Bacillus subtilis RarA Acts as a Positive RecA Accessory Protein

Ubiquitous RarA AAA+ ATPases play crucial roles in the cellular response to blocked replication forks in pro- and eukaryotes. Here, we provide evidence that RarA regulates the activity of the central player in homologous recombination (HR), RecA, in response to DNA damage. During unperturbed growth,...

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Detalles Bibliográficos
Autores: Romero, Héctor, Serrano, Ester, Hernández-Tamayo, Rogelio, Carrasco, Begoña, Cárdenas, Paula P., Ayora, Silvia, Graumann, Peter L., Alonso, Juan C.
Tipo de recurso: artículo
Fecha de publicación:2020
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/214041
Acceso en línea:http://hdl.handle.net/10261/214041
Access Level:acceso abierto
Palabra clave:Mgs1
WRNIP1
Replication stress
RecA mediators
RecA modulators
Descripción
Sumario:Ubiquitous RarA AAA+ ATPases play crucial roles in the cellular response to blocked replication forks in pro- and eukaryotes. Here, we provide evidence that RarA regulates the activity of the central player in homologous recombination (HR), RecA, in response to DNA damage. During unperturbed growth, absence of RarA reduced the viability of recA, recO and recF15 cells, and during repair of H2O2- or MMS-induced DNA damage, rarA was epistatic to recA, recO and recF. Conversely, the inactivation of rarA partially suppressed the HR defect of mutants lacking end-resection (addAB, recJ, recQ, recS) or branch migration (ruvAB, recG, radA) activity. RarA contributes to RecA thread formation, that are thought to be the active forms of RecA during homology search. The absence of RarA reduced RecA accumulation, and the formation of visible RecA threads in vivo upon DNA damage. When rarA was combined with mutations in genuine RecA accessory genes, RecA accumulation was further reduced in rarA recU and rarA recX double mutant cells, and was blocked in rarA recF15 cells. These results suggest that RarA contributes to the assembly of RecA nucleoprotein filaments onto single-stranded DNA (ssDNA), in concert with RecF, and possibly antagonizes RecA filament disassembly by RecX or RecU.