Cloning of the outer membrane high-affinity Fe(III)-pyochelin receptor of Pseudomonas aeruginosa

Ankenbauer, Robert G.

doi:10.1128/jb.174.13.4401-4409.1992

Cited by 35 publications

(27 citation statements)

References 42 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…1 (7, 37, 74, 75, 93, 94, 105, 111, 112). The cognate protein receptors located in the outer membrane for ferric pyochelin, ferric pyoverdine, and ferric enterobactin have now been identified (7,74,75). The ferric enterobactin receptor, PfeA, with a molecular mass of 78 kDa, shows homology with the corresponding enterobactin receptor, FepA, of E. coli, and an activator for this gene, Pfe, has been identified (31).…”

Section: Pyochelin Introductionmentioning

confidence: 99%

Genetics and Assembly Line Enzymology of Siderophore Biosynthesis in Bacteria

Crosa

Walsh

2002

Microbiol Mol Biol Rev

727

697

View full text Add to dashboard Cite

The regulatory logic of siderophore biosynthetic genes in bacteria involves the universal repressor Fur, which acts together with iron as a negative regulator. However in other bacteria, in addition to the Fur-mediated mechanism of regulation, there is a concurrent positive regulation of iron transport and siderophore biosynthetic genes that occurs under conditions of iron deprivation. Despite these regulatory differences the mechanisms of siderophore biosynthesis follow the same fundamental enzymatic logic, which involves a series of elongating acyl-S-enzyme intermediates on multimodular protein assembly lines: nonribosomal peptide synthetases (NRPS). A substantial variety of siderophore structures are produced from similar NRPS assembly lines, and variation can come in the choice of the phenolic acid selected as the N-cap, the tailoring of amino acid residues during chain elongation, the mode of chain termination, and the nature of the capturing nucleophile of the siderophore acyl chain being released. Of course the specific parts that get assembled in a given bacterium may reflect a combination of the inventory of biosynthetic and tailoring gene clusters available. This modular assembly logic can account for all known siderophores. The ability to mix and match domains within modules and to swap modules themselves is likely to be an ongoing process in combinatorial biosynthesis. NRPS evolution will try out new combinations of chain initiation, elongation and tailoring, and termination steps, possibly by genetic exchange with other microorganisms and/or within the same bacterium, to create new variants of iron-chelating siderophores that can fit a particular niche for the producer bacterium

show abstract

Section: Pyochelin Introductionmentioning

confidence: 99%

Genetics and Assembly Line Enzymology of Siderophore Biosynthesis in Bacteria

Crosa

Walsh

2002

Microbiol Mol Biol Rev

727

697

View full text Add to dashboard Cite

show abstract

“…On the other hand, the mechanism of Fe(III)-pyochelin transport in P. aeruginosa is not understood in detail. Three iron-regulated membrane proteins have been identiˆed for pyochelin: (1) a 14 kDa ferripyochelin binding protein, 13) (2) a¿90 kDa periplasmic-space protein, 14) and (3) a 75 kDa iron-regulated outer-membrane protein, 15,16) were detected. There are no reports on Fe(III)-pyochelin transport in P. ‰uorescens.…”

mentioning

confidence: 99%

Siderophore Production and Induction of Iron-regulated Proteins by a Microorganism from Rhizosphere of Barley

Terano¹,

Nomoto²,

Takase³

2002

Bioscience, Biotechnology, and Biochemistry

View full text Add to dashboard Cite

This study provides new information on the Fe uptake system capable of supporting growth of the organism. Pseudomonas ‰uorescens isolated from the rhizosphere of barley, a gramineous plant, produced a siderophore under iron-limiting conditions. Its chemical structure was identiˆed as pyochelin, on the basis of 1 H and 13 C NMR data of a stable methyl ester derivative. The same iron-limiting conditions induced a new set of outer membrane proteins (75 and 55 kDa), consistent with a siderophore-mediated iron-uptake system.

