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The cell envelope stress response mediated by the LiaFSRLm three-component system of Listeria monocytogenes is controlled via the phosphatase activity of the bifunctional histidine kinase LiaSLm

ABSTRACT: Most members of the phylum Firmicutes harbor a two-component system, LiaSR, which is involved in the response to cell envelope stress elicited most notably by inhibitors of the lipid II cycle. In all LiaSR systems studied in detail LiaSR-mediated signal transduction was shown to be negatively controlled by a membrane protein, LiaF, encoded upstream of liaSR. In this study we have analysed the LiaSR homolog of Listeria monocytogenes (LiaSRLm). Whole genome transcriptional profiling indicated that activation of LiaSRLm results in a remodeling of the cell envelope via the massive upregulation of membrane or cell-wall associated proteins in the presence of inducing stimuli. As shown for other LiaSR two-component systems LiaSRLm is activated by cell wall-active antibiotics. We demonstrate that the level of phosphorylated LiaRLm, which is required for the induction of the LiaSRLm regulon, is controlled by the interplay between histidine kinase and phosphatase activity of the bifunctional sensor protein LiaSLm. Our data suggest that the phosphatase activity of LiaSLm is stimulated by LiaF in the absence of cell envelope stress

ORGANISM(S): Listeria monocytogenes Listeria monocytogenes EGD-e

PROVIDER: GSE24107 | GEO | 2010/11/16

SECONDARY ACCESSION(S): PRJNA130197

REPOSITORIES: GEO

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The cell envelope stress response mediated by the LiaFSRLm three-component system of Listeria monocytogenes is controlled via the phosphatase activity of the bifunctional histidine kinase LiaSLm

Project description:Most members of the phylum Firmicutes harbor a two-component system, LiaSR, which is involved in the response to cell envelope stress elicited most notably by inhibitors of the lipid II cycle. In all LiaSR systems studied in detail LiaSR-mediated signal transduction was shown to be negatively controlled by a membrane protein, LiaF, encoded upstream of liaSR. In this study we have analysed the LiaSR homolog of Listeria monocytogenes (LiaSRLm). Whole genome transcriptional profiling indicated that activation of LiaSRLm results in a remodeling of the cell envelope via the massive upregulation of membrane or cell-wall associated proteins in the presence of inducing stimuli. As shown for other LiaSR two-component systems LiaSRLm is activated by cell wall-active antibiotics. We demonstrate that the level of phosphorylated LiaRLm, which is required for the induction of the LiaSRLm regulon, is controlled by the interplay between histidine kinase and phosphatase activity of the bifunctional sensor protein LiaSLm. Our data suggest that the phosphatase activity of LiaSLm is stimulated by LiaF in the absence of cell envelope stress A total of three independently isolated RNA samples from each strain were used for the analysis.

2010-11-16 | E-GEOD-24107 | biostudies-arrayexpress

Depletion of undecaprenyl pyrophosphate phosphatases (UPP-Pases) disrupts cell envelope biogenesis in Bacillus subtilis

Project description:The integrity of the bacterial cell envelope is essential to sustain life by countering the high turgor pressure of the cell and providing a barrier against chemical insults. In Bacillus subtilis, synthesis of both peptidoglycan and wall teichoic acids requires a common C55 lipid carrier, undecaprenyl-pyrophosphate (UPP), to ferry precursors across the cytoplasmic membrane. The synthesis and recycling of UPP requires a phosphatase to generate the monophosphate form Und-P, which is the substrate for peptidoglycan and wall teichoic acid synthases. Using an optimized CRISPR-dCas9 based transcriptional repression system (CRISPRi), we demonstrate that B. subtilis requires either of two UPP phosphatases, UppP or BcrC, for viability. We show that a third predicted lipid phosphatase (YodM), with homology to diacylglycerol pyrophosphatases, can also support growth when overexpressed. Depletion of UPP phosphatase activity leads to morphological defects consistent with a failure of cell envelope synthesis and strongly activates the M-dependent cell envelope stress response, including bcrC which encodes one of the two UPP phosphatases. These results highlight the utility of an optimized CRISPRi system for investigation of synthetic lethal gene pairs, clarify the nature of the B. subtilis UPP-Pase enzymes, and provide further evidence linking the M regulon to cell envelope homeostasis pathways.

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LiaR-dependent gene expression contributes to antimicrobial responses in group A Streptococcus [RNA-seq]

Project description:The ability to sense and respond to host defenses is essential for pathogen survival. Some mechanisms involve two-component systems (TCS) that respond to host molecules, such as antimicrobial peptides (AMPs) and activate specific gene regulatory pathways to aid in survival. Alongside TCSs, bacteria coordinate cell division proteins, chaperones, cell wall sortases and secretory translocons at discrete locations within the cytoplasmic membrane, referred to as functional membrane microdomains (FMMs). In Group A Streptococcus (GAS), the FMM or “ExPortal” coordinates protein secretion, cell wall synthesis and sensing of AMP-mediated cell envelope stress via the LiaFSR three-component system. Previously we showed GAS exposure to a subset of AMPs (-defensins) activates the LiaFSR system by disrupting LiaF and LiaS co-localization in the ExPortal, leading to increased LiaR phosphorylation, expression of the transcriptional regulator SpxA2, and altered GAS virulence gene expression. The mechanisms by which LiaFSR integrates cell envelope stress with responses to AMP activity and virulence are not fully elucidated. Here, we show the LiaFSR regulon is comprised of genes encoding SpxA2 and three membrane-associated proteins: a PspC domain-containing protein (PCP), the lipoteichoic acid-modifying protein LafB and the membrane protein insertase YidC2. Our data show phosphorylated LiaR induces transcription of these genes via a conserved operator, whose disruption attenuates GAS virulence and increases susceptibility to AMPs in a manner primarily dependent on differential expression of SpxA2. Our work expands understanding of the LiaFSR regulatory network in GAS and identifies targets for further investigation of mechanisms of cell envelope stress tolerance contributing to GAS pathogenesis.

