1. Histone H3K27 Trimethylation Inhibits H3 Binding and Function of SET1-Like H3K4 Methyltransferase Complexes.
- Author
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Dae-Hwan Kim, Zhanyun Tang, Miho Shimada, Fierz, Beat, Houck-Loomis, Brian, Bar-Dagen, Maya, Seunghee Lee, Soo-Kyung Lee, Muir, Tom W., Roeder, Robert G., and Jae W. Lee
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HISTONES , *LYSINE , *CHROMATIN , *GENE expression , *PEPTIDES - Abstract
Trimethylated histone H3 lysine 4 (H3K4) and H3K27 generally mark transcriptionally active and repressive chromatins, respectively. In most cell types, these two modifications are mutually exclusive, and this segregation is crucial for the regulation of gene expression. However, how this anticorrelation is achieved has not been fully understood. Here, we show that removal of the H3K27 trimefhyl mark facilitates recruitment of SETl-like H3K4 methyltransferase complexes to their target genes by eliciting a novel interaction between histone H3 and two common subunits, WDR5 and RBBP5, of SETl-like complexes. Consistent with this result, H3K27 trimethylation destabilizes interactions of H3 with SETl-like complexes and antagonizes their ability to carry out H3K4 trimethylation of peptide (H3 residues 1 to 36), histone octamer, and mononucleosome substrates. Altogether, our studies reveal that H3K27 trimethylation of histone H3 represses a previously unrecognized interaction between H3 and SETl-like complexes. This provides an important mechanism that directs the anticorrelation between H3K4 and H3K27 trimethylation. [ABSTRACT FROM AUTHOR]
- Published
- 2013
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