Self-cleavage of the Pseudomonas aeruginosa Cell-surface Signaling Anti-sigma Factor FoxR Occurs through an N-O Acyl Rearrangement*
Explore this paper's citation graph
Summary
Evidence is provided that the self-cleavage of FoxR is not an enzyme-dependent process but is induced by an N-O acyl rearrangement, a conserved feature of these proteins.
- Type
- article
- Published
- 2015-03-25
- Cited by
- 27
- References
- 57
- OpenAlex
- https://openalex.org/W25809487
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:14254066
Keywords
Humanities, Philosophy
References
- The Prc and RseP proteases control bacterial cell-surface signalling activity.
- Cell-surface signaling in Pseudomonas: stress responses, iron transport, and pathogenicity.
- Processing of cell-surface signalling anti-sigma factors prior to signal recognition is a conserved autoproteolytic mechanism that produces two functional domains.
- Nuclear magnetic resonance solution structure of the periplasmic signalling domain of the TonB‐dependent outer membrane transporter FecA from Escherichia coli
- Differential proteolysis of sigma regulators controls cell‐surface signalling in Pseudomonas aeruginosa
- Analysis of the Pseudomonas aeruginosa major outer membrane protein OprF by use of truncated OprF derivatives and monoclonal antibodies
- Recognition of iron‐free siderophores by TonB‐dependent iron transporters
- The Heterologous Siderophores Ferrioxamine B and Ferrichrome Activate Signaling Pathways in Pseudomonas aeruginosa
- Iron acquisition and its control in Pseudomonas aeruginosa: many roads lead to Rome.
- Gene Regulation by Transmembrane Signaling
- Conformational constraints for protein self-cleavage in the proteasome.
- Protein splicing and autoproteolysis mechanisms.
- Signal transduction pathway of TonB-dependent transporters
- Three-dimensional structure of human lysosomal aspartylglucosaminidase
- The chemical basis of protein splicing
- Structural basis of gating by the outer membrane transporter FecA.
- Structure–function relationships in the bifunctional ferrisiderophore FpvA receptor from Pseudomonas aeruginosa
- Structural comparison of Ntn‐hydrolases
- Protein splicing: evidence for an N-O acyl rearrangement as the initial step in the splicing process.
- Dali server: conservation mapping in 3D
Cited by
- Mechanistic implications of the unique structural features and dimerization of the cytoplasmic domain of the Pseudomonas sigma regulator, PupR
- New Insights into the Regulation of Cell-Surface Signaling Activity Acquired from a Mutagenesis Screen of the Pseudomonas putida IutY Sigma/Anti-Sigma Factor
- Influence of the Hfq and Crc global regulators on the control of iron homeostasis in Pseudomonas putida
- Diversity of extracytoplasmic function sigma (σECF) factor‐dependent signaling in Pseudomonas
- Pseudomonas aeruginosa possesses three distinct systems for sensing and using the host molecule heme.
- Structural basis of cell-surface signaling by a conserved sigma regulator in Gram-negative bacteria
- Extracellular Heme Uptake and the Challenge of Bacterial Cell Membranes.
- RskA Is a Dual Function Activator-Inhibitor That Controls SigK Activity Across Distinct Bacterial Genera
- A wide-ranging Pseudomonas aeruginosa PeptideAtlas build: a useful proteomic resource for a versatile pathogen
- Escherichia coli S2P family intramembrane protease RseP is engaged in the regulated sequential cleavages of FecR in the ferric citrate signaling
- The Escherichia coli S2P intramembrane protease RseP regulates ferric citrate uptake by cleaving the sigma factor regulator FecR
- Histamine: A Bacterial Signal Molecule
- Humic acid enhanced pyrene degradation by Mycobacterium sp. NJS-1.
- Host-mediated susceptibility of Pseudomonas aeruginosa to azithromycin
- Up-regulation of ribosomal and carbon metabolism proteins enhanced pyrene biodegradation in fulvic acid-induced biofilm system.
- Extracellular Haem Utilization by the Opportunistic Pathogen Pseudomonas aeruginosa and its Role in Virulence and Pathogenesis
- A single extracellular loop of FoxA controls ligand specificity, uptake, and signaling in Pseudomonas aeruginosa
- The carboxyl-terminal processing proteases Prc and CtpA modulate cell-surface signalling activity and Pseudomonas aeruginosa virulence
- Interactions of TonB-dependent transporter FoxA with siderophores and antibiotics that affect binding, uptake, and signal transduction
- The Prc and CtpA proteases modulate cell-surface signaling activity and virulence in Pseudomonas aeruginosa
Related papers
No related papers recorded.