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Updated: Jun 29, 2025

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones
Published on: July 25, 2019
Structural basis of the histone ubiquitination read-write mechanism of RYBP-PRC1
Maria Ciapponi1, Elena Karlukova1, Sven Schkölziger1
1Laboratory of Chromatin Biology, Max-Planck Institute of Biochemistry, Martinsried, Germany.
Abstract:
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.
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