Abstract
Correction to: The EMBO Journal (2000) 19, 5980–5988. doi: 10.1093/emboj/19.22.5980
During reconstruction of ompL/dsbA double mutants, we observed that null mutation in ompL suppressed the defects of dsbA mutant bacteria in oxidative folding of secreted proteins only partially (about 20–30%). During our initial series of experiments, we observed a complete suppression of dsbA phenotypes upon introduction of the ompL null allele. The discrepancy was repeatedly observed for Escherichia coli strain SR4444Δ (dsbA ompL). We conclude that this strain likely carries a second mutation, which contributes to the complete restoration of oxidative protein folding.
Our conclusions for a role of OmpL in modulating the oxidative environment of E. coli periplasmic space gain further support as we have again cloned the ompL gene, which, when overexpressed from a plasmid, confers resistance to sublethal concentrations of oxidizing agents such as diamide. We would like to bring to the attention of readers that it was MC1000 that was used in our studies and is the parent of SR2262 and SR4444, and that in page 5987 temperature used for motility assay was 30°C and the agar concentration was 0.3%.