ASH1L histone methyltransferase regulates the handoff between damage recognition factors in global-genome nucleotide excision repair

Chiara Balbo Pogliano; Marco Gatti; Peter Rüthemann; Zuzana Garajovà; Lorenza Penengo; Hanspeter Naegeli

doi:10.1038/s41467-017-01080-8

Nature Communications (Nov 2017)

ASH1L histone methyltransferase regulates the handoff between damage recognition factors in global-genome nucleotide excision repair

Chiara Balbo Pogliano,
Marco Gatti,
Peter Rüthemann,
Zuzana Garajovà,
Lorenza Penengo,
Hanspeter Naegeli

Affiliations

Chiara Balbo Pogliano: Institute of Pharmacology and Toxicology, University of Zurich-Vetsuisse
Marco Gatti: Department of Molecular Mechanisms of Disease, University of Zurich
Peter Rüthemann: Institute of Pharmacology and Toxicology, University of Zurich-Vetsuisse
Zuzana Garajovà: Institute of Pharmacology and Toxicology, University of Zurich-Vetsuisse
Lorenza Penengo: Institute of Molecular Cancer Research, University of Zurich
Hanspeter Naegeli: Institute of Pharmacology and Toxicology, University of Zurich-Vetsuisse

DOI: https://doi.org/10.1038/s41467-017-01080-8
Journal volume & issue: Vol. 8, no. 1
pp. 1 – 13

Abstract

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UV-induced mutagenic cyclobutane pyrimidine dimers on nucleosomal DNA are sensed by the damage recognition factors DDB2 and XPC via an unknown mechanism. Here, the authors show that the histone methyltransferase ASH1L regulates the DDB2 to XPC handoff by methylating Lys-4 of histone H3.

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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