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S stability in Escherichia coli
Laboratory of Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892, USA
The 
S subunit of Escherichia coli RNA polymerase regulates the expression of stationary phase and stress response genes. S is highly unstable in exponentially growing cells, whereas its stability increases dramatically upon starvation or under certain stress conditions. The degradation of S is controlled by the phosphorylatable adaptor protein RssB and the ClpXP protease. RssB specifically directs S to ClpXP. An unanswered question is how RssB-mediated degradation of S is blocked by conditions such as glucose or phosphate starvation. We report here the identification and characterization of a new regulator of S stability, IraP (inhibitor of RssB activity during phosphate starvation), that stabilizes S both in vivo and in vitro. Deletion of iraP interferes with 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 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 S degradation and interaction with RssB. Our results reveal a novel mechanism of regulation of S stability through the regulation of RssB activity and identify IraP as a member of a new class of regulators, the anti-adaptor proteins.
[Keywords: RpoS; 38; YaiB; regulated proteolysis; starvation]
Received December 12, 2005; revised version accepted February 6, 2006.
E-MAIL susang{at}helix.nih.gov; FAX (301) 496-3875.
Article and publication are at http://www.genesdev.org/cgi/doi/10.1101/NA
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