H3K27 methylation and H3S28 phosphorylation-dependent transcriptional regulation by INHAT subunit SET/TAF-I beta

Abstract

Significant progress has been made in understanding the relationship between histone modifications and 'reader' molecules and their effects on transcriptional regulation. A previously identified INHAT complex subunit, SET/TAF-I beta, binds to histones and inhibits histone acetylation. To investigate the binding specificities of SET/TAF-I beta to various histone modifications, we employed modified histone tail peptide array analyses. SET/TAF-I beta strongly recognized PRC2-mediated H3K27me1/2/3; however, the bindings were completely disrupted by H3S28 phosphorylation. We have demonstrated that SET/TAF-I beta is sequentially recruited to the target gene promoter ATF3 after the PRC2 complex via H3K27me recognition and may offer additive effects in the repression of the target gene. (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.