Histone H2A monoubiquitination promotes histone H3 methylation in Polycomb repression.
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.
Max Planck Institute of Biochemistry, Laboratory of Chromatin and Chromosome Biology, Martinsried, Germany.
Reinhard
R
Kalb
1] European Molecular Biology Laboratory, Structural and Computational Biology Unit, Heidelberg, Germany. [2].
Sebastian
S
Latwiel
1] Molecular Cancer Research and Cancer Genomics Netherlands, University Medical Center Utrecht, Utrecht, The Netherlands. [2].
H Irem
HI
Baymaz
Molecular Cancer Research and Cancer Genomics Netherlands, University Medical Center Utrecht, Utrecht, The Netherlands.
Pascal W T C
PW
Jansen
European Molecular Biology Laboratory, Structural and Computational Biology Unit, Heidelberg, Germany.
Christoph W
CW
Müller
Molecular Cancer Research and Cancer Genomics Netherlands, University Medical Center Utrecht, Utrecht, The Netherlands.
Michiel
M
Vermeulen
Max Planck Institute of Biochemistry, Laboratory of Chromatin and Chromosome Biology, Martinsried, Germany.
Jürg
J
Müller
D000818:Animals; D004330:Drosophila / Q000235:genetics*; D063185:Epigenetic Repression; D006657:Histones / Q000378:metabolism*; D008745:Methylation; D063146:Polycomb-Group Proteins / Q000235:genetics*; D054875:Ubiquitination
D006657:Histones; D063146:Polycomb-Group Proteins