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- Title
Histone H2A monoubiquitination promotes histone H3 methylation in Polycomb repression.
- Authors
Kalb, Reinhard; Latwiel, Sebastian; Baymaz, H Irem; Jansen, Pascal W T C; Müller, Christoph W; Vermeulen, Michiel; Müller, Jürg
- 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.
- Subjects
HISTONES; UBIQUITINATION; METHYLATION; POLYCOMB group proteins; CHROMATIN
- Publication
Nature Structural & Molecular Biology, 2014, Vol 21, Issue 6, p569
- ISSN
1545-9993
- Publication type
Article
- DOI
10.1038/nsmb.2833