ArticleThe Journal of biological chemistry2015
Self-cleavage of the Pseudomonas aeruginosa Cell-surface Signaling Anti-sigma Factor FoxR Occurs through an N-O Acyl Rearrangement.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed.
- Cleavage cascade of the sigma regulator FecR orchestrates TonB-dependent signal transduction.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Bacterial TonB-dependent transducers interact with the anti-σ factor in absence of the inducing signal protecting it from proteolysis.PLoS biology · 2024Article
- The role of FoxA, FiuA, and FpvB in iron acquisition via hydroxamate-type siderophores in Pseudomonas aeruginosa.Scientific reports · 2024Article
- Insight into the autoproteolysis mechanism of the RsgI9 anti-σ factor from Clostridium thermocellum.Proteins · 2024Article
- Article
- Essential autoproteolysis of bacterial anti-σ factor RsgI for transmembrane signal transduction.Science advances · 2023Article
- Interactions of TonB-dependent transporter FoxA with siderophores and antibiotics that affect binding, uptake, and signal transduction.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Transcription regulation of iron carrier transport genes by ECF sigma factors through signaling from the cell surface into the cytoplasm.FEMS microbiology reviews · 2022Article
- Histamine: A Bacterial Signal Molecule.International journal of molecular sciences · 2021Review
- A wide-ranging Pseudomonas aeruginosa PeptideAtlas build: A useful proteomic resource for a versatile pathogen.Journal of proteomics · 2021Article
- Extracellular haem utilization by the opportunistic pathogen Pseudomonas aeruginosa and its role in virulence and pathogenesis.Advances in microbial physiology · 2021Article
- Structural basis of cell-surface signaling by a conserved sigma regulator in Gram-negative bacteria.The Journal of biological chemistry · 2020Article
- RskA Is a Dual Function Activator-Inhibitor That Controls SigK Activity Across Distinct Bacterial Genera.Frontiers in microbiology · 2020Article
- New Insights into the Regulation of Cell-Surface Signaling Activity Acquired from a Mutagenesis Screen of theFrontiers in microbiology · 2017Article
- Mechanistic Implications of the Unique Structural Features and Dimerization of the Cytoplasmic Domain of the Pseudomonas Sigma Regulator, PupR.Biochemistry · 2015Article
- The Escherichia coli S2P intramembrane protease RseP regulates ferric citrate uptake by cleaving the sigma factor regulator FecR.The Journal of biological chemistryArticle
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5 authors.
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No grant is acknowledged in the PubMed record.
Abstract
The Fox system of Pseudomonas aeruginosa is a cell-surface signaling (CSS) pathway employed by the bacterium to sense and respond to the presence of the heterologous siderophore ferrioxamine in the environment. This regulatory pathway controls the transcription of the foxA ferrioxamine receptor gene through the extracytoplasmic function sigma factor σ(FoxI). In the absence of ferrioxamine, the activity of σ(FoxI) is inhibited by the transmembrane anti-sigma factor FoxR. Upon binding of ferrioxamine by the FoxA receptor, FoxR is processed by a complex proteolytic cascade leading to the release and activation of σ(FoxI). Interestingly, we have recently shown that FoxR undergoes self-cleavage between the periplasmic Gly-191 and Thr-192 residues independent of the perception of ferrioxamine. This autoproteolytic event, which is widespread among CSS anti-sigma factors, produces two distinct domains that interact and function together to transduce the presence of the signal. In this work, we provide evidence that the self-cleavage of FoxR is not an enzyme-dependent process but is induced by an N-O acyl rearrangement. Mutation analysis showed that the nucleophilic side chain of the Thr-192 residue at +1 of the cleavage site is required for an attack on the preceding Gly-191, after which the resulting ester bond is likely hydrolyzed. Because the cleavage site is well preserved and the hydrolysis of periplasmic CSS anti-sigma factors is widely observed, we hypothesize that cleavage via an N-O acyl rearrangement is a conserved feature of these proteins.
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