Pseudomonas bacteria are widespread and are found in soil and water, as well as pathogens of both plants and animals. The ability of Pseudomonas to colonize many different environments is facilitated by the multiple signaling systems these bacteria contain that allow Pseudomonas to adapt to changing circumstances by generating specific responses. Among others, signaling through extracytoplasmic function σ (σ ) factors is extensively present in Pseudomonas. σ factors trigger expression of functions required under particular conditions in response to specific signals. This manuscript reviews the phylogeny and biological roles of σ factors in Pseudomonas, and highlights the diversity of σ -signaling pathways of this genus in terms of function and activation. We show that Pseudomonas σ factors belong to 16 different phylogenetic groups. Most of them are included within the iron starvation group and are mainly involved in iron acquisition. The second most abundant group is formed by RpoE-like σ factors, which regulate the responses to cell envelope stress. Other groups controlling solvent tolerance, biofilm formation and the response to oxidative stress, among other functions, are present in lower frequency. The role of σ factors in the virulence of Pseudomonas pathogenic species is described.
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http://dx.doi.org/10.1111/mmi.14331 | DOI Listing |
PLoS Biol
December 2024
Department of Biotechnology and Environmental Protection, Estación Experimental del Zaidín-Consejo Superior de Investigaciones Científicas, Granada, Spain.
Competitive bacteria like the human pathogen Pseudomonas aeruginosa can acquire iron from different iron carriers, which are usually internalized via outer membrane TonB-dependent receptors (TBDRs). Production of TBDRs is promoted by the presence of the substrate. This regulation often entails a signal transfer pathway known as cell-surface signaling (CSS) that involves the TBDR itself that also functions as transducer (and is thus referred to as TBDT), a cytoplasmic membrane-bound anti-σ factor, and an extracytoplasmic function σ (σECF) factor.
View Article and Find Full Text PDFMedicina (Kaunas)
November 2024
Department of Anatomy, College of Medicine, University of Hail, Hail 55476, Hail, Saudi Arabia.
: ATP-binding cassette (ABC) transporters are prominent drug targets due to their highly efficient trafficking capabilities and their significant physiological and clinical roles. Gaining insight into their biophysical and biomechanistic properties is crucial to maximize their pharmacological potential. : In this study, we present the biochemical and biophysical characterization, and phylogenetic analysis of the domains of () ABC transporters: the exporter Rv1348 (IrtA) and the importer system Rv1349-Rv2895c (IrtB-Rv2895c), both involved in siderophore-mediated iron uptake.
View Article and Find Full Text PDFCommun Biol
November 2024
Institut für Mikrobiologie & Biotechnologie, Rheinische Friedrich-Wilhelms-Universität Bonn, Bonn, Germany.
Many sulfur-oxidizing prokaryotes oxidize sulfur compounds through a combination of initial extracytoplasmic and downstream cytoplasmic reactions. Facultative sulfur oxidizers adjust transcription to sulfur availability. While sulfur-oxidizing enzymes and transcriptional repressors have been extensively studied, sulfur import into the cytoplasm and how regulators sense external sulfur are poorly understood.
View Article and Find Full Text PDFNPJ Antimicrob Resist
November 2024
Centre for Bacterial Resistance Biology, Department of Life Sciences, Imperial College London, London, UK.
Antibiotic resistance is a global healthcare crisis. Bacteria are highly adaptable and can rapidly acquire mechanisms of resistance towards conventional antibiotics. The permeability barrier conferred by the Gram-negative bacteria cell envelope constitutes a first line of defence against the action of antibiotics.
View Article and Find Full Text PDFBiochimie
October 2023
Chemistry Department, Faculty of Science, Universidad Nacional de Colombia, Ciudad Universitaria, Bogotá, Colombia. Electronic address:
The functional difference among the three copper-transporting P-type ATPases (CtpA, CtpB, and CtpV) annotated in genome of Mycobacterium tuberculosis (Mtb) remains unclear. Thus, CtpA and CtpB are believed to deliver copper to extracytoplasmic proteins as a cofactor required to overcome redox and copper stress in the Mtb periplasm. This study investigates an alternative role of CtpA-mediated copper transportation and its possible interaction with the activity of the multicopper oxidase, (MmcO), in response to redox stress.
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