Mechanism of histone H2B monoubiquitination by Bre1

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 pos...

Descripción completa

Detalles Bibliográficos
Autores principales: Zhao, Fan, Hicks, Chad W., Wolberger, Cynthia
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Cold Spring Harbor Laboratory 2023
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10081246/
https://www.ncbi.nlm.nih.gov/pubmed/37034759
http://dx.doi.org/10.1101/2023.03.27.534461
_version_ 1785021072124411904
author Zhao, Fan
Hicks, Chad W.
Wolberger, Cynthia
author_facet Zhao, Fan
Hicks, Chad W.
Wolberger, Cynthia
author_sort Zhao, Fan
collection PubMed
description 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.
format Online
Article
Text
id pubmed-10081246
institution National Center for Biotechnology Information
language English
publishDate 2023
publisher Cold Spring Harbor Laboratory
record_format MEDLINE/PubMed
spelling pubmed-100812462023-04-08 Mechanism of histone H2B monoubiquitination by Bre1 Zhao, Fan Hicks, Chad W. Wolberger, Cynthia bioRxiv Article 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. Cold Spring Harbor Laboratory 2023-08-28 /pmc/articles/PMC10081246/ /pubmed/37034759 http://dx.doi.org/10.1101/2023.03.27.534461 Text en https://creativecommons.org/licenses/by/4.0/This work is licensed under a Creative Commons Attribution 4.0 International License (https://creativecommons.org/licenses/by/4.0/) , which allows reusers to distribute, remix, adapt, and build upon the material in any medium or format, so long as attribution is given to the creator. The license allows for commercial use.
spellingShingle Article
Zhao, Fan
Hicks, Chad W.
Wolberger, Cynthia
Mechanism of histone H2B monoubiquitination by Bre1
title Mechanism of histone H2B monoubiquitination by Bre1
title_full Mechanism of histone H2B monoubiquitination by Bre1
title_fullStr Mechanism of histone H2B monoubiquitination by Bre1
title_full_unstemmed Mechanism of histone H2B monoubiquitination by Bre1
title_short Mechanism of histone H2B monoubiquitination by Bre1
title_sort mechanism of histone h2b monoubiquitination by bre1
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10081246/
https://www.ncbi.nlm.nih.gov/pubmed/37034759
http://dx.doi.org/10.1101/2023.03.27.534461
work_keys_str_mv AT zhaofan mechanismofhistoneh2bmonoubiquitinationbybre1
AT hickschadw mechanismofhistoneh2bmonoubiquitinationbybre1
AT wolbergercynthia mechanismofhistoneh2bmonoubiquitinationbybre1

Ejemplares similares