Electron microscopy has been used to produce the first three-dimensional image of the PRC2 gene-silencing complex.

Biochemical and mutagenesis analysis reveal the long-anticipated RNA-binding elements of Polycomb Repressive Complex 2 (PRC2), an important chromatin modifier, allowing construction of separation-of-function mutants of PRC2 defective in RNA binding but retaining histone-modifying activity.

The PRC2 Polycomb complex made in the mouse oocyte prevents transcriptional inactivation of the maternal X-chromosome in the early embryo.

The E3 ubiquitin ligase activity of polycomb repressive complex 1 is stimulated by RYBP to support a histone modification-dependent communication between polycomb repressive complexes in mice.

Stem-cell-specific transcriptional repressors fine-tune levels of stemness gene transcripts in asymmetrically dividing neural stem cells by depositing low levels of repressive histone marks at these loci allowing progeny to rapidly initiate differentiation.

Heat shock induces relocalization of epigenetic modifiers to the nucleolus, which acts as a dedicated protein quality control center that is indispensable for recovery of epigenetic regulators and epigenetic modifications.

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.

Histone deacetylase 2 (HDAC2) and polycomb repressive complex 2 (PRC2) control endothelial gene expression for BBB development and prevented Wnt/β-catenin target genes from being expressed in adult CNS ECs.

Characterization of Drosophila female germ cell differentiation shows that nurse cells initiate Polycomb silencing by regulating Pcl and Scm levels to alter the biochemical properties of the PRC2 H3K27 methylase.

A protein that can recognize regions of DNA with a high proportion of unmethylated CpG dinucleotides, and then recruit polycomb group proteins to these CpG islands, has been identified.