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TitleMechanism of histone H2B monoubiquitination by Bre1.
Journal, issue, pagesNat Struct Mol Biol, Vol. 30, Issue 11, Page 1623-1627, Year 2023
Publish dateOct 23, 2023
AuthorsFan Zhao / Chad W Hicks / Cynthia Wolberger /
PubMed AbstractMonoubiquitination 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 linksNat Struct Mol Biol / PubMed:37872231
MethodsEM (single particle)
Resolution3.21 - 3.47 Å
Structure data

41011

8t3t

EMDB-41011, PDB-8t3t:
Structure of Bre1-nucleosome complex - state3
Method: EM (single particle) / Resolution: 3.21 Å

41015

8t3w

EMDB-41015, PDB-8t3w:
Structure of Bre1-nucleosome complex - state2
Method: EM (single particle) / Resolution: 3.25 Å

41016

8t3y

EMDB-41016, PDB-8t3y:
Structure of Bre1-nucleosome complex - state1
Method: EM (single particle) / Resolution: 3.47 Å

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • saccharomyces cerevisiae (brewer's yeast)
  • xenopus laevis (African clawed frog)
  • synthetic construct (others)
  • saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
KeywordsDNA BINDING PROTEIN/Transferase/DNA / H2B ubiquitin E3 ligase / dimer / nucleosome acidic patch binding protein / DNA BINDING PROTEIN-Transferase-DNA complex / H2B ubiquitin

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