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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引用

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

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

要旨

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.