Six putative two-component regulatory systems isolated from Lactococcus lactis subsp. cremoris MG1363 The GenBank accession numbers for the sequences of the six 2CSs and surrounding ORFs determined in this work are AF172649, AF176556, AF178425, AF172650, AF176557 and AF176809 for systems A–F, respectively.

Motherway, Mary O’Connell; Sinderen, Douwe van; Morel‐Deville, Françoise; Fitzgerald, Gerald F.; Ehrlich, S. Dusko; Morel, Patrice

doi:10.1099/00221287-146-4-935

Cited by 69 publications

(56 citation statements)

References 48 publications

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“…lactis. Disrupting the gene for CesR led to a reduction in the ability to resist salt and osmotic stresses (66). The authors could not generate a CesS mutant, probably because that mutation was lethal.…”

Section: Mechanosensitive Channelsmentioning

confidence: 99%

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Stress Physiology of Lactic Acid Bacteria

Papadimitriou

Alegría

Bron

et al. 2016

Microbiol Mol Biol Rev

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508

404

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SUMMARYLactic acid bacteria (LAB) are important starter, commensal, or pathogenic microorganisms. The stress physiology of LAB has been studied in depth for over 2 decades, fueled mostly by the technological implications of LAB robustness in the food industry. Survival of probiotic LAB in the host and the potential relatedness of LAB virulence to their stress resilience have intensified interest in the field. Thus, a wealth of information concerning stress responses exists today for strains as diverse as starter (e.g.,Lactococcus lactis), probiotic (e.g., severalLactobacillusspp.), and pathogenic (e.g.,EnterococcusandStreptococcusspp.) LAB. Here we present the state of the art for LAB stress behavior. We describe the multitude of stresses that LAB are confronted with, and we present the experimental context used to study the stress responses of LAB, focusing on adaptation, habituation, and cross-protection as well as on self-induced multistress resistance in stationary phase, biofilms, and dormancy. We also consider stress responses at the population and single-cell levels. Subsequently, we concentrate on the stress defense mechanisms that have been reported to date, grouping them according to their direct participation in preserving cell energy, defending macromolecules, and protecting the cell envelope. Stress-induced responses of probiotic LAB and commensal/pathogenic LAB are highlighted separately due to the complexity of the peculiar multistress conditions to which these bacteria are subjected in their hosts. Induction of prophages under environmental stresses is then discussed. Finally, we present systems-based strategies to characterize the “stressome” of LAB and to engineer new food-related and probiotic LAB with improved stress tolerance.

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Section: Mechanosensitive Channelsmentioning

confidence: 99%

“…The involvement of TCSs in stress responses in LAB has been evidenced mainly by phenotypic analyses of TCS-defective mutants (60)(61)(62)(63)(64)(65)(66)(67). Inactivation of homologous TCSs often results in different phenotypes, suggesting that they have different physiological roles.…”

Section: Two-component Systemsmentioning

confidence: 99%

Stress Physiology of Lactic Acid Bacteria

Papadimitriou

Alegría

Bron

et al. 2016

Microbiol Mol Biol Rev

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508

404

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“…LiaRS has also been identified as upregulating dltA expression in Streptococcus gordonii (149). CesSR (also referred to as TCS-D) (141,150) is an LiaRS homologue found in L. lactis. Upstream of cesSR is llmg1650, an liaF homologue.…”

Section: Liars and Liars-like Two-component Systemsmentioning

confidence: 99%

Lantibiotic Resistance

Draper

Cotter

Hill

et al. 2015

Microbiol Mol Biol Rev

132

129

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SUMMARY The dramatic rise in the incidence of antibiotic resistance demands that new therapeutic options will have to be developed. One potentially interesting class of antimicrobials are the modified bacteriocins termed lantibiotics, which are bacterially produced, posttranslationally modified, lanthionine/methyllanthionine-containing peptides. It is interesting that low levels of resistance have been reported for lantibiotics compared with commercial antibiotics. Given that there are very few examples of naturally occurring lantibiotic resistance, attempts have been made to deliberately induce resistance phenotypes in order to investigate this phenomenon. Mechanisms that hinder the action of lantibiotics are often innate systems that react to the presence of any cationic peptides/proteins or ones which result from cell well damage, rather than being lantibiotic specific. Such resistance mechanisms often arise due to altered gene regulation following detection of antimicrobials/cell wall damage by sensory proteins at the membrane. This facilitates alterations to the cell wall or changes in the composition of the membrane. Other general forms of resistance include the formation of spores or biofilms, which are a common mechanistic response to many classes of antimicrobials. In rare cases, bacteria have been shown to possess specific antilantibiotic mechanisms. These are often species specific and include the nisin lytic protein nisinase and the phenomenon of immune mimicry.

