1. Histone H3K27 Trimethylation Inhibits H3 Binding and Function of SET1-Like H3K4 Methyltransferase Complexes
- Author
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Robert G. Roeder, Seunghee Lee, Soo Kyung Lee, Zhanyun Tang, Tom W. Muir, Dae-Hwan Kim, Beat Fierz, Maya Bar-Dagen, Brian Houck-Loomis, Jae Woon Lee, and Miho Shimada
- Subjects
Transcriptional Activation ,Histone H3 Lysine 4 ,Cell Survival ,Tretinoin ,environment and public health ,Methylation ,Epigenesis, Genetic ,Histones ,Histone H3 ,Multienzyme Complexes ,Histone H2A ,Humans ,Histone code ,Protein Interaction Domains and Motifs ,Histone octamer ,Molecular Biology ,Histone Demethylases ,Binding Sites ,biology ,fungi ,Intracellular Signaling Peptides and Proteins ,Nuclear Proteins ,Histone-Lysine N-Methyltransferase ,Articles ,Cell Biology ,Cell biology ,DNA-Binding Proteins ,HEK293 Cells ,Histone ,Biochemistry ,Histone methyltransferase ,biology.protein ,lipids (amino acids, peptides, and proteins) ,Protein Processing, Post-Translational ,HeLa Cells ,Protein Binding - 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 trimethyl mark facilitates recruitment of SET1-like H3K4 methyltransferase complexes to their target genes by eliciting a novel interaction between histone H3 and two common subunits, WDR5 and RBBP5, of SET1-like complexes. Consistent with this result, H3K27 trimethylation destabilizes interactions of H3 with SET1-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 SET1-like complexes. This provides an important mechanism that directs the anticorrelation between H3K4 and H3K27 trimethylation.
- Published
- 2013
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