8pp6

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Current revision (06:13, 31 July 2024) (edit) (undo)
 
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== Function ==
== Function ==
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[https://www.uniprot.org/uniprot/A0A7L0PXJ3_9AVES A0A7L0PXJ3_9AVES] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.[ARBA:ARBA00002001]
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[https://www.uniprot.org/uniprot/H3_DROME H3_DROME]
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== Publication Abstract from PubMed ==
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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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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>
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From MEDLINE&reg;/PubMed&reg;, 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>
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== References ==
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<references/>
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</StructureSection>
</StructureSection>

Current revision

human RYBP-PRC1 bound to H2AK118ub1 nucleosome

PDB ID 8pp6

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