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“…The fact that the arginine degradative pathway is involved in a range of diverse cellular functions such as energy production, acid stress resistance, and pyrimidine biosynthesis could explain the presence of such a complex regulatory circuit. Interestingly, O'Connell-Motherway et al (36) have reported on an essential two-component system that is involved in activation of arginine degradation. Whether and how this system is responsible for some of the effects described above remain to be elucidated.…”

Section: Vol 186 2004 Regulation Of Arginine Metabolism In L Lactimentioning

confidence: 99%

ArgR and AhrC Are Both Required for Regulation of Arginine Metabolism in Lactococcus lactis

et al. 2004

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The DNA binding proteins ArgR and AhrC are essential for regulation of arginine metabolism in Escherichia coli and Bacillus subtilis, respectively. A unique property of these regulators is that they form hexameric protein complexes, mediating repression of arginine biosynthetic pathways as well as activation of arginine catabolic pathways. The gltS-argE operon of Lactococcus lactis encodes a putative glutamate or arginine transport protein and acetylornithine deacetylase, which catalyzes an important step in the arginine biosynthesis pathway. By random integration knockout screening we found that derepression mutants had ISS1 integrations in, among others, argR and ahrC. Single as well as double regulator deletion mutants were constructed from Lactococcus lactis subsp. cremoris MG1363. The three arginine biosynthetic operons argCJDBF, argGH, and gltS-argE were shown to be repressed by the products of argR and ahrC. Furthermore, the arginine catabolic arcABD1C1C2TD2 operon was activated by the product of ahrC but not by that of argR. Expression from the promoter of the argCJDBF operon reached similar levels in the single mutants and in the double mutant, suggesting that the regulators are interdependent and not able to complement each other. At the same time they also appear to have different functions, as only AhrC is involved in activation of arginine catabolism. This is the first study where two homologous arginine regulators are shown to be involved in arginine regulation in a prokaryote, representing an unusual mechanism of regulation.Arginine, a nonessential amino acid in the lactic acid bacterium Lactococcus lactis, is synthesized de novo from glutamate in eight enzymatic steps (Fig. 1). The recent publication of the L. lactis genome sequence (5) has revealed that the putative arginine biosynthesis genes are encoded by the three operons argCJDBF, gltS-argE, and argGH. The products of these genes all show homology to known arginine biosynthetic enzymes, except for that of gltS, which has been annotated as a putative glutamate or arginine ABC transporter (5). While the biosynthetic genes have been shown to be regulated by the presence of arginine in other organisms, this has not been investigated in lactic acid bacteria (LAB). The activities of the biosynthetic enzymes have been shown to be repressed by arginine in Lactobacillus plantarum (6), but regulatory studies on the transcriptional level have not been performed on LAB.Mechanisms for arginine catabolism vary among organisms (1). In L. lactis, complete degradation of arginine into ornithine, ammonium, and carbon dioxide takes place via the arginine deiminase pathway (ADI pathway) in three enzymatic steps catalyzed by arginine deiminase (ArcA), ornithine carbamoyltransferase (ArcB), and carbamate kinase (ArcC) (Fig. 1). The genes arcA, arcB, arcC1, and arcC2 encoding these enzymes are located in the arcABD1C1C2TD2 gene cluster. L. lactis harbors an extra arcC homologue, called arcC3, which is located distant from the remainder of the arginine-related ge...

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Cited by 69 publications

References 48 publications

Stress Physiology of Lactic Acid Bacteria

Stress Physiology of Lactic Acid Bacteria

Lantibiotic Resistance

ArgR and AhrC Are Both Required for Regulation of Arginine Metabolism in Lactococcus lactis

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