RAD54 N-terminal domain is a DNA sensor that couples ATP hydrolysis with branch migration of Holliday junctions

RAD54 stimulates activity of the RAD51 recombinase and catalyzes branch migration of Holliday junctions during DNA repair and recombination. Here the authors show that the N-terminal domain of RAD54 mediates RAD54 oligomerization to promote branch migration, and is the target of phosphorylation that...

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Auteurs principaux:	Nadish Goyal, Matthew J. Rossi, Olga M. Mazina, Yong Chi, Robert L. Moritz, Bruce E. Clurman, Alexander V. Mazin
Format:	article
Langue:	EN
Publié:	Nature Portfolio 2018
Sujets:	Science Q
Accès en ligne:	https://doaj.org/article/b15bd6aeba5249c9abdcd8a19d96755d
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spelling	oai:doaj.org-article:b15bd6aeba5249c9abdcd8a19d96755d2021-12-02T17:32:19ZRAD54 N-terminal domain is a DNA sensor that couples ATP hydrolysis with branch migration of Holliday junctions10.1038/s41467-017-02497-x2041-1723https://doaj.org/article/b15bd6aeba5249c9abdcd8a19d96755d2018-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-02497-xhttps://doaj.org/toc/2041-1723RAD54 stimulates activity of the RAD51 recombinase and catalyzes branch migration of Holliday junctions during DNA repair and recombination. Here the authors show that the N-terminal domain of RAD54 mediates RAD54 oligomerization to promote branch migration, and is the target of phosphorylation that inhibits oligomerization and branch migration but not RAD51 stimulation.Nadish GoyalMatthew J. RossiOlga M. MazinaYong ChiRobert L. MoritzBruce E. ClurmanAlexander V. MazinNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-10 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Nadish Goyal Matthew J. Rossi Olga M. Mazina Yong Chi Robert L. Moritz Bruce E. Clurman Alexander V. Mazin RAD54 N-terminal domain is a DNA sensor that couples ATP hydrolysis with branch migration of Holliday junctions
description	RAD54 stimulates activity of the RAD51 recombinase and catalyzes branch migration of Holliday junctions during DNA repair and recombination. Here the authors show that the N-terminal domain of RAD54 mediates RAD54 oligomerization to promote branch migration, and is the target of phosphorylation that inhibits oligomerization and branch migration but not RAD51 stimulation.
format	article
author	Nadish Goyal Matthew J. Rossi Olga M. Mazina Yong Chi Robert L. Moritz Bruce E. Clurman Alexander V. Mazin
author_facet	Nadish Goyal Matthew J. Rossi Olga M. Mazina Yong Chi Robert L. Moritz Bruce E. Clurman Alexander V. Mazin
author_sort	Nadish Goyal
title	RAD54 N-terminal domain is a DNA sensor that couples ATP hydrolysis with branch migration of Holliday junctions
title_short	RAD54 N-terminal domain is a DNA sensor that couples ATP hydrolysis with branch migration of Holliday junctions
title_full	RAD54 N-terminal domain is a DNA sensor that couples ATP hydrolysis with branch migration of Holliday junctions
title_fullStr	RAD54 N-terminal domain is a DNA sensor that couples ATP hydrolysis with branch migration of Holliday junctions
title_full_unstemmed	RAD54 N-terminal domain is a DNA sensor that couples ATP hydrolysis with branch migration of Holliday junctions
title_sort	rad54 n-terminal domain is a dna sensor that couples atp hydrolysis with branch migration of holliday junctions
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/b15bd6aeba5249c9abdcd8a19d96755d
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RAD54 N-terminal domain is a DNA sensor that couples ATP hydrolysis with branch migration of Holliday junctions

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