Bacillus subtilis RarA Acts as a Positive RecA Accessory Protein
Ubiquitous RarA AAAC ATPases play crucial roles in the cellular response to blocked replication forks in pro- and eukaryotes. Here, we provide evidence that absence of RarA reduced the viability of recA, recO, and recF15 cells during unperturbed growth. The rarA gene was epistatic to recO and recF g...
| Autores: | , , , , , , , |
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| Tipo de recurso: | artículo |
| Fecha de publicación: | 2020 |
| País: | España |
| Institución: | Universidad Complutense de Madrid (UCM) |
| Repositorio: | Docta Complutense |
| Idioma: | inglés |
| OAI Identifier: | oai:docta.ucm.es:20.500.14352/113204 |
| Acceso en línea: | https://hdl.handle.net/20.500.14352/113204 |
| Access Level: | acceso abierto |
| Palabra clave: | 577 579 Mgs1 WRNIP1 Replication stress RecA mediators RecA modulators Biología molecular (Biología) Bioquímica (Biología) Microbiología (Biología) 2403 Bioquímica 2415.01 Biología Molecular de Microorganismos 2414 Microbiología |
| Sumario: | Ubiquitous RarA AAAC ATPases play crucial roles in the cellular response to blocked replication forks in pro- and eukaryotes. Here, we provide evidence that absence of RarA reduced the viability of recA, recO, and recF15 cells during unperturbed growth. The rarA gene was epistatic to recO and recF genes in response to H2O2- or MMS-induced DNA damage. 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, and possibly antagonizes RecA filament disassembly. |
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