Nucleotide sequence analysis and potential environmental distribution of a ferric pseudobactin receptor gene of Pseudomonas sp. strain M114

Morris, J. Carrell; Donnelly, Daniel F.; O'Neill, Elaine; McConnell, Fiona I.; O’Gara, Fergal

doi:10.1007/bf00277342

Cited by 23 publications

(2 citation statements)

References 40 publications

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“…Hybridization studies suggest that homologues are present in a variety of P. aeruginosa strains as well as in P. aureofaciens, P. putida and P. fluorescens (129), and, indeed, receptors for ferric pseudobactin have been cloned and sequenced from P. putida WCS368 ( pupA) (137) and Pseudomonas fluorescens M114 ( pbuA) (138).…”

Section: Transportmentioning

confidence: 99%

Iron acquisition and its control in pseudomonas aeruginosa many roads lead to rome

Poole

McKay²

2003

Front Biosci

222

189

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Iron plays an important role in the pathogenesis and rhizosphere competence of the fluorescent group of pseudomonads and it is, thus, fitting that the characteristic fluorescence of these organisms is attributable to an iron-chelating molecule, pyoverdine. Pseudomonas aeruginosa is likely the best-studied member of this group, and while it synthesizes two siderophores, pyochelin and pyoverdine, it is also able to use a number of heterologous siderophores of fungal and bacterial origin and its genome is rich with homologues of iron-siderophore receptor genes, reflecting the enormous flexibility of the organism vis-a-vis iron carriers that it can use in nature. The ability to utilize a variety of heterologous siderophores is shared by other fluorescent pseudomonads and likely reflects both the importance of this vital nutrient for growth and survival and the need to compete with other microorganisms in the aquatic and terrestrial environments that they inhabit. Expression of the various receptors is, however, regulated, with receptor production responding positively to available siderophores only, and selection from multiple available siderophores based on their successful chelation of iron and subsequent transport. Thus, the superior siderophore in a given environment will upregulate the cognate receptor at the expense of other receptors. Such siderophore-dependent regulation of receptor gene expression is common in bacteria, particularly the fluorescent pseudomonads, and typically requires a signal transduction cascade that involves the receptor itself, whose binding to the siderophore initiates the cascade, as well as a regulatory protein pair that includes an environmentally-responsive so-called extracytoplasmic function (ECF) sigma factor, which activates receptor gene expression, and an anti-sigma factor that controls sigma factor activity. Despite the plethora of ferric siderophore receptors in P. aeruginosa, its genome sequence reveals a striking lack of obvious periplasmic and cytoplasmic membrane transport components capable of accommodating these molecules. Unlike e.g. Escherichia coli, then, where ferric siderophore permeases providing transport to the cytoplasm are clearly in evidence, iron-siderophore complexes in P. aeruginosa may be dissociated in the periplasm, with a common iron carrier then responsible for iron uptake into the cell interior.

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Section: Transportmentioning

confidence: 99%

Iron acquisition and its control in pseudomonas aeruginosa many roads lead to rome

Poole

McKay²

2003

Front Biosci

222

189

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“…While data accumulate concerning the complex regulation of siderophoremediated high-affinity iron uptake in fluorescent pseudomonads (recently reviewed by Venturi et al, 1995), less is known concerning the biosynthesis of pyoverdine and the mechanism of its excretion. The study of pyoverdine transport has focused mainly on the uptake of the ferric siderophore (Meyer et al, 1990;Poole et al, 1990;Bitter et al, 1991;Ankenbauer and Quan, 1994;Morris et al, 1994) rather than on its excretion. This is probably due to the difficulty of obtaining a siderophore-excretion mutant, which could be non-viable (Poole et al, 1993).…”

Section: Introductionmentioning

confidence: 99%

**A cytochrome c biogenesis gene involved in pyoverdine production in Pseudomonas fluorescens ATCC 17400**

Gaballa

Koedam

Cornélis

1996

Molecular Microbiology

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Pseudomonas fluorescens ATCC 17400 produces pyoverdine under iron-limiting conditions. A Tn5 mutant, 2G11, produced lower amounts of different pyoverdine forms and was unable to grow under iron limitation caused by ethylenediamine-di(o-hydroxy-phenylacetic acid) (EDDHA) or zinc. This mutant was complemented by a 9.6 kb HindIII-BamHI DNA fragment that contained eight contiguous open reading frames (ORFs cytA to cytH). The proteins possibly encoded by this polycistronic gene cluster were all similar to the products of cytochrome c biogenesis genes from, amongst others, Rhodobacter capsulatus and Bradyrhizobium japonicum, not only in terms of amino acid sequence, but also in the overall hydropathy index of these proteins. By TnphoA mutagenesis and site-specific gene replacement it was found that the first three ORFs (cytA to cytC) were essential for cytochrome c production while only the product of cytA was needed for normal pyoverdine production. The presence of a putative haem-binding site in the CytA protein (WGSWWVWD) was confirmed. From analysis of a constructed phoA fusion, a periplasmic location was found for this motif. The ability of the cytA gene to restore both cytochrome c and pyoverdine production suggests the involvement of this particular gene both in haem and in pyoverdine transport in P. fluorescens.

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New Insights on Iron Acquisition Mechanisms in Pathogenic Pseudomonas

Schalk¹

Pseudomonas

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Nucleotide sequence analysis and potential environmental distribution of a ferric pseudobactin receptor gene of Pseudomonas sp. strain M114

Cited by 23 publications

References 40 publications

Iron acquisition and its control in pseudomonas aeruginosa many roads lead to rome

Iron acquisition and its control in pseudomonas aeruginosa many roads lead to rome

**A cytochrome c biogenesis gene involved in pyoverdine production in Pseudomonas fluorescens ATCC 17400**

New Insights on Iron Acquisition Mechanisms in Pathogenic Pseudomonas

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