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Anti-adaptors provide multiple modes for regulation of the RssB adaptor protein.

ABSTRACT: RpoS, an RNA polymerase ? factor, controls the response of Escherichia coli and related bacteria to multiple stress responses. During nonstress conditions, RpoS is rapidly degraded by ClpXP, mediated by the adaptor protein RssB, a member of the response regulator family. In response to stress, RpoS degradation ceases. Small anti-adaptor proteins--IraP, IraM, and IraD, each made under a different stress condition--block RpoS degradation. RssB mutants resistant to either IraP or IraM were isolated and analyzed in vivo and in vitro. Each of the anti-adaptors is unique in its interaction with RssB and sensitivity to RssB mutants. One class of mutants defined an RssB N-terminal region close to the phosphorylation site and critical for interaction with IraP but unnecessary for IraM and IraD function. A second class, in the RssB C-terminal PP2C-like domain, led to activation of RssB function. These mutants allowed the response regulator to act in the absence of phosphorylation but did not abolish interaction with anti-adaptors. This class of mutants is broadly resistant to the anti-adaptors and bears similarity to constitutively activated mutants found in a very different PP2C protein. The mutants provide insight into how the anti-adaptors perturb RssB response regulator function and activation.

SUBMITTER: Battesti A

PROVIDER: S-EPMC3877760 | biostudies-literature | 2013 Dec

REPOSITORIES: biostudies-literature

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Anti-adaptors provide multiple modes for regulation of the RssB adaptor protein.

Battesti Aurelia A Hoskins Joel R JR Tong Song S Milanesio Paola P Mann Jessica M JM Kravats Andrea A Tsegaye Yodit M YM Bougdour Alexandre A Wickner Sue S Gottesman Susan S

Genes & development 20131201 24

RpoS, an RNA polymerase σ factor, controls the response of Escherichia coli and related bacteria to multiple stress responses. During nonstress conditions, RpoS is rapidly degraded by ClpXP, mediated by the adaptor protein RssB, a member of the response regulator family. In response to stress, RpoS degradation ceases. Small anti-adaptor proteins--IraP, IraM, and IraD, each made under a different stress condition--block RpoS degradation. RssB mutants resistant to either IraP or IraM were isolated ...[more]

PMID: 24352426

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Project description:UnlabelledRpoS (?(S)), the general stress response sigma factor, directs the expression of genes under a variety of stressful conditions. Control of the cellular ?(S) concentration is critical for appropriately scaled ?(S)-dependent gene expression. One way to maintain appropriate levels of ?(S) is to regulate its stability. Indeed, ?(S) degradation is catalyzed by the ClpXP protease and the recognition of ?(S) by ClpXP depends on the adaptor protein RssB. Three anti-adaptors (IraD, IraM, and IraP) exist in Escherichia coli K-12; each interacts with RssB and inhibits RssB activity under different stress conditions, thereby stabilizing ?(S). Unlike K-12, some E. coli isolates, including uropathogenic E. coli strain CFT073, show comparable cellular levels of ?(S) during the logarithmic and stationary growth phases, suggesting that there are differences in the regulation of ?(S) levels among E. coli strains. Here, we describe IraL, an RssB anti-adaptor that stabilizes ?(S) during logarithmic phase growth in CFT073 and other E. coli and Shigella strains. By immunoblot analyses, we show that IraL affects the levels and stability of ?(S) during logarithmic phase growth. By computational and PCR-based analyses, we reveal that iraL is found in many E. coli pathotypes but not in laboratory-adapted strains. Finally, by bacterial two-hybrid and copurification analyses, we demonstrate that IraL interacts with RssB by a mechanism distinct from that used by other characterized anti-adaptors. We introduce a fourth RssB anti-adaptor found in E. coli species and suggest that differences in the regulation of ?(S) levels may contribute to host and niche specificity in pathogenic and nonpathogenic E. coli strains.ImportanceBacteria must cope with a variety of environmental conditions in order to survive. RpoS (?(S)), the general stress response sigma factor, directs the expression of many genes under stressful conditions in both pathogenic and nonpathogenic Escherichia coli strains. The regulation of ?(S) levels and activity allows appropriately scaled ?(S)-dependent gene expression. Here, we describe IraL, an RssB anti-adaptor that, unlike previously described anti-adaptors, stabilizes ?(S) during the logarithmic growth phase in the absence of additional stress. We also demonstrate that iraL is found in a large number of E. coli and Shigella isolates. These data suggest that strains containing iraL are able to initiate ?(S)-dependent gene expression under conditions under which strains without iraL cannot. Therefore, IraL-mediated ?(S) stabilization may contribute to host and niche specificity in E. coli.

Dataset Information

Anti-adaptors provide multiple modes for regulation of the RssB adaptor protein.

Publications

Anti-adaptors provide multiple modes for regulation of the RssB adaptor protein.

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