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Unlabelled: In alginate biosynthesis gene expression is inhibited by the transmembrane anti-sigma factor MucA, which sequesters the AlgU sigma factor. Cell envelope stress initiates cleavage of the MucA periplasmic domain by site-1 protease AlgW, followed by further MucA degradation to release AlgU. However, after colonizing the lungs of people with cystic fibrosis, converts to a mucoid form that produces alginate constitutively. Mucoid isolates often have mutations, with the most common being , which truncates the periplasmic domain. MucA22 is degraded constitutively, and genetic studies suggested that the Prc protease is responsible. Some studies also suggested that Prc contributes to induction in strains with wild type MucA, whereas others suggested the opposite. However, missing from all previous studies is a demonstration that Prc cleaves any protein directly, which leaves open the possibility that the effect of a null mutation is indirect. To address the ambiguities and shortfalls, we reevaluated the roles of AlgW and Prc as MucA and MucA22 site-1 proteases. analyses using three different assays, and two different inducing conditions, all suggested that AlgW is the only site-1 protease for wild type MucA in any condition. In contrast, genetics suggested that AlgW or Prc act as MucA22 site-1 proteases in inducing conditions, whereas Prc is the only MucA22 site-1 protease in non-inducing conditions. For the first time, we also show that Prc is unable to degrade the periplasmic domain of wild type MucA, but does degrade the mutated periplasmic domain of MucA22 directly.
Importance: After colonizing the lungs of individuals with cystic fibrosis, undergoes mutagenic conversion to a mucoid form, worsening the prognosis. Most mucoid isolates have a truncated negative regulatory protein MucA, which leads to constitutive production of the extracellular polysaccharide alginate. The protease Prc has been implicated, but not shown, to degrade the most common MucA variant, MucA22, to trigger alginate production. This work provides the first demonstration that the molecular mechanism of Prc involvement is direct degradation of the MucA22 periplasmic domain, and perhaps other truncated MucA variants as well. MucA truncation and degradation by Prc might be the predominant mechanism of mucoid conversion in cystic fibrosis infections, suggesting that Prc activity could be a useful therapeutic target.
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http://dx.doi.org/10.1101/2024.05.28.596254 | DOI Listing |
Chemistry
December 2024
CEA lRlG: Commissariat a l'energie atomique et aux energies alternatives lnstitut de Recherche Interdisciplinaire de Grenoble, IRIG/SYMMES, FRANCE.
Maintaining tightly copper homeostasis is crucial for the survival of all living organisms, in particular microorganisms like bacteria. They have evolved a number of proteins to capture, transport and deliver Cu(I), while avoiding Fenton-like reactions. Some Cu proteins exhibit methionine-rich (Met-rich) domains, whose role remains elusive.
View Article and Find Full Text PDFBiotechnol Lett
December 2024
Department of Bioinformatics, BioNome, Bengaluru, Karnataka, 560043, India.
Objectives: Pseudomonas aeruginosa, identified as an ESKAPE pathogen, contributes to severe clinical diseases worldwide and despite its prevalence an effective vaccine or treatment remains elusive. Numerous computational methods are being employed to target hypothetical proteins (HPs). Presently, no studies have predicted multi-epitope vaccines for these HPs.
View Article and Find Full Text PDFJ Hazard Mater
December 2024
State Key Laboratory of Pollution Control and Resource Reuse, School of Environment, Nanjing University, Nanjing 210023, PR China. Electronic address:
Real-time monitoring of estrogenic activity in the aquatic environment is a challenging task. Current biosensors face difficulties due to their limited response speed and environmental tolerance, especially for detecting wastewater, the major source of estrogenic compounds in aquatic environments. To address these difficulties, this study developed a single fluorescent protein (FP) -based whole-cell bacterial biosensor named ER-Light, which was achieved by inserting the sensing domain of the estrogen receptor (ER) into the FP Citrine and expressing it in the periplasm of Escherichia coli.
View Article and Find Full Text PDFbioRxiv
December 2024
Department of Chemistry and Biochemistry, Florida State University, Tallahassee, FL 32306.
CrgA is a key transmembrane (TM) protein in the cell division process of (), the pathogen responsible for tuberculosis. While many of the divisome proteins have been identified, their structures and interactions remain largely unknown. Previous studies of CrgA using oriented-sample solid-state NMR have defined the tilt and rotation of the TM helices, but the cytoplasmic and periplasmic domains and even the oligomeric state were uncharacterized.
View Article and Find Full Text PDFMicrobiol Spectr
December 2024
Department of Medicine, Division of Infectious Diseases, Massachusetts General Hospital, Harvard Medical School, Boston, Massachusetts, USA.
Beta-lactam antibiotics are often the treatment of choice for serious bacterial infections. In a previous screen for novel genetic mediators affecting beta-lactam susceptibility, we discovered that deletion of , a conserved gene of unknown function, leads to increased resistance to beta-lactams, as well as increased susceptibility to detergent compounds. Here, we further characterize YdgH in , and using a combination of biochemical and cell biological approaches.
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