A TAF4 coactivator function for E proteins that involves enhanced TFIID binding

ABSTRACT: 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 (i) is mediated through interaction of a novel E protein activation domain (AD3) with the TAF homology (TAFH) domain of TAF4, (ii) is critical for activation of a natural target gene by an E protein and (iii) 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 gene activation in

ORGANISM(S): Mus musculus

SUBMITTER: Huimin Geng 

PROVIDER: E-GEOD-46807 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress