Abstract
Coregulator Codes of Transcriptional Regulation by Nuclear Receptors
Highlights
Nuclear Receptor Coactivators A diverse group of proteins have emerged as potential coactivators for nuclear receptors
As the number of potential coregulators clearly exceeds the capacity for direct interaction by a single receptor, the most plausible hypothesis is that transcriptional activation by nuclear receptors involves the actions of multiple factors
This concept was further supported by the subsequent finding that the mammalian Gcn5 orthologues, including p/CAF, CREB-binding protein (CBP), adenovirus E1A-binding protein p300, and TAFII250, each possess intrinsic histone acetyltransferase (HAT) activity [7,8,9,10,11]
Summary
The discovery that a mammalian histone deacetylase (HDAC) was a homologue of the yeast corepressor, RPD3 [13], gave rise to the hypothesis that regulated activation events might involve the exchange of complexes containing histone deacetylase functions with those containing histone acetyltransferase activity (Fig. 1) It appears that in most cases the acetyltransferases are not directly recruited to nuclear receptors but associate with other coactivators that exhibit higher affinity for the liganded receptor. The TRAP1⁄7DRIP1⁄7ARC complex consists of more than a dozen polypeptides, a subset of which appears to constitute modules that are components of other activator complexes, including CRSP, NAT, SMCC, and mouse mediator, and have no known enzymatic functions [29, 31, 34] These factors may function to recruit RNA polymerase II holoenzyme to ligand-bound nuclear receptors. Recruitment of complexes such as the TRAP1⁄7DRIP1⁄7ARC complex may function to enhance RNA polymerase II recruitment to the promoter
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