Molecular basis for PrimPol recruitment to replication forks by RPA

PrimPol is a multifunctional replicative enzyme that can bypass DNA damage, as well as reprime replication restart. Here, the authors have elucidated how PrimPol is recruited to stalled replication forks via specific interactions with RPA, which stimulates its primase activity.

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Autores principales:	Thomas A. Guilliam, Nigel C. Brissett, Aaron Ehlinger, Benjamin A. Keen, Peter Kolesar, Elaine M. Taylor, Laura J. Bailey, Howard D. Lindsay, Walter J. Chazin, Aidan J. Doherty
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/6c3b35c0421a4ab2b8722df6acbdcac6
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spelling	oai:doaj.org-article:6c3b35c0421a4ab2b8722df6acbdcac62021-12-02T17:06:20ZMolecular basis for PrimPol recruitment to replication forks by RPA10.1038/ncomms152222041-1723https://doaj.org/article/6c3b35c0421a4ab2b8722df6acbdcac62017-05-01T00:00:00Zhttps://doi.org/10.1038/ncomms15222https://doaj.org/toc/2041-1723PrimPol is a multifunctional replicative enzyme that can bypass DNA damage, as well as reprime replication restart. Here, the authors have elucidated how PrimPol is recruited to stalled replication forks via specific interactions with RPA, which stimulates its primase activity.Thomas A. GuilliamNigel C. BrissettAaron EhlingerBenjamin A. KeenPeter KolesarElaine M. TaylorLaura J. BaileyHoward D. LindsayWalter J. ChazinAidan J. DohertyNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-14 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Thomas A. Guilliam Nigel C. Brissett Aaron Ehlinger Benjamin A. Keen Peter Kolesar Elaine M. Taylor Laura J. Bailey Howard D. Lindsay Walter J. Chazin Aidan J. Doherty Molecular basis for PrimPol recruitment to replication forks by RPA
description	PrimPol is a multifunctional replicative enzyme that can bypass DNA damage, as well as reprime replication restart. Here, the authors have elucidated how PrimPol is recruited to stalled replication forks via specific interactions with RPA, which stimulates its primase activity.
format	article
author	Thomas A. Guilliam Nigel C. Brissett Aaron Ehlinger Benjamin A. Keen Peter Kolesar Elaine M. Taylor Laura J. Bailey Howard D. Lindsay Walter J. Chazin Aidan J. Doherty
author_facet	Thomas A. Guilliam Nigel C. Brissett Aaron Ehlinger Benjamin A. Keen Peter Kolesar Elaine M. Taylor Laura J. Bailey Howard D. Lindsay Walter J. Chazin Aidan J. Doherty
author_sort	Thomas A. Guilliam
title	Molecular basis for PrimPol recruitment to replication forks by RPA
title_short	Molecular basis for PrimPol recruitment to replication forks by RPA
title_full	Molecular basis for PrimPol recruitment to replication forks by RPA
title_fullStr	Molecular basis for PrimPol recruitment to replication forks by RPA
title_full_unstemmed	Molecular basis for PrimPol recruitment to replication forks by RPA
title_sort	molecular basis for primpol recruitment to replication forks by rpa
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/6c3b35c0421a4ab2b8722df6acbdcac6
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Molecular basis for PrimPol recruitment to replication forks by RPA

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