Cryo-EM structures of the XPF-ERCC1 endonuclease reveal how DNA-junction engagement disrupts an auto-inhibited conformation

The endonuclease XPF-ERCC1 is a key component of the repair machinery to process both intra-strand and inter-strand DNA crosslinks. Here the authors present the cryo-EM structures of DNA-free and DNA-bound human XPF-ERCC1 and find that DNA-free XPF-ERCC1 adopts an auto-inhibited conformation, which...

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Autores principales:	Morgan Jones, Fabienne Beuron, Aaron Borg, Andrea Nans, Christopher P. Earl, David C. Briggs, Ambrosius P. Snijders, Maureen Bowles, Edward P. Morris, Mark Linch, Neil Q. McDonald
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/92077ba79c5f4633a25574477d6776b9
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spelling	oai:doaj.org-article:92077ba79c5f4633a25574477d6776b92021-12-02T14:40:51ZCryo-EM structures of the XPF-ERCC1 endonuclease reveal how DNA-junction engagement disrupts an auto-inhibited conformation10.1038/s41467-020-14856-22041-1723https://doaj.org/article/92077ba79c5f4633a25574477d6776b92020-02-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-14856-2https://doaj.org/toc/2041-1723The endonuclease XPF-ERCC1 is a key component of the repair machinery to process both intra-strand and inter-strand DNA crosslinks. Here the authors present the cryo-EM structures of DNA-free and DNA-bound human XPF-ERCC1 and find that DNA-free XPF-ERCC1 adopts an auto-inhibited conformation, which is opened up upon DNA binding and they also characterise the biochemical properties of patient-derived XPF-ERCC1 mutations.Morgan JonesFabienne BeuronAaron BorgAndrea NansChristopher P. EarlDavid C. BriggsAmbrosius P. SnijdersMaureen BowlesEdward P. MorrisMark LinchNeil Q. McDonaldNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-14 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Morgan Jones Fabienne Beuron Aaron Borg Andrea Nans Christopher P. Earl David C. Briggs Ambrosius P. Snijders Maureen Bowles Edward P. Morris Mark Linch Neil Q. McDonald Cryo-EM structures of the XPF-ERCC1 endonuclease reveal how DNA-junction engagement disrupts an auto-inhibited conformation
description	The endonuclease XPF-ERCC1 is a key component of the repair machinery to process both intra-strand and inter-strand DNA crosslinks. Here the authors present the cryo-EM structures of DNA-free and DNA-bound human XPF-ERCC1 and find that DNA-free XPF-ERCC1 adopts an auto-inhibited conformation, which is opened up upon DNA binding and they also characterise the biochemical properties of patient-derived XPF-ERCC1 mutations.
format	article
author	Morgan Jones Fabienne Beuron Aaron Borg Andrea Nans Christopher P. Earl David C. Briggs Ambrosius P. Snijders Maureen Bowles Edward P. Morris Mark Linch Neil Q. McDonald
author_facet	Morgan Jones Fabienne Beuron Aaron Borg Andrea Nans Christopher P. Earl David C. Briggs Ambrosius P. Snijders Maureen Bowles Edward P. Morris Mark Linch Neil Q. McDonald
author_sort	Morgan Jones
title	Cryo-EM structures of the XPF-ERCC1 endonuclease reveal how DNA-junction engagement disrupts an auto-inhibited conformation
title_short	Cryo-EM structures of the XPF-ERCC1 endonuclease reveal how DNA-junction engagement disrupts an auto-inhibited conformation
title_full	Cryo-EM structures of the XPF-ERCC1 endonuclease reveal how DNA-junction engagement disrupts an auto-inhibited conformation
title_fullStr	Cryo-EM structures of the XPF-ERCC1 endonuclease reveal how DNA-junction engagement disrupts an auto-inhibited conformation
title_full_unstemmed	Cryo-EM structures of the XPF-ERCC1 endonuclease reveal how DNA-junction engagement disrupts an auto-inhibited conformation
title_sort	cryo-em structures of the xpf-ercc1 endonuclease reveal how dna-junction engagement disrupts an auto-inhibited conformation
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/92077ba79c5f4633a25574477d6776b9
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Cryo-EM structures of the XPF-ERCC1 endonuclease reveal how DNA-junction engagement disrupts an auto-inhibited conformation

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