Histone H2A monoubiquitination promotes histone H3 methylation in Polycomb repression — C. Müller, Vermeulen, and J. Müller labs (2014)
Sunday, May 18, 2014
Reinhard Kalb, Sebastian Latwiel, H Irem Baymaz, Pascal W T C Jansen, Christoph W Müller, Michiel Vermeulen & Jürg Müller
A key step in gene repression by Polycomb is trimethylation of histone H3 K27 by PCR2 to form H3K27me3. H3K27me3 provides a binding surface for PRC1. We show that monoubiquitination of histone H2A by PRC1-type complexes to form H2Aub creates a binding site for Jarid2-Aebp2-containing PRC2 and promotes H3K27 trimethylation on H2Aub nucleosomes. Jarid2, Aebp2 and H2Aub thus constitute components of a positive feedback loop establishing H3K27me3 chromatin domains.
Nature Structural & Molecular Biology (2014) 21:569-571 doi: 10.1038/nsmb.2833