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. 2014 Jun;21(6):569-71.
doi: 10.1038/nsmb.2833. Epub 2014 May 18.

Histone H2A monoubiquitination promotes histone H3 methylation in Polycomb repression

Reinhard Kalb  1 , Sebastian Latwiel  2 , H Irem Baymaz  3 , Pascal W T C Jansen  4 , Christoph W Müller  5 , Michiel Vermeulen  4 , Jürg Müller  1
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Histone H2A monoubiquitination promotes histone H3 methylation in Polycomb repression

Reinhard Kalb et al. Nat Struct Mol Biol. 2014 Jun.

Abstract

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.

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