Histone H2A monoubiquitination promotes histone H3 methylation in Polycomb 
repression

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

doi:10.1038/nsmb.2833

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Histone H2A monoubiquitination promotes histone H3 methylation in Polycomb repression

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Kalb, Reinhard
Müller, Jürg / Chromatin Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Müller, Jürg
Müller, Jürg / Chromatin Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Citation

Kalb, R., Latwiel, S., Baymaz, H. I., Jansen, P. W. T. C., Müller, C. W., Vermeulen, M., et al. (2014). Histone H2A monoubiquitination promotes histone H3 methylation in Polycomb repression. NATURE STRUCTURAL & MOLECULAR BIOLOGY, 21(6), 569-571. doi:10.1038/nsmb.2833.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0019-DBED-A

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.