Regulation of neuronal diversity and fate through protein complexes involved in gene repression and chromatin condensation.

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.

Extra protein memory storage elements with positive feedbacks, in addition to histone modifications, can explain epigenetic switching and memory at the PRC2 target gene FLOWERING LOCUS C (FLC).

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.

PCGF6 links sequence specific target recognition by the MAX/MGA transcription factor complex to PRC1 (polycomb repressive complex 1) -dependent transcriptional silencing of germ cell-specific genes in mouse pluripotent stem cells.

Redistribution of the PRC2 complex in H3.3K27M mutant cells to poised enhancers contributes to the global reduction of H3K27me3 in cells expressing the mutant proteins.

The Polycomb group protein SCML2 contributes to the assembly and gene silencing function of Polycomb Repressive Complex 1 (PRC1) and requires an RNA-binding region to reach chromatin targets.

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

Live-cell single-molecule tracking reveals that hierarchical cooperation within the Polycomb Cbx7 protein between the low-affinity H3K27me3-binding module and the high-affinity DNA-binding cassette targets Polycomb repressive complex 1 to chromatin.