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TitleStructural basis of the histone ubiquitination read-write mechanism of RYBP-PRC1.
Journal, issue, pagesNat Struct Mol Biol, Year 2024
Publish dateMar 25, 2024
AuthorsMaria Ciapponi / Elena Karlukova / Sven Schkölziger / Christian Benda / Jürg Müller /
PubMed AbstractHistone 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 ...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.
External linksNat Struct Mol Biol / PubMed:38528151
MethodsEM (single particle)
Resolution2.91 - 3.18 Å
Structure data

17796

8pp6

EMDB-17796, PDB-8pp6:
human RYBP-PRC1 bound to H2AK118ub1 nucleosome
Method: EM (single particle) / Resolution: 3.18 Å

17797

8pp7

EMDB-17797, PDB-8pp7:
human RYBP-PRC1 bound to mononucleosome
Method: EM (single particle) / Resolution: 2.91 Å

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • homo sapiens (human)
  • drosophila melanogaster (fruit fly)
KeywordsGENE REGULATION / ncPRC1 / RYBP-PRC1 / nucleosome / H2A / histones / RYBP / Ubiquitin / K119 / ncPRC1 complex / RING1B / BMI1 / heterodimer / E3 ligase

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