The ferrichrome uptake pathway in Pseudomonas aeruginosa involves an iron release mechanism with acylation of the siderophore and recycling of the modified desferrichrome
| Autor: | Yaniv Barda, Gaëtan L. A. Mislin, Isabelle J. Schalk, Abraham Shanzer, Mélissa Hannauer |
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| Přispěvatelé: | Biotechnologie et signalisation cellulaire (BSC), Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Institut de recherche de l'Ecole de biotechnologie de Strasbourg (IREBS) |
| Rok vydání: | 2010 |
| Předmět: |
Siderophore
Acylation Iron Physiology and Metabolism Biology medicine.disease_cause Microbiology 03 medical and health sciences chemistry.chemical_compound Bacterial Proteins medicine Inner membrane Molecular Biology Escherichia coli 030304 developmental biology Ferrichrome 0303 health sciences Pyoverdine 030306 microbiology Pseudomonas aeruginosa Permease Membrane Transport Proteins Sciences du Vivant [q-bio]/Microbiologie et Parasitologie [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology Biochemistry chemistry Bacterial outer membrane Metabolic Networks and Pathways |
| Zdroj: | Journal of Bacteriology Journal of Bacteriology, American Society for Microbiology, 2010, 192 (5), pp.1212-1220. ⟨10.1128/JB.01539-09⟩ |
| ISSN: | 1098-5530 0021-9193 |
| DOI: | 10.1128/JB.01539-09⟩ |
| Popis: | The uptake of iron into Pseudomonas aeruginosa is mediated by two major siderophores produced by the bacterium, pyoverdine and pyochelin. The bacterium is also able of utilize several heterologous siderophores of bacterial or fungal origin. In this work, we have investigated the iron uptake in P. aeruginosa PAO1 by the heterologous ferrichrome siderophore. 55 Fe uptake assays showed that ferrichrome is transported across the outer membrane primarily (80%) by the FiuA receptor and to a lesser extent (20%) by a secondary transporter. Moreover, we demonstrate that like in the uptake of ferripyoverdine and ferripyochelin, the energy required for both pathways of ferrichrome uptake is provided by the inner membrane protein TonB1. Desferrichrome- 55 Fe uptake in P. aeruginosa was also dependent on the expression of the permease FiuB, suggesting that this protein is the inner membrane transporter of the ferrisiderophore. A biomimetic fluorescent analogue of ferrichrome, RL1194, was used in vivo to monitor the kinetics of iron release from ferrichrome in P. aeruginosa in real time. This dissociation involves acylation of ferrichrome and its biomimetic analogue RL1194 and recycling of both modified siderophores into the extracellular medium. FiuC, an N -acetyltransferase, is certainly involved in this mechanism of iron release, since its mutation abolished desferrichrome- 55 Fe uptake. The acetylated derivative reacts with iron in the extracellular medium and is able to be taken up again by the cells. All these observations are discussed in light of the current knowledge concerning ferrichrome uptake in P. aeruginosa and in Escherichia coli . |
| Databáze: | OpenAIRE |
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