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Mechanism of histone H2B monoubiquitination by Bre1

View ORCID ProfileFan Zhao, View ORCID ProfileChad W. Hicks, View ORCID ProfileCynthia Wolberger
doi: https://doi.org/10.1101/2023.03.27.534461
Fan Zhao
Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA
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Chad W. Hicks
Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA
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Cynthia Wolberger
Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA
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  • For correspondence: cwolberg@jhmi.edu
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Abstract

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 Statement

The authors have declared no competing interest.

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The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY 4.0 International license.
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Posted March 29, 2023.
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Mechanism of histone H2B monoubiquitination by Bre1
Fan Zhao, Chad W. Hicks, Cynthia Wolberger
bioRxiv 2023.03.27.534461; doi: https://doi.org/10.1101/2023.03.27.534461
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Mechanism of histone H2B monoubiquitination by Bre1
Fan Zhao, Chad W. Hicks, Cynthia Wolberger
bioRxiv 2023.03.27.534461; doi: https://doi.org/10.1101/2023.03.27.534461

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