| First Author | Chen WY | Year | 2013 |
| Journal | Genes Dev | Volume | 27 |
| Issue | 14 | Pages | 1596-609 |
| PubMed ID | 23873942 | Mgi Jnum | J:199361 |
| Mgi Id | MGI:5502465 | Doi | 10.1101/gad.216192.113 |
| Citation | Chen WY, et al. (2013) A TAF4 coactivator function for E proteins that involves enhanced TFIID binding. Genes Dev 27(14):1596-609 |
| abstractText | The multisubunit TFIID plays a direct role in transcription initiation by binding to core promoter elements and directing preinitiation complex assembly. Although TFIID may also function as a coactivator through direct interactions with promoter-bound activators, mechanistic aspects of this poorly defined function remain unclear. Here, biochemical studies show a direct TFIID-E-protein interaction that (1) is mediated through interaction of a novel E-protein activation domain (activation domain 3 [AD3]) with the TAF homology (TAFH) domain of TAF4, (2) is critical for activation of a natural target gene by an E protein, and (3) mechanistically acts by enhancing TFIID binding to the core promoter. Complementary assays establish a gene-specific role for the TAFH domain in TFIID recruitment and activation of a large subset of genes in vivo. These results firmly establish TAF4 as a bona fide E-protein coactivator as well as a mechanism involving facilitated TFIID binding through direct interaction with an E-protein activation domain. |
