Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Quorum sensing regulation by the nitrogen phosphotransferase system in Pseudomonas aeruginosa

ABSTRACT: This study was conducted to learn the transcriptional effects of deleting different components of the nitrogen-related phosphotransfer system (Nitro-PTS or PTS-Ntr) in Pseudomonas aeruginosa under infection-similar culture conditions using synthetic cystic fibrosis sputum medium (SCFM2). This system regulates a number of different genes and processes in different bacterial species, but few of its targets have been identified in P. aeruginosa. Because PtsP is required for PtsN phosphorylation, the ptsP mutant provides an opportunity to assess the impact of unphosphorylated PtsN (versus the ptsP ptsN double deletion). We also tested the transcriptional impact of adding 7.5 mM supplementary citrate to this medium. The different deletions showed distinct sets of differentially regulated genes that help yield insight into how the different components of the Nitro-PTS differentially influence expression. The results also aided in identifying previously unrecognized citrate transport proteins.

ORGANISM(S): Pseudomonas aeruginosa

PROVIDER: GSE297711 | GEO | 2025/05/20

REPOSITORIES: GEO

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
		Other

Items per page:

1 - 1 of 1

Similar Datasets

Effect of markerless deletion of ptsP from P. aeruginosa PA14 biofilm colonies on M6301-glycerol agar for 3 d at 25C

Project description:To determine the transcriptomic effect when ptsP, which encodes enzyme I of the nitrogen-related phosphotransfer system (Nitro-PTS), is absent from cells. Deletion of this gene results in lower exopolysaccharide levels (a biofilm defect). Here, we compared PA14 deleted for amrZ (which has a moderately hyper-biofilm phenotype) and cells deleted for both amrZ and ptsP. We also analyzed wild-type PA14 cells (see GSE226104).

2023-08-09 | GSE239971 | GEO

Identification of the major PEP-phosphotransferase systems (PTS) for glucose, mannose and cellobiose of L. monocytogenes

Project description:Identification of the major PEP-phosphotransferase systems (PTS) for glucose, mannose and cellobiose of Listeria monocytogenes, and their significance for extra- and intracellular growth. Transcriptional profile of prfA, the dependent genes and the PTS genes after growth in MM (minimal medium (Premaratne et al. 2001)) (supplemented with 10 mM Glucose). Listeria monocytogenes EGD-e possesses 86 pts genes encoding 29 complete and several incomplete PEP-dependent phosphotransferase systems (PTS) for the transport of carbohydrates and sugar alcohols. By a systematic deletion analysis we identified the major PTS involved in glucose, mannose and cellobiose transport, when L. monocytogenes grows in a defined minimal medium in the presence of either of these carbohydrates. Under these conditions two of the four PTSMan and at least one of the five PTSGlc function as glucose transporter with different affinities. Cellobiose is transported (with different efficiencies) mainly by two of the six PTSLac and by a PTSGlc that also transports glucose. One of the PTSMan and both PTSLac are regulated by LevR-homologous PRD containing transcriptional activators, detected with PRD deletion mutants. The growth rates of mutants that are lacking these PTS are drastically reduced compared to the wild-type strain upon growth in a defined medium with low concentrations of glucose and cellobiose, respectively. In contrast, replication of these PTS mutants within epithelial cells or macrophages is as efficient as that of the wild-type strain. Keywords: pts and prd deletion mutants

2009-12-01 | GSE18363 | GEO

Identification of the major PEP-phosphotransferase systems (PTS) for glucose, mannose and cellobiose of L. monocytogenes

2010-05-19 | E-GEOD-18363 | biostudies-arrayexpress

Proteome analysis of Escherichia coli ptsN-null strain under different nitrogen regimes

Project description:The carbohydrate-uptake phosphorelay PTS system plays a key role in metabolic regulation in Bacteria controlling the utilization of secondary carbon sources. Some Bacteria, such as Escherichia coli, encode a paralogue system named PTSNtr (nitrogen related PTS). PTSNtr is composed of EINtr (ptsP), NPr (ptsO), and EIIANtr (ptsN). These proteins act as a phosphorely system transfering phosphoryl from phosphoenolpyruvate to EINtr, NPr and them to EIIANtr. PTSNtr is not involved in carbohydrate uptake and it may be dedicated to play regulatory functions. The phosphorylation state of the EINtr is regulated by allosteric binding of glutamine and 2-oxoglutarate, metabolites whose intracellular levels reflect the nitrogen levels. Despite the denomination and nitrogen-sensory properties no major effect of PTSNtr on nitrogen regulation has been described in E. coli. Here we show that an E. coli ∆ptsN has impaired growth in minimal medium. Proteome analysis of the ∆ptsN strain under different nitrogen regimes revealed that ptsN is not involved in the regulation of the canonical nitrogen starvation response. The proteomic data support that ptsN is required for proper balance between RpoS and sigma 70 activities such that, in the absence of ptsN, RpoS-depended genes are preferentially expressed.

