Reduction of Yield Depressions in High Frequency Potato Cropping Soil after Seed Tuber Treatments with Antagonistic Fluorescent <i>Pseudomonas</i> spp.

Geels, F.P.; Schippers, B.

doi:10.1111/j.1439-0434.1983.tb00580.x

Cited by 177 publications

(90 citation statements)

References 6 publications

(2 reference statements)

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“…In particular, we have focused on the earliest stage of biofilm formation, that is, attachment to a surface. We have chosen to study Pseudomonas fluorescens strain WCS365, a plant-beneficial root colonizer used as a biological control agent on a variety of crops (Geels and Schippers, 1983;Simons et al, 1996), as our model organism. Here, we report the isolation and phenotypic and molecular analyses of mutants defective in the initiation of biofilm formation.…”

Section: Introductionmentioning

confidence: 99%

Initiation of biofilm formation in Pseudomonas fluorescens WCS365 proceeds via multiple, convergent signalling pathways: a genetic analysis

O’Toole

Kolter

1998

Molecular Microbiology

2,273

1,795

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SummaryPopulations of surface-attached microorganisms comprising either single or multiple species are commonly referred to as biofilms. Using a simple assay for the initiation of biofilm formation (e.g. attachment to an abiotic surface) by Pseudomonas fluorescens strain WCS365, we have shown that: (i) P. fluorescens can form biofilms on an abiotic surface when grown on a range of nutrients; (ii) protein synthesis is required for the early events of biofilm formation; (iii) one (or more) extracytoplasmic protein plays a role in interactions with an abiotic surface; (iv) the osmolarity of the medium affects the ability of the cell to form biofilms. We have isolated transposon mutants defective for the initiation of biofilm formation, which we term surface attachment defective (sad ). Molecular analysis of the sad mutants revealed that the ClpP protein (a component of the cytoplasmic Clp protease) participates in biofilm formation in this organism. Our genetic analyses suggest that biofilm formation can proceed via multiple, convergent signalling pathways, which are regulated by various environmental signals. Finally, of the 24 sad mutants analysed in this study, only three had defects in genes of known function. This result suggests that our screen is uncovering novel aspects of bacterial physiology.

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Section: Introductionmentioning

confidence: 99%

Initiation of biofilm formation in Pseudomonas fluorescens WCS365 proceeds via multiple, convergent signalling pathways: a genetic analysis

O’Toole

Kolter

1998

Molecular Microbiology

2,273

1,795

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“…Strains used in this study include Escherichia coli DH5a (Hanahan, 1983), XL1-Blue (Bullock et al, 1987) and JMlOl (Messing, 1983). Pseudomonas putida WCS358 is a plant-growth-promoting strain isolated from the rhizosphere of potato roots (Geels & Schippers, 1983). …”

Section: Methodsmentioning

confidence: 99%

Genetics of ferulic acid bioconversion to protocatechuic acid in plant-growth-promoting Pseudomonas putida WCS358

et al. 1998

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Transposon Tn5 genomic mutants of plant-growth-promoting Pseudomonas putida strain WCS358 have been isolated which no longer utilize ferufic and coumaric acids as sole sources of carbon and energy. Genetic studies confirmed previous biochemical data showing that ferulic acid is degraded via vanillic acid, and coumaric acid via hydroxybenzoic acid. The genes involved in these enzymic steps were cloned and characterized. Two proteins designated Fca (26-5 kDa) and Vdh (50.3 kDa) were identified as responsible for the conversion of ferulic acid to vanillic acid; the proteins are encoded by the fca and vdh genes which are organized in an operon structure in the chromosome. The Vdh protein is 69% identical a t the amino acid level to the Vdh protein recently identified in Pseudomonas sp. strain HR199 and converts vanillin to vanillic acid. Homology studies revealed that the Vdh proteins exhibited significant identity to aldehyde dehydrogenases from different organisms whereas Fca belonged to the enoyl-CoA hydratase family of proteins. Two proteins, designated VanA (39.9 kDa) and VanB (343 kDa), encoded by two genes, vanA and van& are organized in an operon in the chromosome. They were found to be responsible for the demethylation of vanillic acid to protocatechuic acid. The VanA proteins showed no homology to any other known protein, while VanB belonged to the ferredoxin family of proteins. This two-component enzyme system demethylated another phenolic monomer, veratric acid, thus indicating broad specificity. Studies of the regulation of the vanAB operon demonstrated that the genes were induced by the substrate, vanillic acid; however, the strongest induction was observed when cells were grown in the presence of the product of the reaction, protocatechuic acid.

