The RecD2 helicase balances RecA activities

Ramos, C., Hernández-Tamayo, R., López-Sanz, M., Carrasco, B., Serrano, E. , Alonso, J. C., Graumann, P. L. and Ayora, S. (2022) The RecD2 helicase balances RecA activities. Nucleic Acids Research, 50(6), pp. 3432-3444. (doi: 10.1093/nar/gkac131) (PMID:35234892) (PMCID:PMC8989531)

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DNA helicases of the RecD2 family are ubiquitous. Bacillus subtilis RecD2 in association with the single-stranded binding protein SsbA may contribute to replication fork progression, but its detailed action remains unknown. In this work, we explore the role of RecD2 during DNA replication and its interaction with the RecA recombinase. RecD2 inhibits replication restart, but this effect is not observed in the absence of SsbA. RecD2 slightly affects replication elongation. RecA inhibits leading and lagging strand synthesis, and RecD2, which physically interacts with RecA, counteracts this negative effect. In vivo results show that recD2 inactivation promotes RecA–ssDNA accumulation at low mitomycin C levels, and that RecA threads persist for a longer time after induction of DNA damage. In vitro, RecD2 modulates RecA-mediated DNA strand-exchange and catalyzes branch migration. These findings contribute to our understanding of how RecD2 may contribute to overcome a replicative stress, removing RecA from the ssDNA and, thus, it may act as a negative modulator of RecA filament growth.

Item Type:Articles
Additional Information:Ministerio de Ciencia e Innovacion MCIN ´ / AEI/ FEDER, EU [PGC2018-097054-B-I00 to J.C.A. and S.A.]; Deutsche Forschungsgemeinschaft (DFG-funded consortium TRR 178 to P.L.G.). Funding for open access charge: CSIC Open Access Publication Support Initiative.
Glasgow Author(s) Enlighten ID:Serrano, Dr Ester
Authors: Ramos, C., Hernández-Tamayo, R., López-Sanz, M., Carrasco, B., Serrano, E., Alonso, J. C., Graumann, P. L., and Ayora, S.
College/School:College of Medical Veterinary and Life Sciences > School of Infection & Immunity
Journal Name:Nucleic Acids Research
Publisher:Oxford University Press
ISSN (Online):1362-4962
Published Online:02 March 2022
Copyright Holders:Copyright © The Author(s) 2022
First Published:First published in Nucleic Acids Research 50(6):3432-3444
Publisher Policy:Reproduced under a Creative Commons license

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