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LiaR-dependent gene expression contributes to antimicrobial responses in group A Streptococcus [ChIP-seq]

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Sigma(M) regulated genes under antibiotic stress (vancomycin)

Project description:Abstract of associated manuscript: The Bacillus subtilis extracytoplasmic function (ECF) sigma(M) factor is activated by cell envelope stress elicited by antibiotics, and by acid, heat, ethanol and superoxide stresses. Here, we have used several complementary approaches to identify genes controlled by sigma(M). In many cases, expression is only partially dependent on sigma(M) because of both overlapping promoter recognition with other ECF sigma factors and the presence of additional promoter elements. Genes regulated by sigma(M) have a characteristic pattern of induction in response to cell envelope-acting antibiotics as evidenced by hierarchical clustering analysis. sigma(M) also contributes to the expression of the Spx transcription factor and thereby indirectly regulates genes of the Spx regulon. Cell envelope stress responses also include regulons controlled by sigma(W), sigma(B) and several two-component regulatory systems (e.g. LiaRS, YycFG, BceRS). Activation of the sigma(M) regulon increases expression of proteins functioning in transcriptional control, cell wall synthesis and shape determination, cell division, DNA damage monitoring, recombinational repair and detoxification.

2008-12-05 | GSE13820 | GEO

A unique mode of cross regulation in a cell envelope stress signaling system [RNA-seq]

Project description:A multi-layered structure known as the cell envelope separates the controlled interior of Gram-negative bacteria from a fluctuating physical and chemical environment. Transcription of genes that determine cell envelope structure and function is commonly controlled by a class of environmental regulators known as two-component signal transduction systems (TCS), which are comprised of 1) sensor histidine kinases and 2) response regulators. To discover TCS genes that contribute to cell envelope function in the intracellular mammalian pathogen, Brucella ovis, we subjected a comprehensive collection of non-essential TCS mutants to compounds that disrupt cell membranes and the peptidoglycan cell wall. Our screen led to the discovery of three TCS proteins with unusual regulatory properties that coordinately function to confer resistance to cell envelope stress and to support B. ovis replication in the intracellular niche. This tripartite regulatory system consists of the conserved cell envelope regulator, CenR, and a previously uncharacterized TCS, EssRS. The CenR and EssR response regulators bind a shared set of sites on the B. ovis chromosomes to control transcription of an overlapping set of genes with cell envelope functions. CenR directly interacts with EssR and functions to stimulate phosphoryl transfer from the EssS kinase to EssR and control steady-state levels of EssR protein in the cell via a post-transcriptional mechanism. Our data provide evidence for a new mode of TCS cross-regulation in which a non-cognate response regulator both regulates activity and influences cellular levels of a cognate TCS system.

2023-05-30 | GSE229181 | GEO

A unique mode of cross regulation in a cell envelope stress signaling system [ChIP-seq]

2023-05-30 | GSE229120 | GEO

Differential Expression Analysis of a Histidine phosphotransferase RNAi mutant in Magnaporthe oryzae

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2022-02-09 | GSE192934 | GEO

The three-component system EsrISR regulates a cell envelope stress response in Corynebacterium glutamicum

Project description:When the cell envelope integrity is compromised, bacteria trigger signaling cascades that result in the production of proteins that counteract these extracytoplasmic stresses. Here, we show that the two-component system EsrSR regulates a cell envelope stress response in the Actinobacterium Corynebacterium glutamicum. The sensor kinase EsrS possesses an amino-terminal phage shock protein C (PspC) domain, a property that sets EsrSR apart from all other two-component systems characterized so far. An integral membrane protein, EsrI, whose gene is divergently transcribed to the esrSR gene locus and which interestingly also possesses a PspC domain, acts as an inhibitor of EsrSR under non-stress conditions. The EsrISR three-component system is activated among others by antibiotics inhibiting the lipid II cycle, such as bacitracin and vancomycin, and it orchestrates a broad regulon including the esrI-esrSR gene locus itself, genes encoding heat shock proteins, ABC transporters, and several putative membrane-associated or secreted proteins of unknown function. Among those, the ABC transporter encoded by cg3322-3320 was shown to be directly involved in bacitracin resistance of C. glutamicum. Since similar esrI-esrSR loci are present in a large number of actinobacterial genomes, EsrISR represents a novel type of stress-responsive systems whose components are highly conserved in the phylum Actinobacteria.

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2024-05-31 | GSE261583 | GEO

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