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Significance The σE stress response monitors outer membrane protein (OMP) assembly. Uninduced, σE is sequestered to the plasma membrane by its anti-sigma factor, RseA. Mutations perturbing OMP biogenesis induce degradation of RseA by the proteases DegS and RseP, liberating σE so it can activate gene expression. σE activity is essential in wild-typeEscherichia coli , although why it is essential has remained unclear. We report that batimastat is an inhibitor of RseP, preventing it from cleaving RseA and thereby causing a lethal decrease in σE activity. Surprisingly, lethality is caused by the accumulation of unfolded OMPs, despite a wild-type OMP biogenesis pathway. Hence, σE is essential because it must fine-tune OMP synthesis, assembly, and degradation to prevent the appearance of toxic unfolded OMPs.

Inhibitor of intramembrane protease RseP blocks the σ E response causing lethal accumulation of unfolded outer membrane proteins

Inhibitor of intramembrane protease RseP blocks the σ ^E response causing lethal accumulation of unfolded outer membrane proteins