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Published on: January 26, 2018
Histone H2A monoubiquitination promotes histone H3 methylation in Polycomb repression
Reinhard Kalb1, Sebastian Latwiel2, H Irem Baymaz3
1Max Planck Institute of Biochemistry, Laboratory of Chromatin and Chromosome Biology, Martinsried, Germany.
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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