Overexpression of the ATP-dependent helicase RecG improves resistance to weak organic acids in Escherichia coli.
Increased resistance to several weak organic acids was conferred on Escherichia coli by overexpression of the ATP-dependent helicase RecG and, to a lesser extent, by overexpressing the helicase RuvAB. This property of helicases was identified by reproducible selection of recG-bearing clones from genomic libraries of the acetate-resistant species Acetobacter aceti and Staphylococcus capitis. We show that overexpression of RecG from both species, but also from E. coli, increased the maximum biomass concentration attained by E. coli cultures that were grown in the presence of various weak organic acids and uncouplers. Furthermore, overexpression of RecG from A. aceti significantly improved the maximum growth rates of E. coli under weak organic acid challenge. Based on the known role of RecG in DNA replication/repair, our data provide a first indication that weak organic acids negatively affect DNA replication and/or repair, and that these negative effects may be counteracted by helicase activity.
Steiner
P
P
Institute of Biotechnology, ETH Zürich, 8093, Zürich, Switzerland.
Sauer
U
U
D000091:Acetobacter / Q000235:genetics; D000143:Acids / Q000494:pharmacology; D000255:Adenosine Triphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D004265:DNA Helicases / Q000378:metabolism; D004260:DNA Repair; D024881:Drug Resistance, Bacterial; D004926:Escherichia coli / Q000187:drug effects / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000378:metabolism*; D008969:Molecular Sequence Data; D017385:Sequence Homology; D013210:Staphylococcus / Q000235:genetics
D000143:Acids; D029968:Escherichia coli Proteins; C071446:RecG protein, E coli; D000255:Adenosine Triphosphate; D004265:DNA Helicases