Structural basis of the histone ubiquitination read-write mechanism of RYBP-PRC1
Nature Structural & Molecular Biology artivle from the Müller lab
25.03.2024
Maria Ciapponi, Elena Karlukova, Sven Schkölziger, Christian Benda & Jürg Müller (2024 March 25) Structural basis of the histone ubiquitination read–write mechanism of RYBP–PRC1. Nature Structural & Molecular Biology https://doi.org/10.1038/s41594-024-01258-x
Abstract cited directly from the article:
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.