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“…We have investigated the pseudobactin 358-specific siderophore receptor with P. putida WCS358 and Pseudomonas fluorescens WCS374 (16). The structure of pseudobactin 374, the siderophore of WCS374, has been determined and differs considerably from that of pseudobactin 358 (G. A. J. M. van der Hofstad, unpublished results).…”

mentioning

confidence: 99%

“…Rhizosphere-colonizing Pseudomonas putida WCS358 (16) produces large quantities of the siderophore pseudobactin 358 when grown under iron-limited conditions (23). Pseudobactin 358 has a nine-amino-acid-long peptide which is attached to the fluorescent chromophore, and it contains three bidentate iron(III)-chelating groups (G. A. J. M. van der Hofstad et al, manuscript in preparation).…”

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confidence: 99%

Cloning and characterization of a gene encoding an outer membrane protein required for siderophore-mediated uptake of Fe3+ in Pseudomonas putida WCS358

et al. 1989

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In iron-limited environments plant-growth-stimulating Pseudomonas putida WCS358 produces a yellow- green Like most other bacteria, fluorescent pseudomonads possess a high-affinity iron uptake system that is used for growth in environments in which the amount of available iron is low. The system involves the synthesis and excretion of powerful iron(III)-chelating molecules, i.e., siderophores (25), the subsequent binding of the iron-siderophore complex by specific membrane-associated proteins, and the uptake of the iron cation. The different fluorescent pseudomonads produce pyoverdin-or pseudobactin-type siderophores which have very similar structures. Their structures consist of a fluorescent chromophore, a dihydroxyquinoline moiety linked to an oligopeptide 5 to 10 amino acids long. They differ mainly in amino acid composition and sequence (7,9,22,28).Rhizosphere-colonizing Pseudomonas putida WCS358 (16) Upon iron limitation new large outer membrane proteins with apparent molecular weights (MWs) between 70,000 and 100,000 are synthesized by fluorescent pseudomonads (8,11, 20,24 Construction of a gene bank. A partial Sau3A digest of genomic WCS358 DNA was fractionated as described previously (23). DNA fragments ranging from 15 to 35 kilobases (kb) were ligated in the BamHI site of pLAFR1B. The ligated DNA was packaged into lambda phage heads, followed by transduction of phage particles to E. coli HB101 as described previously (17,23).Tn5 mutagenesis. TnS mutagenesis of E. coli HB101 carrying cosmid pMR was carried out by the method of Shaw and Berg (27). Mutagenized cosmids were selected by isola- WCS358 and WCS374 were equally efficient in utilizing the iron from the Fe)3 X-pseudobactin 374 complex, whereas WCS358 was about four times more efficient than was WCS374 when it used its own siderophore.

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Reduction of Yield Depressions in High Frequency Potato Cropping Soil after Seed Tuber Treatments with Antagonistic Fluorescent Pseudomonas spp.

Cited by 177 publications

References 6 publications

Initiation of biofilm formation in Pseudomonas fluorescens WCS365 proceeds via multiple, convergent signalling pathways: a genetic analysis

Initiation of biofilm formation in Pseudomonas fluorescens WCS365 proceeds via multiple, convergent signalling pathways: a genetic analysis

Genetics of ferulic acid bioconversion to protocatechuic acid in plant-growth-promoting Pseudomonas putida WCS358

Cloning and characterization of a gene encoding an outer membrane protein required for siderophore-mediated uptake of Fe3+ in Pseudomonas putida WCS358

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