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Nat Struct Mol Biol. 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.

Author information

1
Max Planck Institute of Biochemistry, Laboratory of Chromatin and Chromosome Biology, Martinsried, Germany.
2
1] European Molecular Biology Laboratory, Structural and Computational Biology Unit, Heidelberg, Germany. [2].
3
1] Molecular Cancer Research and Cancer Genomics Netherlands, University Medical Center Utrecht, Utrecht, The Netherlands. [2].
4
Molecular Cancer Research and Cancer Genomics Netherlands, University Medical Center Utrecht, Utrecht, The Netherlands.
5
European Molecular Biology Laboratory, Structural and Computational Biology Unit, Heidelberg, 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.

PMID:
24837194
DOI:
10.1038/nsmb.2833
[Indexed for MEDLINE]

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