Mechanism of histone H2B monoubiquitination by Bre1

Fan Zhao; Chad W. Hicks; Cynthia Wolberger

doi:10.1038/s41594-023-01137-x

Mechanism of histone H2B monoubiquitination by Bre1

Fan Zhao, Chad W. Hicks, Cynthia Wolberger

School of Medicine

Research output: Contribution to journal › Article › peer-review

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 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.

Original language	English (US)
Pages (from-to)	1623-1627
Number of pages	5
Journal	Nature Structural and Molecular Biology
Volume	30
Issue number	11
DOIs	https://doi.org/10.1038/s41594-023-01137-x
State	Published - Nov 2023

ASJC Scopus subject areas

Structural Biology
Molecular Biology

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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 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.",

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Mechanism of histone H2B monoubiquitination by Bre1

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