The Rcs Two-Component System Regulates Expression of Lysozyme Inhibitors and Is Induced by Exposure to Lysozyme

Callewaert, Lien; Vanoirbeek, Kristof; Lurquin, Ine; Michiels, Chris W.; Aertsen, Abram

doi:10.1128/jb.01549-08

Cited by 53 publications

(47 citation statements)

References 15 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Anhydromuropeptide monomers or subsequent PG degradation products may initiate signaling in the periplasm. However, neither the well-studied Rcs phosphorelay system, the major signaling pathway that senses perturbations in PG turnover (6,24,33), nor the Cpx phosphorelay system was found to contribute to the downregulation of CsgD by MltE/MltC. Consistently with this finding, susceptibility to selected ␤-lactam antibiotics was not changed in the ⌬mltE ⌬mltC double mutant (data not shown).…”

Section: Discussionmentioning

confidence: 55%

Regulation of Biofilm Components in Salmonella enterica Serovar Typhimurium by Lytic Transglycosylases Involved in Cell Wall Turnover

et al. 2011

View full text Add to dashboard Cite

In Salmonella enterica serovar Typhimurium, a biofilm mode of growth known as the rdar morphotype is regulated by several networks which sense multiple environmental signals. The transcriptional regulator CsgD is the major target for these regulatory pathways. In this study, we show that two lytic transglycosylases of family I, MltE and MltC, in combination increase CsgD expression and rdar morphotype. MltE and MltC, which share a highly similar transglycosylase SLT domain, work redundantly to regulate CsgD at the transcriptional and posttranscriptional levels. The effect of MltE and MltC on CsgD levels was independent of the known regulatory pathways that sense cell envelope stress. These findings reveal, for the first time, a specific function of lytic transglycosylases in S. Typhimurium and suggest the existence of a new signaling pathway that links cell wall turnover to biofilm formation.

show abstract

Section: Discussionmentioning

confidence: 55%

Regulation of Biofilm Components in Salmonella enterica Serovar Typhimurium by Lytic Transglycosylases Involved in Cell Wall Turnover

et al. 2011

View full text Add to dashboard Cite

show abstract

“…Because the Rcs system strongly induces the rprA promoter in E. coli (21), and other cell envelope-damaging conditions trigger RprA synthesis through RcsB (21,(43)(44)(45), we hypothesized that the bile-induced increase in RicI synthesis is indirect, resulting from the Rcs-mediated activation of RprA. To test this, we constructed single-gene deletion strains of various components of the Rcs signaling cascade and evaluated bile-induced changes in the levels of RprA and RicI levels in these mutants.…”

Section: Resultsmentioning

confidence: 99%

Small RNA-based feedforward loop with AND-gate logic regulates extrachromosomal DNA transfer in Salmonella

Papenfort

Espinosa

Casadesús

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

Horizontal gene transfer via plasmid conjugation is a major driving force in microbial evolution but constitutes a complex process that requires synchronization with the physiological state of the host bacteria. Although several host transcription factors are known to regulate plasmid-borne transfer genes, RNA-based regulatory circuits for host-plasmid communication remain unknown. We describe a posttranscriptional mechanism whereby the Hfq-dependent small RNA, RprA, inhibits transfer of pSLT, the virulence plasmid of Salmonella enterica. RprA employs two separate seed-pairing domains to activate the mRNAs of both the sigma-factor σ S and the RicI protein, a previously uncharacterized membrane protein here shown to inhibit conjugation. Transcription of ricI requires σ S and, together, RprA and σ S orchestrate a coherent feedforward loop with AND-gate logic to tightly control the activation of RicI synthesis. RicI interacts with the conjugation apparatus protein TraV and limits plasmid transfer under membrane-damaging conditions. To our knowledge, this study reports the first small RNA-controlled feedforward loop relying on posttranscriptional activation of two independent targets and an unexpected role of the conserved RprA small RNA in controlling extrachromosomal DNA transfer.RprA | sRNA | feedforward control | plasmid conjugation | Hfq

show abstract

“…In Escherichia coli, RcsFCDB contributes to resistance to select ␤-lactams; lysozyme exposure and a variety of other conditions result in its activation. For example, mutants with diverse weakened or altered envelope structures demonstrate Rcs regulon activation (8,9,17,27,36,39,42). The different disruptions include altered lipopolysaccharide (LPS) structure in rfa-1 mutants, dysregulation of membrane-derived oligosaccharides in mdoH mutants, and defects in acidic phospholipid synthesis in pgsA mutants (9,17,36,42).…”

mentioning

confidence: 99%

Antimicrobial Peptides Activate the Rcs Regulon through the Outer Membrane Lipoprotein RcsF

et al. 2010

View full text Add to dashboard Cite

Salmonella enterica species are exposed to envelope stresses due to their environmental and infectious lifestyles. Such stresses include amphipathic cationic antimicrobial peptides (CAMPs), and resistance to these peptides is an important property for microbial virulence for animals. Bacterial mechanisms used to sense and respond to CAMP-induced envelope stress include the RcsFCDB phosphorelay, which contributes to survival from polymyxin B exposure. The Rcs phosphorelay includes two inner membrane (IM) proteins, RcsC and RcsD; the response regulator RcsB; the accessory coregulator RcsA; and an outer membrane bound lipoprotein, RcsF. Transcriptional activation of the Rcs regulon occurred within minutes of exposure to CAMP and during the first detectable signs of CAMP-induced membrane disorder. Rcs transcriptional activation by CAMPs required RcsF and preservation of its two internal disulfide linkages. The rerouting of RcsF to the inner membrane or its synthesis as an unanchored periplasmic protein resulted in constitutive activation of the Rcs regulon and RcsCD-dependent phosphorylation. These findings suggest that RcsFCDB activation in response to CAMP-induced membrane disorder is a result of a change in structure or availability of RcsF to the IM signaling constituents of the Rcs phosphorelay.

show abstract

The Rcs Two-Component System Regulates Expression of Lysozyme Inhibitors and Is Induced by Exposure to Lysozyme

Cited by 53 publications

References 15 publications

Regulation of Biofilm Components in Salmonella enterica Serovar Typhimurium by Lytic Transglycosylases Involved in Cell Wall Turnover

Regulation of Biofilm Components in Salmonella enterica Serovar Typhimurium by Lytic Transglycosylases Involved in Cell Wall Turnover

Small RNA-based feedforward loop with AND-gate logic regulates extrachromosomal DNA transfer in Salmonella

Antimicrobial Peptides Activate the Rcs Regulon through the Outer Membrane Lipoprotein RcsF

Contact Info

Product

Resources

About