DisA Restrains the Processing and Cleavage of Reversed Replication Forks by the RuvAB-RecU Resolvasome

DNA lesions that impede fork progression cause replisome stalling and threaten genome stability. <i>Bacillus subtilis</i> RecA, at a lesion-containing gap, interacts with and facilitates DisA pausing at these branched intermediates. Paused DisA suppresses its synthesis of the essential c...

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Autores principales:	Carolina Gándara, Rubén Torres, Begoña Carrasco, Silvia Ayora, Juan C. Alonso
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	replication stress DNA damage signal fork reversal c-di-AMP RuvAB RecU Biology (General) QH301-705.5 Chemistry QD1-999
Acceso en línea:	https://doaj.org/article/baa81b4f188b4ffa8959324883e7bcf4
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spelling	oai:doaj.org-article:baa81b4f188b4ffa8959324883e7bcf42021-11-11T16:48:33ZDisA Restrains the Processing and Cleavage of Reversed Replication Forks by the RuvAB-RecU Resolvasome10.3390/ijms2221113231422-00671661-6596https://doaj.org/article/baa81b4f188b4ffa8959324883e7bcf42021-10-01T00:00:00Zhttps://www.mdpi.com/1422-0067/22/21/11323https://doaj.org/toc/1661-6596https://doaj.org/toc/1422-0067DNA lesions that impede fork progression cause replisome stalling and threaten genome stability. <i>Bacillus subtilis</i> RecA, at a lesion-containing gap, interacts with and facilitates DisA pausing at these branched intermediates. Paused DisA suppresses its synthesis of the essential c-di-AMP messenger. The RuvAB-RecU resolvasome branch migrates and resolves formed Holliday junctions (HJ). We show that DisA prevents DNA degradation. DisA, which interacts with RuvB, binds branched structures, and reduces the RuvAB DNA-dependent ATPase activity. DisA pre-bound to HJ DNA limits RuvAB and RecU activities, but such inhibition does not occur if the RuvAB- or RecU-HJ DNA complexes are pre-formed. RuvAB or RecU pre-bound to HJ DNA strongly inhibits DisA-mediated synthesis of c-di-AMP, and indirectly blocks cell proliferation. We propose that DisA limits RuvAB-mediated fork remodeling and RecU-mediated HJ cleavage to provide time for damage removal and replication restart in order to preserve genome integrity.Carolina GándaraRubén TorresBegoña CarrascoSilvia AyoraJuan C. AlonsoMDPI AGarticlereplication stressDNA damage signalfork reversalc-di-AMPRuvABRecUBiology (General)QH301-705.5ChemistryQD1-999ENInternational Journal of Molecular Sciences, Vol 22, Iss 11323, p 11323 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	replication stress DNA damage signal fork reversal c-di-AMP RuvAB RecU Biology (General) QH301-705.5 Chemistry QD1-999
spellingShingle	replication stress DNA damage signal fork reversal c-di-AMP RuvAB RecU Biology (General) QH301-705.5 Chemistry QD1-999 Carolina Gándara Rubén Torres Begoña Carrasco Silvia Ayora Juan C. Alonso DisA Restrains the Processing and Cleavage of Reversed Replication Forks by the RuvAB-RecU Resolvasome
description	DNA lesions that impede fork progression cause replisome stalling and threaten genome stability. <i>Bacillus subtilis</i> RecA, at a lesion-containing gap, interacts with and facilitates DisA pausing at these branched intermediates. Paused DisA suppresses its synthesis of the essential c-di-AMP messenger. The RuvAB-RecU resolvasome branch migrates and resolves formed Holliday junctions (HJ). We show that DisA prevents DNA degradation. DisA, which interacts with RuvB, binds branched structures, and reduces the RuvAB DNA-dependent ATPase activity. DisA pre-bound to HJ DNA limits RuvAB and RecU activities, but such inhibition does not occur if the RuvAB- or RecU-HJ DNA complexes are pre-formed. RuvAB or RecU pre-bound to HJ DNA strongly inhibits DisA-mediated synthesis of c-di-AMP, and indirectly blocks cell proliferation. We propose that DisA limits RuvAB-mediated fork remodeling and RecU-mediated HJ cleavage to provide time for damage removal and replication restart in order to preserve genome integrity.
format	article
author	Carolina Gándara Rubén Torres Begoña Carrasco Silvia Ayora Juan C. Alonso
author_facet	Carolina Gándara Rubén Torres Begoña Carrasco Silvia Ayora Juan C. Alonso
author_sort	Carolina Gándara
title	DisA Restrains the Processing and Cleavage of Reversed Replication Forks by the RuvAB-RecU Resolvasome
title_short	DisA Restrains the Processing and Cleavage of Reversed Replication Forks by the RuvAB-RecU Resolvasome
title_full	DisA Restrains the Processing and Cleavage of Reversed Replication Forks by the RuvAB-RecU Resolvasome
title_fullStr	DisA Restrains the Processing and Cleavage of Reversed Replication Forks by the RuvAB-RecU Resolvasome
title_full_unstemmed	DisA Restrains the Processing and Cleavage of Reversed Replication Forks by the RuvAB-RecU Resolvasome
title_sort	disa restrains the processing and cleavage of reversed replication forks by the ruvab-recu resolvasome
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/baa81b4f188b4ffa8959324883e7bcf4
work_keys_str_mv	AT carolinagandara disarestrainstheprocessingandcleavageofreversedreplicationforksbytheruvabrecuresolvasome AT rubentorres disarestrainstheprocessingandcleavageofreversedreplicationforksbytheruvabrecuresolvasome AT begonacarrasco disarestrainstheprocessingandcleavageofreversedreplicationforksbytheruvabrecuresolvasome AT silviaayora disarestrainstheprocessingandcleavageofreversedreplicationforksbytheruvabrecuresolvasome AT juancalonso disarestrainstheprocessingandcleavageofreversedreplicationforksbytheruvabrecuresolvasome
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DisA Restrains the Processing and Cleavage of Reversed Replication Forks by the RuvAB-RecU Resolvasome

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