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- W1993048758 abstract "A growing body of evidence shows that there is an intimate connection between proteins required for genome stability and stationary phase survival. In this work we show that the integral membrane protein UspB, a member of the RpoS regulon, is required for proper DNA repair as mutants lacking uspB are hypersensitive to several DNA damaging agents including ultraviolet light, mitomycin C, bleomycin and ciprofloxacin. Genetic and physical studies demonstrate that UspB acts in the RuvABC recombination repair pathway and removing uspB creates a phenocopy of the Holliday junction resolvase mutant, ruvC. Further, we show that the uspB mutant phenotype can be suppressed by ectopic overproduction of RuvC and that both ruvC and uspB mutants can be suppressed by inactivating recD. The fact that RuvABC-dependent repair requires UspB for proper activity suggests that the sigma-S regulon works together with DNA repair pathways under stress conditions to defend the cell against genotoxic stress." @default.
- W1993048758 created "2016-06-24" @default.
- W1993048758 creator A5041540706 @default.
- W1993048758 creator A5057438201 @default.
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- W1993048758 date "2010-11-01" @default.
- W1993048758 modified "2023-10-03" @default.
- W1993048758 title "UspB, a member of the sigma-S regulon, facilitates RuvC resolvase function" @default.
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- W1993048758 doi "https://doi.org/10.1016/j.dnarep.2010.08.004" @default.
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