Structural basis of specific H2A K13/K15 ubiquitination by RNF168

Velten Horn; Michael Uckelmann; Heyi Zhang; Jelmer Eerland; Ivette Aarsman; Ulric B. le Paige; Chen Davidovich; Titia K. Sixma; Hugo van Ingen

doi:10.1038/s41467-019-09756-z

Nature Communications (Apr 2019)

Structural basis of specific H2A K13/K15 ubiquitination by RNF168

Velten Horn,
Michael Uckelmann,
Heyi Zhang,
Jelmer Eerland,
Ivette Aarsman,
Ulric B. le Paige,
Chen Davidovich,
Titia K. Sixma,
Hugo van Ingen

Affiliations

Velten Horn: Department of Macromolecular Biochemistry, Leiden Institute of Chemistry, Leiden University
Michael Uckelmann: Division of Biochemistry and Oncode Institute, Netherlands Cancer Institute
Heyi Zhang: Department of Macromolecular Biochemistry, Leiden Institute of Chemistry, Leiden University
Jelmer Eerland: Department of Macromolecular Biochemistry, Leiden Institute of Chemistry, Leiden University
Ivette Aarsman: Division of Biochemistry and Oncode Institute, Netherlands Cancer Institute
Ulric B. le Paige: Department of Macromolecular Biochemistry, Leiden Institute of Chemistry, Leiden University
Chen Davidovich: Department of Biochemistry and Molecular Biology, Biomedicine Discovery Institute, Faculty of Medicine, Nursing and Health Sciences, Monash University
Titia K. Sixma: Division of Biochemistry and Oncode Institute, Netherlands Cancer Institute
Hugo van Ingen: Department of Macromolecular Biochemistry, Leiden Institute of Chemistry, Leiden University

DOI: https://doi.org/10.1038/s41467-019-09756-z
Journal volume & issue: Vol. 10, no. 1
pp. 1 – 12

Abstract

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Ubiquitination of histone H2A can occur on distinct lysine residues, but how each site is recognised by the specific E3 ligase remains poorly understood. Here the authors demonstrate that the E3 ligase RNF168 binds the acidic patch on the nucleosome surface, directing the E2 to the target lysine K13/K15.

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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