Siderophores and outer membrane proteins of antagonistic, plant-growth-stimulating, root-colonizing Pseudomonas spp

Weger, Letty A. de; Boxtel, Ria van; Burg, Bart van der; Gruters, R A; Geels, F.P.; Schippers, B.; Lugtenberg, Ben

doi:10.1128/jb.165.2.585-594.1986

Cited by 124 publications

(87 citation statements)

References 37 publications

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“…It has already been demonstrated that for R meliloti 1021 siderophore production is not essential for nodule formation and nitrogen fixation, although it may significantly increase the efficiency of this process (14). Siderophore-mediated competition for iron in microbial systems appears to be a widespread phenomenon (5,(8)(9)(10)41), and it therefore seems likely that siderophores produced by Rhizobium strains could play a role in competition in a manner similar to that of siderophores in the pseudomonads. It Finally, the results presented here strongly indicate that in Rhizobium spp.…”

Section: Resultsmentioning

confidence: 99%

Siderophore-mediated iron transport correlates with the presence of specific iron-regulated proteins in the outer membrane of Rhizobium meliloti

Reigh

O’Connell

1993

J Bacteriol

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A universal chemical assay used to detect the production of siderophores in a range of Rhizobium strains showed that production is strain specific. Iron nutrition bioassays carried out on Rhizobium meliloh strains to determine cross-utilization of their siderophores showed that R. melilod 2011, 220-5, and 220-3 could each use the siderophores produced by the other two but not the siderophore produced by R. melilot DM4 (and vice versa). Mutants of R. meliloti 2011 and 220-5 defective in siderophore production were isolated by TnS-mob mutagenesis. The TnS-mob-containing EcoRI fragment of mutant R. melilot 220-5-1 was cloned into pUC19. By using this fragment as a probe, the presence of a homologous region was observed in R. melilti 2011 and 220-3 but not in R. melilod DM4. A complementing cosmid from a gene bank of R. melilot 2011 was identified by using the same probe. Introduction of this cosmid into R. meliloti 102F34, a strain not producing a siderophore, resulted in the ability of this strain to produce a siderophore and also in the ability to utilize the siderophores produced by R. meliloti 2011, 220-5, and 220-3 but not the siderophore produced by R. meliloti DM4. A comparative analysis of the outer membrane proteins prepared from iron-deficient cultures of R. meliloti 102F34 and 102F34 harboring the cosmid revealed the presence, in the latter, of a low-iron-induced outer membrane protein corresponding to a low-iron-induced protein in R. meliloti 2011, 220-5, and 220-3. This protein is not present in R. melilot DM4. The results suggest that R. melilot 2011, and 220-3 produce siderophores that are identical or sufficiently similar in structure to be transported by the membrane transport system of each strain while also indicating that utilization of a particular siderophore is correlated with the presence of specific outer membrane proteins.

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Section: Resultsmentioning

confidence: 99%

Siderophore-mediated iron transport correlates with the presence of specific iron-regulated proteins in the outer membrane of Rhizobium meliloti

Reigh

O’Connell

1993

J Bacteriol

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“…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). The presence of such iron-regulated proteins in the outer membrane suggests that they are involved in high-affinity siderophore-mediated Fe3" uptake (26).…”

mentioning

confidence: 99%

“…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).…”

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confidence: 99%

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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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“…High-molecular-weight iron-regulated proteins (80K to 88K) have been identified in the Pseudomonas fluorescens-related strain B10 (38,39). Large iron-regulated proteins have also been demonstrated in the outer membranes of various root-colonizing strains of fluorescent pseudomonads (18), in Pseudomonas aeruginosa PAO1 (48), and in Pseudomonas syringae pv. syringae (17).…”

Section: Discussionmentioning

confidence: 99%

Structural and chemical characterization of the S layer of a Pseudomonas-like bacterium

1990

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Sections and freeze-fractured preparations showed an S layer on the surface ofPseudomonas-like strain EU2. Polyacrylamide gel electrophoresis of cell envelopes extracted with 1% sodium dodecyl sulfate (SDS) at room temperature showed three proteins (45K, 55K, and 110K). The 55K protein was identified as the S-layer protein. Incubation in 1.5 M guanidine hydrochloride removed the S layer from cell envelopes and dissociated the structure into subunits. The soluble 55K protein reassembled into planar sheets upon removal of the guanidine hydrochloride by dialysis. Electron microscopy and image processing indicated that these sheets had p4 symmetry in projection with a lattice constant of 13.2 ± 0.1 nm (corresponding to 9.3 nm between adjacent fourfold axes). In some instances these reassemblies appeared to form small three-dimensional crystals which gave particularly clear views of the structure in projection because of the superimposition of information from a number of layers. A model is proposed with molecules having rounded lobes connected by a narrower linker region and joining at the lobes to form the fourfold axes of the array. The pattern superficially resembles those of other bacterial S layers, such as those of Aeromonas salmonicida, Aeromonas hydrophila, and Azotobacter vinelandii. Extraction of cell envelopes with 1% SDS at 50°C released the 110K protein from the envelopes and removed an amorphous backing layer from the S layer. The 45K protein displayed heat-modifiable migration in SDS-polyacrylamide gel electrophoresis and was insoluble in SDS at 50°C or in high concentrations of guanidine hydrochloride, suggesting that it was associated with the peptidoglycan.S layers form regular arrays on the external surfaces of many bacteria. These layers often consist of the highestmolecular-weight protein in cells possessing such layers, and that protein is present in higher amounts than any other cellular protein. They may also perform important protective functions in the bacteria, possibly related to their forming a barrier to molecules (enzymes) and predators (35). S layers have also been suggested to form specific cell-cell connections involving alignment of the pores to form continuous channels between cells (5). They are found in a wide variety of eubacteria and archaebacteria (35,(45)(46)(47) and are arranged in p2, p4, or p6 symmetry with lattice spacings ranging from 2.8 to 35 nm. The protein subunits range in molecular weight from 13,000 to 255,000 (45, 46) and assemble in multimeric units, usually held together by noncovalent bonds including hydrogen bonds, hydrophobic bonds, and ionic bonds (45,46). Determination of the three-dimensional structure of S layers is becoming increasingly common (30) and reveals a high degree of variability of structure on the outer surfaces, whereas the inner surfaces of S layers tend to be more conserved (4), at least to the ca. 2-nm resolution of these studies.Although S layers have been recognized in a great number of species from most phylogenetic lines, very few S ...

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Siderophores and outer membrane proteins of antagonistic, plant-growth-stimulating, root-colonizing Pseudomonas spp

Cited by 124 publications

References 37 publications

Siderophore-mediated iron transport correlates with the presence of specific iron-regulated proteins in the outer membrane of Rhizobium meliloti

Siderophore-mediated iron transport correlates with the presence of specific iron-regulated proteins in the outer membrane of Rhizobium meliloti

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

Structural and chemical characterization of the S layer of a Pseudomonas-like bacterium

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