8pp6
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human RYBP-PRC1 bound to H2AK118ub1 nucleosome
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Structural highlights
FunctionPublication Abstract from PubMedHistone 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
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This page was last modified 06:13, 31 July 2024.