Journal Article

Histone H2A monoubiquitination promotes histone H3 methylation in Polycomb repression

Baymaz, H Irem, Müller, Christoph W, Jansen, Pascal W T C, Müller, Jürg, Latwiel, Sebastian, Vermeulen, Michiel, Kalb, Reinhard

2014

Overview

PRC2 promotes methylation of H3K27, a modification that recruits PRC1, which in turn deposits H2A ubiquitin marks. Müller and colleagues use biochemistry approaches to show that H2Aub recruits Jarid–Aebp2–containing PRC2 to promote H3K27 trimethylation on H2Aub nucleosomes, thus forming a positive feedback loop to establish repressed chromatin domains. 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.

• Publisher: Nature Publishing Group US,Nature Publishing Group
• Subject: 631/208/200 / 631/337/176 / 631/337/458/582 / 631/535 / Animals / Binding sites / Biochemistry / Biological Microscopy / brief-communication / DNA methylation / Drosophila - genetics / Epigenetic Repression / Gene expression / Genetic aspects / Genetic research / Histones / Histones - metabolism / Life Sciences / Membrane Biology / Methylation / Polycomb-Group Proteins - genetics / Properties / Protein Structure / Proteins / Ubiquitin-proteasome system / Ubiquitination