Nucleosome binding by PRC2 threads H3K27 into its active site via an interaction network set in register by unmodified H3K36.

Two SET-domain containing proteins regulate H3K4me3 by their binding to H3K4me3 through their PHD domain and directly regulate expression of a subset of genes.

Complex structures of Tudor domains of PHF1/19 with H3tK27me3 provide structural basis for preferential recognition of H3tK27me3 over canonical H3K27me3, implicating that H3tK27me3 might be a physiological ligand of PHF1/19.

H3K23me3 is a RNAi-mediated transgenerationally heritable heterochromatin mark in Caenorhabditis elegans.

Post-translational modification of histone H3K36 is not required to suppress cryptic transcription initiation or to include alternative exons in Drosophila; instead it promotes expression of active genes by stimulating polyadenylation.

While SET-2 methylates histone H3K36 during transcription, ASH1 methylates this residue in repressed regions, is important for silencing, and can both positively and negatively influence methylation of histone H3K27.

Loss of Dnmt3a in excitatory neurons disrupts synaptic morphology and behavior, and triggers the expansion of H3K27me3 binding, suggestive of increased polycomb repression.

Bidirectional regulation of the chromatin modification H3K27me3 orchestrates programs of gene expression that underlie postmitotic stages of neuronal maturation.

Epigenetic drift of H3K27me3 is one of the molecular mechanisms that contribute to aging, and stimulation of glycolysis promotes metabolic health and longevity.

Active and repressive chromatin marks, asymmetrically distributed between alleles, distinguish gene bodies subject to epigenetically controlled monoallelic expression on autosomes in human cells.