A bidentate Polycomb Repressive-Deubiquitinase complex is required for efficient activity on nucleosomes

The Polycomb Repressive-Deubiquitinase (PR-DUB) complex is responsible for the removal of the ubiquitin epigenetic modification from Histone 2A. Here the authors describe the structure of the Drosophila PR-DUB complex, providing new insight into its regulation and how cancer-associated mutations dis...

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Autores principales: Martina Foglizzo, Adam J. Middleton, Abigail E. Burgess, Jennifer M. Crowther, Renwick C. J. Dobson, James M. Murphy, Catherine L. Day, Peter D. Mace
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Lenguaje:EN
Publicado: Nature Portfolio 2018
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Acceso en línea:https://doaj.org/article/5fe6531411b6437bb98f283f88b4a26c
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spelling oai:doaj.org-article:5fe6531411b6437bb98f283f88b4a26c2021-12-02T16:56:57ZA bidentate Polycomb Repressive-Deubiquitinase complex is required for efficient activity on nucleosomes10.1038/s41467-018-06186-12041-1723https://doaj.org/article/5fe6531411b6437bb98f283f88b4a26c2018-09-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-06186-1https://doaj.org/toc/2041-1723The Polycomb Repressive-Deubiquitinase (PR-DUB) complex is responsible for the removal of the ubiquitin epigenetic modification from Histone 2A. Here the authors describe the structure of the Drosophila PR-DUB complex, providing new insight into its regulation and how cancer-associated mutations disrupt PR-DUB activity.Martina FoglizzoAdam J. MiddletonAbigail E. BurgessJennifer M. CrowtherRenwick C. J. DobsonJames M. MurphyCatherine L. DayPeter D. MaceNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-15 (2018)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Martina Foglizzo
Adam J. Middleton
Abigail E. Burgess
Jennifer M. Crowther
Renwick C. J. Dobson
James M. Murphy
Catherine L. Day
Peter D. Mace
A bidentate Polycomb Repressive-Deubiquitinase complex is required for efficient activity on nucleosomes
description The Polycomb Repressive-Deubiquitinase (PR-DUB) complex is responsible for the removal of the ubiquitin epigenetic modification from Histone 2A. Here the authors describe the structure of the Drosophila PR-DUB complex, providing new insight into its regulation and how cancer-associated mutations disrupt PR-DUB activity.
format article
author Martina Foglizzo
Adam J. Middleton
Abigail E. Burgess
Jennifer M. Crowther
Renwick C. J. Dobson
James M. Murphy
Catherine L. Day
Peter D. Mace
author_facet Martina Foglizzo
Adam J. Middleton
Abigail E. Burgess
Jennifer M. Crowther
Renwick C. J. Dobson
James M. Murphy
Catherine L. Day
Peter D. Mace
author_sort Martina Foglizzo
title A bidentate Polycomb Repressive-Deubiquitinase complex is required for efficient activity on nucleosomes
title_short A bidentate Polycomb Repressive-Deubiquitinase complex is required for efficient activity on nucleosomes
title_full A bidentate Polycomb Repressive-Deubiquitinase complex is required for efficient activity on nucleosomes
title_fullStr A bidentate Polycomb Repressive-Deubiquitinase complex is required for efficient activity on nucleosomes
title_full_unstemmed A bidentate Polycomb Repressive-Deubiquitinase complex is required for efficient activity on nucleosomes
title_sort bidentate polycomb repressive-deubiquitinase complex is required for efficient activity on nucleosomes
publisher Nature Portfolio
publishDate 2018
url https://doaj.org/article/5fe6531411b6437bb98f283f88b4a26c
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