2018-09-13 | PXD008034 | Pride

Synbiotic impact of tagatose on viability of Lactobacillus rhamnosus strain GG mediated by the phosphotransferase system (PTS)

Project description:The presence of tagatose in Lactobacillus rhamnosus strain GG caused induction of a large number of genes associated with carbohydrate metabolism including the phosphotransferase system. In addition, these results indicate the tagatose enhanced the growth of Lactobacillus casei 01 and Lactobacillus rhamnosus strain GG and their probiotic activities by activating tagatose-associated PTS networks. Two-condition experiment, Lactobacillus rhamnosus GG with glucose vs. Lactobacillus rhamnosus GG with tagatose. For preparing the total RNA, Lactobacillus rhamnosus GG cells were grown at 37M-BM-0C in prebiotic minimum medium supplemented with 2% glucose or tagatose for 24 h.

2013-09-19 | E-GEOD-41073 | biostudies-arrayexpress

Identification and functional characterization of a fructose-inducible phosphotransferase system in Azospirillum brasilense Sp7

Project description:Plant growth promoting rhizobacterium Azospirillum brasilense Sp7 utilizes fructose efficiently via a fructose phosphotransferase system (Fru-PTS). Its genome encodes two putative Fru-PTS, each consisting of FruB (EIIA), FruK (Pfk) and FruA (EIIBC) proteins. We compared the proteomes of A. brasilense Sp7 grown with malate or fructose as sole carbon source, and observed upregulation of component proteins of Fru-PTS1 and several proteins involved in the biogenesis of the type 6 secretion system (T6SS) only on fructose.

2024-11-04 | PXD055876 | Pride

Functional dissection of the PTS provides insight into the prevalence of Faecalibacterium prausnitzii in the host intestinal environment

Project description:Faecalibacterium prausnitzii is a dominant member of healthy human colon microbiota, regarded as a beneficial gut bacterium due to its ability to produce anti-inflammatory substances. However, little is known about how F. prausnitzii utilizes the nutrients present in the human gut, influencing its prevalence in the host intestinal environment. The phosphoenolpyruvate (PEP):carbohydrate phosphotransferase system (PTS) is a widely distributed and highly efficient carbohydrate transport system found in most bacterial species that catalyses the simultaneous phosphorylation and import of cognate carbohydrates; its components play physiological roles through interaction with other regulatory proteins. Here, we performed a systematic analysis of the 16 genes encoding putative PTS components (2 enzyme I, 2 HPr, and 12 enzyme II components) in F. prausnitzii A2-165. We identified the general PTS components responsible for the PEP-dependent phosphotransfer reaction and the sugar-specific PTS components involved in the transport of two carbohydrates, N-acetylglucosamine and fructose, among five enzyme II complexes. We suggest that the dissection of the functional PTS in F. prausnitzii may help to understand how this species outcompetes other bacterial species in the human intestine.

2021-03-06 | GSE168352 | GEO

A controlled study of efficacy and safety in CT colonography preparation with Mosapride Citrate Hydrate

Project description:Interventions: Polyethylene glycol lavage solution plus contrast medium (PEG-C) preparation before CT colonography Polyethylene glycol lavage solution plus contrast medium and Mosapride Citrate Hydrate (PEG-CM) preparation before CT colonography Primary outcome(s): PEG-C versus PEG-C + Mosapride Citrate Hydrate for bowel preparation before CT colonography to be asscessed by the amount of residual fluid. Study Design: Parallel Randomized

| 2620536 | ecrin-mdr-crc

Ptp107 versus wild type Rlv3841

Project description:Strain PtsP107 has a Tn5 insertion in PtsP and it was grown on glucose/ ammonia minimal medium and gene expression compared to the wild type Rhizobium leguminosarum biovar viciae strain Rlv3841 grown on the same medium.

2011-09-23 | E-MEXP-3381 | biostudies-arrayexpress

The effect of citrate supplementation on medium viscosity and poly-γ-glutamic acid synthesis by engineered B. subtilis 168

Project description:The industrially attractive biopolymer Poly-γ-glutamic acid (γ-PGA) is commonly produced by species of the genus Bacillus by co-feeding different carbon- and nitrogen sources. Recent studies have highlighted the pivotal role of co-metabolization of a rapidly degradable carbon source such as glycerol together with citrate for γ-PGA production, independently fueling biomass generation as well as TCA cycle precursor supply. With this study, we report that the sole presence of citrate in the production medium greatly influences growth behavior, γ-PGA production, and the viscosity of microbial cultures during biopolymer synthesis. Independent of the citrate concentration in the medium. only minor amounts of citrate were imported by B. subtilis 168 in presence of glycerol due to carbon catabolite repression. However, a high citrate concentration resulted in a 6-fold increase in γ-PGA titer as compared to low levels of exogenous citrate. Data suggests that citrate was not used as a precursor in γ-PGA synthesis but rather influenced the fate of imported glutamate. The citrate concentration also affected medium viscosity as depletion resulted in a remarkable spike in broth viscosity. Additionally, cellular proteome analysis at different levels of citrate availability revealed significant changes in protein abundance involved in motility and fatty acid degradation

2025-02-10 | PXD058048 | Pride

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data