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

Martina Foglizzo; Adam J. Middleton; Abigail E. Burgess; Jennifer M. Crowther; Renwick C. J. Dobson; James M. Murphy; Catherine L. Day; Peter D. Mace

doi:10.1038/s41467-018-06186-1

Nature Communications (Sep 2018)

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

Martina Foglizzo,
Adam J. Middleton,
Abigail E. Burgess,
Jennifer M. Crowther,
Renwick C. J. Dobson,
James M. Murphy,
Catherine L. Day,
Peter D. Mace

Affiliations

Martina Foglizzo: Biochemistry Department, School of Biomedical Sciences, University of Otago
Adam J. Middleton: Biochemistry Department, School of Biomedical Sciences, University of Otago
Abigail E. Burgess: Biochemistry Department, School of Biomedical Sciences, University of Otago
Jennifer M. Crowther: Biomolecular Interaction Centre, School of Biological Sciences, University of Canterbury
Renwick C. J. Dobson: Biomolecular Interaction Centre, School of Biological Sciences, University of Canterbury
James M. Murphy: The Walter and Eliza Hall Institute of Medical Research
Catherine L. Day: Biochemistry Department, School of Biomedical Sciences, University of Otago
Peter D. Mace: Biochemistry Department, School of Biomedical Sciences, University of Otago

DOI: https://doi.org/10.1038/s41467-018-06186-1
Journal volume & issue: Vol. 9, no. 1
pp. 1 – 15

Abstract

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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.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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