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The σ S  subunit of  Escherichia coli  RNA polymerase regulates the expression of stationary phase and stress response genes. σ S  is highly unstable in exponentially growing cells, whereas its stability increases dramatically upon starvation or under certain stress conditions. The degradation of σ S  is controlled by the phosphorylatable adaptor protein RssB and the ClpXP protease. RssB specifically directs σ S  to ClpXP. An unanswered question is how RssB-mediated degradation of σ S  is blocked by conditions such as glucose or phosphate starvation. We report here the identification and characterization of a new regulator of σ S  stability, IraP (inhibitor of RssB activity during phosphate starvation), that stabilizes σ S  both in vivo and in vitro. Deletion of  iraP  interferes with σ S  stabilization during phosphate starvation, but not during carbon starvation, and has a partial effect in stationary phase and nitrogen starvation. IraP interferes with RssB-dependent degradation of σ S  through a direct protein–protein interaction with RssB. A point mutant of IraP was isolated and found to be defective both for inhibition of σ S  degradation and interaction with RssB. Our results reveal a novel mechanism of regulation of σ S  stability through the regulation of RssB activity and identify IraP as a member of a new class of regulators, the anti-adaptor proteins.

Modulating RssB activity: IraP, a novel regulator of σS stability in Escherichia coli

Modulating RssB activity: IraP, a novel regulator of σ^S stability in Escherichia coli