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

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.

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Autores principales:	Chiara Balbo Pogliano, Marco Gatti, Peter Rüthemann, Zuzana Garajovà, Lorenza Penengo, Hanspeter Naegeli
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/9d9aa0b04f364233b240cfb6b9393ea7
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spelling	oai:doaj.org-article:9d9aa0b04f364233b240cfb6b9393ea72021-12-02T14:40:59ZASH1L histone methyltransferase regulates the handoff between damage recognition factors in global-genome nucleotide excision repair10.1038/s41467-017-01080-82041-1723https://doaj.org/article/9d9aa0b04f364233b240cfb6b9393ea72017-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-01080-8https://doaj.org/toc/2041-1723UV-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.Chiara Balbo PoglianoMarco GattiPeter RüthemannZuzana GarajovàLorenza PenengoHanspeter NaegeliNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-13 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Chiara Balbo Pogliano Marco Gatti Peter Rüthemann Zuzana Garajovà Lorenza Penengo Hanspeter Naegeli ASH1L histone methyltransferase regulates the handoff between damage recognition factors in global-genome nucleotide excision repair
description	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.
format	article
author	Chiara Balbo Pogliano Marco Gatti Peter Rüthemann Zuzana Garajovà Lorenza Penengo Hanspeter Naegeli
author_facet	Chiara Balbo Pogliano Marco Gatti Peter Rüthemann Zuzana Garajovà Lorenza Penengo Hanspeter Naegeli
author_sort	Chiara Balbo Pogliano
title	ASH1L histone methyltransferase regulates the handoff between damage recognition factors in global-genome nucleotide excision repair
title_short	ASH1L histone methyltransferase regulates the handoff between damage recognition factors in global-genome nucleotide excision repair
title_full	ASH1L histone methyltransferase regulates the handoff between damage recognition factors in global-genome nucleotide excision repair
title_fullStr	ASH1L histone methyltransferase regulates the handoff between damage recognition factors in global-genome nucleotide excision repair
title_full_unstemmed	ASH1L histone methyltransferase regulates the handoff between damage recognition factors in global-genome nucleotide excision repair
title_sort	ash1l histone methyltransferase regulates the handoff between damage recognition factors in global-genome nucleotide excision repair
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/9d9aa0b04f364233b240cfb6b9393ea7
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ASH1L histone methyltransferase regulates the handoff between damage recognition factors in global-genome nucleotide excision repair

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