The Ku-binding motif is a conserved module for recruitment and stimulation of non-homologous end-joining proteins

Werner syndrome is a progeroid disease characterised by genetic instability due to mutations to the WRN helicase/exonuclease. Here the authors define a novel Ku binding motif (KBM) and show that two such motifs facilitate the involvement of WRN in DNA double-strand break repair.

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Autores principales:	Gabrielle J. Grundy, Stuart L. Rulten, Raquel Arribas-Bosacoma, Kathryn Davidson, Zuzanna Kozik, Antony W. Oliver, Laurence H. Pearl, Keith W. Caldecott
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2016
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/f76baaf3e5cb4dc5b122d503eff9616e
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spelling	oai:doaj.org-article:f76baaf3e5cb4dc5b122d503eff9616e2021-12-02T15:34:57ZThe Ku-binding motif is a conserved module for recruitment and stimulation of non-homologous end-joining proteins10.1038/ncomms112422041-1723https://doaj.org/article/f76baaf3e5cb4dc5b122d503eff9616e2016-04-01T00:00:00Zhttps://doi.org/10.1038/ncomms11242https://doaj.org/toc/2041-1723Werner syndrome is a progeroid disease characterised by genetic instability due to mutations to the WRN helicase/exonuclease. Here the authors define a novel Ku binding motif (KBM) and show that two such motifs facilitate the involvement of WRN in DNA double-strand break repair.Gabrielle J. GrundyStuart L. RultenRaquel Arribas-BosacomaKathryn DavidsonZuzanna KozikAntony W. OliverLaurence H. PearlKeith W. CaldecottNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-11 (2016)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Gabrielle J. Grundy Stuart L. Rulten Raquel Arribas-Bosacoma Kathryn Davidson Zuzanna Kozik Antony W. Oliver Laurence H. Pearl Keith W. Caldecott The Ku-binding motif is a conserved module for recruitment and stimulation of non-homologous end-joining proteins
description	Werner syndrome is a progeroid disease characterised by genetic instability due to mutations to the WRN helicase/exonuclease. Here the authors define a novel Ku binding motif (KBM) and show that two such motifs facilitate the involvement of WRN in DNA double-strand break repair.
format	article
author	Gabrielle J. Grundy Stuart L. Rulten Raquel Arribas-Bosacoma Kathryn Davidson Zuzanna Kozik Antony W. Oliver Laurence H. Pearl Keith W. Caldecott
author_facet	Gabrielle J. Grundy Stuart L. Rulten Raquel Arribas-Bosacoma Kathryn Davidson Zuzanna Kozik Antony W. Oliver Laurence H. Pearl Keith W. Caldecott
author_sort	Gabrielle J. Grundy
title	The Ku-binding motif is a conserved module for recruitment and stimulation of non-homologous end-joining proteins
title_short	The Ku-binding motif is a conserved module for recruitment and stimulation of non-homologous end-joining proteins
title_full	The Ku-binding motif is a conserved module for recruitment and stimulation of non-homologous end-joining proteins
title_fullStr	The Ku-binding motif is a conserved module for recruitment and stimulation of non-homologous end-joining proteins
title_full_unstemmed	The Ku-binding motif is a conserved module for recruitment and stimulation of non-homologous end-joining proteins
title_sort	ku-binding motif is a conserved module for recruitment and stimulation of non-homologous end-joining proteins
publisher	Nature Portfolio
publishDate	2016
url	https://doaj.org/article/f76baaf3e5cb4dc5b122d503eff9616e
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The Ku-binding motif is a conserved module for recruitment and stimulation of non-homologous end-joining proteins

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