department of Chemistry, University of Michigan, Ann Arbor, MI; Department of Medicinal Chemistry, University of Michigan, Ann Arbor, MI EP - 581 TI - Assessing the permissiveness of transcriptional activator binding sites VL - 89 SP - 578 KW - activator KW - b-peptides KW - binding-study KW - kix KW - peptides KW - peptoids KW - transcription AU - Rowe, Steven AU - Mapp, Anna PY - 2008/// UR - http://dx.doi.org/10.1002/bip.20946 ER -