+検索条件
-Structure paper
タイトル | Structural basis of the histone ubiquitination read-write mechanism of RYBP-PRC1. |
---|---|
ジャーナル・号・ページ | Nat Struct Mol Biol, Year 2024 |
掲載日 | 2024年3月25日 |
![]() | Maria Ciapponi / Elena Karlukova / Sven Schkölziger / Christian Benda / Jürg Müller / ![]() |
PubMed 要旨 | 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 ...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. |
![]() | ![]() ![]() |
手法 | EM (単粒子) |
解像度 | 2.91 - 3.18 Å |
構造データ | EMDB-17796, PDB-8pp6: EMDB-17797, PDB-8pp7: |
化合物 | ![]() ChemComp-ZN: |
由来 |
|
![]() | GENE REGULATION / ncPRC1 / RYBP-PRC1 / nucleosome / H2A / histones / RYBP / Ubiquitin / K119 / ncPRC1 complex / RING1B / BMI1 / heterodimer / E3 ligase |