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H3K27 methylation and H3S28 phosphorylation‐dependent transcriptional regulation by INHAT subunit SET/TAF‐Iβ
Author(s) -
Kim Ji-Young,
Kim Kee-Beom,
Son Hye-Ju,
Chae Yun-Cheol,
Oh Si-Taek,
Kim Dong-Wook,
Pak Jhang Ho,
Seo Sang-Beom
Publication year - 2012
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2012.06.026
Subject(s) - prc2 , histone , histone h2a , histone h3 , epigenetics , acetylation , histone methylation , ezh2 , histone h4 , histone methyltransferase , histone code , phosphorylation , chemistry , microbiology and biotechnology , biology , genetics , gene , dna methylation , nucleosome , gene expression
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.