show abstract

“…Moreover, the presence of a second pyoverdine receptor, FpvB, in P. aeruginosa has recently been reported (21). Besides these two pyoverdine receptors and the characterized receptor for pyochelin (FptA) (2,27), this bacterium also produces receptors for heterologous iron sources: there are two receptors, PhuR and HasR, involved in the utilization of heme (44), and two, PfeA and PirA, that mediate the uptake of enterobactin (14,22). However, these receptors are probably just a small sample of the real iron acquisition potential of P. aeruginosa, because in silico analysis of its genome revealed an impressive total of 34 genes encoding putative TonB-dependent outer membrane receptors (11).…”

mentioning

confidence: 99%

The Heterologous Siderophores Ferrioxamine B and Ferrichrome Activate Signaling Pathways inPseudomonas aeruginosa

et al. 2006

View full text Add to dashboard Cite

Pseudomonas aeruginosa secretes two siderophores, pyoverdine and pyochelin, under iron-limiting conditions. These siderophores are recognized at the cell surface by specific outer membrane receptors, also known as TonB-dependent receptors. In addition, this bacterium is also able to incorporate many heterologous siderophores of bacterial or fungal origin, which is reflected by the presence of 32 additional genes encoding putative TonB-dependent receptors. In this work, we have used a proteomic approach to identify the inducing conditions for P. aeruginosa TonB-dependent receptors. In total, 11 of these receptors could be discerned under various conditions. Two of them are only produced in the presence of the hydroxamate siderophores ferrioxamine B and ferrichrome. Regulation of their synthesis is affected by both iron and the presence of a cognate siderophore. Analysis of the P. aeruginosa genome showed that both receptor genes are located next to a regulatory locus encoding an extracytoplasmic function sigma factor and a transmembrane sensor. The involvement of this putative regulatory locus in the specific induction of the ferrioxamine B and ferrichrome receptors has been demonstrated. These results show that P. aeruginosa has evolved multiple specific regulatory systems to allow the regulation of TonB-dependent receptors.In most environments, the amount of free iron (approximately 10 Ϫ9 M) is below the concentration required by most microorganisms for growth (49). To fulfill their requirements for iron, bacteria have developed several strategies, including (i) the reduction of ferric to ferrous ions, (ii) the direct acquisition of iron from host proteins, (iii) the secretion of highaffinity iron-chelating compounds, called siderophores, and (iv) the uptake of heterologous siderophores (23). The transport of (heterologous) siderophores and heme/hemophores through the outer membranes of gram-negative bacteria is an energy-dependent process that needs the function of the ExbBExbD-TonB system. This system transduces the proton-motive force of the cytoplasmic membrane to the high-affinity outer membrane receptors, which are therefore also known as TonBdependent receptors (48). The synthesis of siderophores and their transport systems is negatively regulated by the Fur repressor protein (18). In addition, some siderophore transport systems are also positively regulated by the presence of their cognate siderophores (12). This level of regulation often involves extracytoplasmic function (ECF) sigma factors (56). The ECF family of sigma factors constitutes a group of environmentally responsive transcriptional factors of the RpoD ( 70 ) family that control a wide range of bacterial functions (39). The ECF factors involved in the regulation of iron uptake systems have been classified as the iron starvation class of sigma factors (35). One well-studied example is ferric dicitrate uptake by Escherichia coli (10

show abstract

Cloning of the outer membrane high-affinity Fe(III)-pyochelin receptor of Pseudomonas aeruginosa

Cited by 35 publications

References 42 publications

Genetics and Assembly Line Enzymology of Siderophore Biosynthesis in Bacteria

Genetics and Assembly Line Enzymology of Siderophore Biosynthesis in Bacteria

Siderophore Production and Induction of Iron-regulated Proteins by a Microorganism from Rhizosphere of Barley

The Heterologous Siderophores Ferrioxamine B and Ferrichrome Activate Signaling Pathways inPseudomonas aeruginosa

Contact Info

Product

Resources

About