Iron acquisition with the natural siderophore enantiomers pyochelin and enantio-pyochelin in Pseudomonas species

Youard, Zeb A.; Wenner, Nicolas; Reimmann, Cornelia

doi:10.1007/s10534-010-9399-9

Cited by 80 publications

(131 citation statements)

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“…It is important to note here that both siderophores are synthetized through non-ribosomal peptide synthesis [11,12]. This means that an entire machinery of enzymes first needs to be produced, and only then are the siderophores assembled from amino acids and other chemical compounds.…”

Section: (E) Fitness Consequences Of Siderophore Switchingmentioning

confidence: 99%

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Switching between apparently redundant iron-uptake mechanisms benefits bacteria in changeable environments

2013

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Bacteria often possess multiple siderophore-based iron uptake systems for scavenging this vital resource from their environment. However, some siderophores seem redundant, because they have limited iron-binding efficiency and are seldom expressed under iron limitation. Here, we investigate the conundrum of why selection does not eliminate this apparent redundancy. We focus on Pseudomonas aeruginosa, a bacterium that can produce two siderophores-the highly efficient but metabolically expensive pyoverdine, and the inefficient but metabolically cheap pyochelin. We found that the bacteria possess molecular mechanisms to phenotypically switch from mainly producing pyoverdine under severe iron limitation to mainly producing pyochelin when iron is only moderately limited. We further show that strains exclusively producing pyochelin grew significantly better than strains exclusively producing pyoverdine under moderate iron limitation, whereas the inverse was seen under severe iron limitation. This suggests that pyochelin is not redundant, but that switching between siderophore strategies might be beneficial to trade off efficiencies versus costs of siderophores. Indeed, simulations parameterized from our data confirmed that strains retaining the capacity to switch between siderophores significantly outcompeted strains defective for one or the other siderophore under fluctuating iron availabilities. Finally, we discuss how siderophore switching can be viewed as a form of collective decision-making, whereby a coordinated shift in behaviour at the group level emerges as a result of positive and negative feedback loops operating among individuals at the local scale.

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Section: (E) Fitness Consequences Of Siderophore Switchingmentioning

confidence: 99%

“…) [12] than pyoverdine (K f ¼ 10 24 M 21 ) [11] and is less important for virulence [16]. Despite its apparent inferiority to pyoverdine under typical conditions, it has been suggested that under less stringent iron limitation, pyochelin might prove most useful [4].…”

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confidence: 99%

Switching between apparently redundant iron-uptake mechanisms benefits bacteria in changeable environments

2013

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“…Iron uptake with Pch and its regulation have been studied in detail and reviewed by Youard et al (2011). The genes responsible for Pch biosynthesis are organized in two operons, pchDCBA and pchEFGHI, which are located next to the pchR regulatory gene and to the ferriPch (iron-loaded form of Pch) transport operon fptABCX (Fig.…”

Section: Introductionmentioning

confidence: 99%

“…The genes for EPch biosynthesis in P. fluorescens are organized in a single transcriptional unit, pchDHIEFKCBA, which is clustered with pchR and a putative ferriEPch transport operon, fetABCDEF ( Fig. 1b; Youard et al, 2011). By analogy with P. aeruginosa, the PchR protein of P. fluorescens, together with EPch, activates expression of the pchDHIEFKCBA operon ( Fig.…”

Section: Introductionmentioning

confidence: 99%

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Inner-membrane transporters for the siderophores pyochelin in Pseudomonas aeruginosa and enantio-pyochelin in Pseudomonas fluorescens display different enantioselectivities

Reimmann

2012

Microbiology

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Iron uptake and transcriptional regulation by the enantiomeric siderophores pyochelin (Pch) and enantio-pyochelin (EPch) of Pseudomonas aeruginosa and Pseudomonas fluorescens, respectively, are stereospecific processes. The iron-loaded forms of Pch (ferriPch) and of EPch (ferriEPch) are recognized stereospecifically (i) at the outer membrane by the siderophore receptors FptA in P. aeruginosa and FetA in P. fluorescens and (ii) in the cytoplasm by the two AraC-type regulators PchR, which are activated by their cognate siderophore. Here, stereospecific siderophore recognition is shown to occur at the inner membrane also. In P. aeruginosa, translocation of ferriPch across the inner membrane is carried out by the singlesubunit siderophore transporter FptX. In contrast, the uptake of ferriEPch into the cytoplasm of P. fluorescens was found to involve a classical periplasmic binding protein-dependent ABC transporter (FetCDE), which is encoded by the fetABCDEF operon. Expression of a translational fetA-gfp fusion was repressed by ferric ions, and activated by the cognate siderophore bound to PchR, thus resembling the analogous regulation of the P. aeruginosa ferriPch transport operon fptABCX. The inner-membrane transporters FetCDE and FptX were expressed in combination with either of the two siderophore receptors FetA and FptA in a siderophore-negative P. aeruginosa mutant deleted for the fptABCX operon. Growth tests conducted under iron limitation with ferriPch or ferriEPch as the iron source revealed that FptX was able to transport ferriPch as well as ferriEPch, whereas FetCDE specifically transported ferriEPch. Thus, stereospecific siderophore recognition occurs at the inner membrane by the FetCDE transporter.

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Biological and Biomedical Aspects of Metal Phenolates

Ming

2014

Patai's Chemistry of Functional Groups

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The phenol functionality is involved in diverse biological processes and functions, serving as a proton donor and as a metal‐binding ligand. It is commonly found in many biochemicals (such as siderophores and the amino acids tyrosine and tryptophan), pharmaceuticals (including antibiotics, metal‐chelating agents, and diagnostic agents), and natural products (such as polyphenols, flavonoids, and salicylic acid). In association with other functional groups, the phenol moiety forms various types of metal‐binding sites of diverse structures and functions, for example, for iron binding and transport, in enzymes for oxygenation of substrates, and for biotransformation of aromatic compounds. Many environmentally hazardous aromatic compounds such as bisphenol A, PCB, and DDT can be degraded by tyrosinate(phenolate)‐containing metalloenzymes from microorganisms, which provides a clue for bioremediation of these toxic substances. Moreover, the phenol‐containing wet‐adhesive byssal proteins from some clams and mussels has stimulated further development of adhesive materials for medical and other applications; and the study of binding of transferrin with nanoparticles affords better understanding of protein–mineral interfacial interactions. In addition to these naturally occurring metal‐phenolate centers, there are many metal complexes of phenol and derivatives that exhibit various catalytic activities and serve as structural and/or functional model systems for tyrosinate‐containing metalloproteins.

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Iron acquisition with the natural siderophore enantiomers pyochelin and enantio-pyochelin in Pseudomonas species

Cited by 80 publications

References 61 publications

Switching between apparently redundant iron-uptake mechanisms benefits bacteria in changeable environments

Switching between apparently redundant iron-uptake mechanisms benefits bacteria in changeable environments

Inner-membrane transporters for the siderophores pyochelin in Pseudomonas aeruginosa and enantio-pyochelin in Pseudomonas fluorescens display different enantioselectivities

Biological and Biomedical Aspects of Metal Phenolates

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