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-Structure paper
Title | Mechanism of histone H2B monoubiquitination by Bre1. |
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Journal, issue, pages | Nat Struct Mol Biol, Vol. 30, Issue 11, Page 1623-1627, Year 2023 |
Publish date | Oct 23, 2023 |
Authors | Fan Zhao / Chad W Hicks / Cynthia Wolberger / |
PubMed Abstract | Monoubiquitination of histone H2B-K120/123 plays several roles in regulating transcription, DNA replication and the DNA damage response. The structure of a nucleosome in complex with the dimeric RING ...Monoubiquitination of histone H2B-K120/123 plays several roles in regulating transcription, DNA replication and the DNA damage response. The structure of a nucleosome in complex with the dimeric RING E3 ligase Bre1 reveals that one RING domain binds to the nucleosome acidic patch, where it can position the E2 ubiquitin conjugating enzyme Rad6, while the other RING domain contacts the DNA. Comparisons with H2A-specific E3 ligases suggest a general mechanism of tuning histone specificity via the non-E2-binding RING domain. |
External links | Nat Struct Mol Biol / PubMed:37872231 |
Methods | EM (single particle) |
Resolution | 3.21 - 3.47 Å |
Structure data | EMDB-41011, PDB-8t3t: EMDB-41015, PDB-8t3w: EMDB-41016, PDB-8t3y: |
Chemicals | ChemComp-ZN: |
Source |
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Keywords | DNA BINDING PROTEIN/Transferase/DNA / H2B ubiquitin E3 ligase / dimer / nucleosome acidic patch binding protein / DNA BINDING PROTEIN-Transferase-DNA complex / H2B ubiquitin |