| Literature DB >> 22796192 |
Ji-Young Kim1, Kee-Beom Kim, Hye-Ju Son, Yun-Cheol Chae, Si-Taek Oh, Dong-Wook Kim, Jhang Ho Pak, Sang-Beom Seo.
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-Iβ, binds to histones and inhibits histone acetylation. To investigate the binding specificities of SET/TAF-Iβ to various histone modifications, we employed modified histone tail peptide array analyses. SET/TAF-Iβ strongly recognized PRC2-mediated H3K27me1/2/3; however, the bindings were completely disrupted by H3S28 phosphorylation. We have demonstrated that SET/TAF-Iβ 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.Entities:
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Year: 2012 PMID： 22796192 DOI： 10.1016/j.febslet.2012.06.026
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124