8pp6: Difference between revisions
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/ | [https://www.uniprot.org/uniprot/H3_DROME H3_DROME] | ||
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== 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<ref>PMID:38528151</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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<div class="pdbe-citations 8pp6" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Latest revision as of 06:13, 31 July 2024
human RYBP-PRC1 bound to H2AK118ub1 nucleosome
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