Faculty Opinions recommendation of The PhoP/PhoQ two-component system stabilizes the alternative sigma factor RpoS in Salmonella enterica.

Author(s):  
Tracy Raivio
2007 ◽  
Vol 189 (20) ◽  
pp. 7335-7342 ◽  
Author(s):  
María L. Cabeza ◽  
Andrés Aguirre ◽  
Fernando C. Soncini ◽  
Eleonora García Véscovi

ABSTRACT Bacterial survival in diverse and changing environments relies on the accurate interplay between different regulatory pathways, which determine the design of an adequate adaptive response. The proper outcome depends on a precise gene expression profile generated from the finely tuned and concerted action of transcriptional factors of distinct regulatory hierarchies. Salmonella enterica serovar Typhimurium harbors multiple regulatory systems that are crucial for the bacterium to cope with harsh extra- and intracellular environments. In this work, we found that the expression of Salmonella RstA, a response regulator from the two-component system family, was able to downregulate the expression of three RpoS-controlled genes (narZ, spvA, and bapA). Furthermore, this downregulation was achieved by a reduction in RpoS cellular levels. The alternative sigma factor RpoS is critical for bacterial endurance under the most-stressful conditions, including stationary-phase entrance and host adaptation. Accordingly, RpoS cellular levels are tightly controlled by complex transcriptional, translational, and posttranslational mechanisms. The analysis of each regulatory step revealed that in Salmonella, RstA expression was able to promote RpoS degradation independently of the MviA-ClpXP proteolytic pathway. Additionally, we show that RstA is involved in modulating Salmonella biofilm formation. The fact that the RpoS-modulated genes affected by RstA expression have previously been demonstrated to contribute to Salmonella pathogenic traits, which include biofilm-forming capacity, suggests that under yet unknown conditions, RstA may function as a control point of RpoS-dependent pathways that govern Salmonella virulence.


2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Tomoko Kadowaki ◽  
Hideharu Yukitake ◽  
Mariko Naito ◽  
Keiko Sato ◽  
Yuichiro Kikuchi ◽  
...  

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Hideharu Yukitake ◽  
Mikio Shoji ◽  
Keiko Sato ◽  
Yusuke Handa ◽  
Mariko Naito ◽  
...  

AbstractPorphyromonas gingivalis, a periodontal pathogen, translocates many virulence factors including the cysteine proteases referred to as gingipains to the cell surface via the type IX secretion system (T9SS). Expression of the T9SS component proteins is regulated by the tandem signaling of the PorXY two-component system and the ECF sigma factor SigP. However, the details of this regulatory pathway are still unknown. We found that one of the T9SS conserved C-terminal domain-containing proteins, PGN_0123, which we have designated PorA, is involved in regulating expression of genes encoding T9SS structural proteins and that PorA can be translocated onto the cell surface without the T9SS translocation machinery. X-ray crystallography revealed that PorA has a domain similar to the mannose-binding domain of Escherichia coli FimH, the tip protein of Type 1 pilus. Mutations in the cytoplasmic domain of the sensor kinase PorY conferred phenotypic recovery on the ΔporA mutant. The SigP sigma factor, which is activated by the PorXY two-component system, markedly decreased in the ΔporA mutant. These results strongly support a potential role for PorA in relaying a signal from the cell surface to the PorXY-SigP signaling pathway.


Microbiology ◽  
2005 ◽  
Vol 151 (1) ◽  
pp. 209-218 ◽  
Author(s):  
Bae Hoon Kim ◽  
Seungki Kim ◽  
Hyeon Guk Kim ◽  
Jin Lee ◽  
In Soo Lee ◽  
...  

The formation of cyclopropane fatty acid (CFA) and its role in the acid shock response in Salmonella enterica serovar Typhimurium (S. typhimurium) was investigated. Data obtained by GC/MS demonstrated that the CFA level in S. typhimurium increased upon its entry to the stationary phase, as in other bacteria. The cfa gene encoding CFA synthase was cloned, and mutants of the cfa gene were constructed by allelic exchange. A cfa mutant could not produce CFA and was sensitive to low pH. Introduction of a functional cfa gene into a cfa mutant cell made the mutant convert all unsaturated fatty acids to CFAs and partially restored resistance to low pH. Interestingly, the alternative sigma factor RpoS, which was induced during the stationary phase, affected the production of C19 CFA but not C17 CFA. Western blotting analysis showed that the increase in expression of CFA synthase at early stationary phase was due to the alternative sigma factor RpoS.


2004 ◽  
Vol 186 (8) ◽  
pp. 2476-2480 ◽  
Author(s):  
Sergio Lejona ◽  
María Eugenia Castelli ◽  
María Laura Cabeza ◽  
Linda J. Kenney ◽  
Eleonora García Véscovi ◽  
...  

ABSTRACT The PhoP/PhoQ two-component system controls the extracellular magnesium depletion response in Salmonella enterica. Previous studies have shown that PhoP is unable to up-regulate its target genes in the absence of PhoQ function. In this work, we demonstrate that PhoP overexpression can substitute for PhoQ- and phosphorylation-dependent activation. Either a high concentration of PhoP or activation via phosphorylation stimulates PhoP self-association.


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