RT Journal Article
SR Electronic
T1 Mechanism of histone H2B monoubiquitination by Bre1
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 2023.03.27.534461
DO 10.1101/2023.03.27.534461
A1 Fan Zhao
A1 Chad W. Hicks
A1 Cynthia Wolberger
YR 2023
UL http://biorxiv.org/content/early/2023/03/29/2023.03.27.534461.abstract
AB Monoubiquitination of histone H2BK120/123 plays multiple 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 Rad6 E2, while the other RING domain contacts the DNA. Comparisons with H2A-specific E3 ligases suggests a general mechanism of tuning histone specificity via the non-E2-binding RING domain.Competing Interest StatementThe authors have declared no competing interest.