Multivalent binding of p53 to the STAGA complex mediates coactivator recruitment after UV damage.

ABSTRACT: The recruitment of transcriptional coactivators, including histone modifying enzymes, is an important step in transcription regulation. A typical activator is thought to interact with several cofactors, presumably in a sequential manner. The common use of several cofactors raises the question of how activators achieve both cofactor selectivity and diversity. Human STAGA is a multiprotein complex with the acetyltransferase GCN5L as the catalytic subunit. Here, we first show, through RNA interference-mediated knock-down and chromatin immunoprecipitation assays, that GCN5 plays a role in p53-dependent gene activation. We then employ p53 mutagenesis, in vitro binding, protein-protein cross-linking, and chromatin immunoprecipitation assays to establish a novel role for the second p53 activation

SUBMITTER: Gamper AM 

PROVIDER: S-EPMC2293101 | biostudies-literature | 2008 Apr

REPOSITORIES: biostudies-literature