| Literature DB >> 22408168 |
A Battesti1, Y M Tsegaye, D G Packer, N Majdalani, S Gottesman.
Abstract
RpoS, the master sigma factor during stationary phase and under a variety of stress conditions, is regulated at multiple levels, including regulated degradation. Degradation is dependent upon ClpXP and the RssB adaptor protein. H-NS, a nucleoid-associated protein, affects the regulated degradation of RpoS; in the absence of H-NS, RpoS is stable. The mechanisms involved in this regulation were not known. We have found that H-NS inhibits the expression of iraD and iraM, the genes coding for two antiadaptor proteins that stabilize RpoS when overexpressed. The regulation by H-NS of iraM is independent from the previously demonstrated regulation by the PhoP/PhoQ two-component system. Moreover, differences in the behavior of several hns alleles are explained by a role for StpA, an H-NS-like protein, in the regulation of RpoS stability. This finding parallels recent observations for a role of StpA in regulation of RpoS stability in Salmonella.Mesh:
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Year: 2012 PMID: 22408168 PMCID: PMC3347191 DOI: 10.1128/JB.00132-12
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490