Structural highlights
Function
H3_DROME
Publication Abstract from PubMed
Histone H2A monoubiquitination (H2Aub1) by the PRC1 subunit RING1B entails a positive feedback loop, mediated by the RING1B-interacting protein RYBP. We uncover that human RYBP-PRC1 binds unmodified nucleosomes via RING1B but H2Aub1-modified nucleosomes via RYBP. RYBP interactions with both ubiquitin and the nucleosome acidic patch create the high binding affinity that favors RYBP- over RING1B-directed PRC1 binding to H2Aub1-modified nucleosomes; this enables RING1B to monoubiquitinate H2A in neighboring unmodified nucleosomes.
Structural basis of the histone ubiquitination read-write mechanism of RYBP-PRC1.,Ciapponi M, Karlukova E, Schkolziger S, Benda C, Muller J Nat Struct Mol Biol. 2024 Jul;31(7):1023-1027. doi: 10.1038/s41594-024-01258-x. , Epub 2024 Mar 25. PMID:38528151[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ciapponi M, Karlukova E, Schkölziger S, Benda C, Müller J. Structural basis of the histone ubiquitination read-write mechanism of RYBP-PRC1. Nat Struct Mol Biol. 2024 Jul;31(7):1023-1027. PMID:38528151 doi:10.1038/s41594-024-01258-x
