ArticleThe Journal of biological chemistry2015
Differential contributions of the outer membrane receptors PhuR and HasR to heme acquisition in Pseudomonas aeruginosa.
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 57 papers.
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Who cites it
57 citing papers in PubMed.
- A generalizable method for the purification and biophysical characterization of bacterial membrane receptors.Protein science : a publication of the Protein Society · 2026Article
- Identification of iron and zinc responsive TonB-dependent transporters in Pseudomonas aeruginosa.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2026Article
- The two-component system ColRS discriminates metal signals to regulate virulence and resistance in Pseudomonas aeruginosa.PLoS pathogens · 2026Article
- Metal-independent effects of calprotectin on cocultures ofbioRxiv : the preprint server for biology · 2026Article
- PhuS conformational dynamics are essential for DNA binding and heme-responsive control of the prrF operon in Pseudomonas aeruginosa.The Journal of biological chemistry · 2026Article
- Heme in Bacterial Pathogenesis and as an Antimicrobial Target.Chemical reviews · 2025Review
- Calprotectin protectsmSystems · 2025Article
- GaSal-2: A Water-Soluble Antipseudomonal Agent Targeting the Extracellular Hemophore HasAp.ACS infectious diseases · 2025Article
- Calprotectin-mediated survival ofmBio · 2025Article
- The Pseudomonas aeruginosa PhuS proximal ligand His-209 triggers a conformational switch in function from DNA binding to heme transfer.The Journal of biological chemistry · 2025Article
- Calprotectin elicits aberrant iron starvation responses inJournal of bacteriology · 2025Article
- Characterization of intact FeoB in a lipid bilayer using styrene-maleic acid (SMA) copolymers.Biochimica et biophysica acta. Biomembranes · 2025Article
- Involvement of HemI, an ECF sigma factor, in hemin acquisition and antibiotic susceptibility inFrontiers in cellular and infection microbiology · 2025Article
- Review
- Chaperone-assisted cryo-EM structure ofbioRxiv : the preprint server for biology · 2024Article
- Structural Determinants ofbioRxiv : the preprint server for biology · 2024Article
- Chaperone-assisted cryo-EM structure of P. aeruginosa PhuR reveals molecular basis for heme binding.Structure (London, England : 1993) · 2024Article
- Article
- The heme-responsive PrrH sRNA regulatesmSphere · 2023Article
- Iron acquisition strategies in pseudomonads: mechanisms, ecology, and evolution.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2023Review
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2 authors.
Funding
Abstract
Pseudomonas aeruginosa PAO1 encodes two outer membrane receptors, PhuR (Pseudomonas heme uptake) and HasR (heme assimilation system). The HasR and PhuR receptors have distinct heme coordinating ligands and substrate specificities. HasR is encoded in an operon with a secreted hemophore, HasAp. In contrast the non-hemophore-dependent PhuR is encoded within an operon along with proteins required for heme translocation into the cytoplasm. Herein we report on the contributions of the HasR and PhuR receptors to heme uptake and utilization. Employing bacterial genetics and isotopic [(13)C]heme labeling studies we have shown both PhuR and HasR are required for optimal heme utilization. However, the unique His-Tyr-ligated PhuR plays a major role in the acquisition of heme. In contrast the HasR receptor plays a primary role in the sensing of extracellular heme and a supplementary role in heme uptake. We propose PhuR and HasR represent non-redundant heme receptors, capable of accessing heme across a wide range of physiological conditions on colonization of the host.
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