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DC Field | Value | Language |
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dc.contributor.author | Hartney, Sierra L. | - |
dc.contributor.author | Mazurier, Sylvie | - |
dc.contributor.author | Girard, Maëva K. | - |
dc.contributor.author | Mehnaz, Samina | - |
dc.contributor.author | Davis II, Edward W. | - |
dc.contributor.author | Gross, Harald | - |
dc.contributor.author | Lemanceau, , Philippe | - |
dc.contributor.author | Loper, Joyce E. | - |
dc.date.accessioned | 2021-03-08T07:57:27Z | - |
dc.date.available | 2021-03-08T07:57:27Z | - |
dc.date.issued | 2012-12-07 | - |
dc.identifier.citation | J. Bacteriol. 2013, 195(4):765. DOI: 10.1128/JB.01639-12. | en_US |
dc.identifier.other | DOI: 10.1128/JB.01639-12. | - |
dc.identifier.uri | http://localhost:8080/xmlui/handle/123456789/1089 | - |
dc.description.abstract | The soil bacterium Pseudomonas protegens Pf-5 (previously called P. fluorescens Pf-5) produces two siderophores, enantio-pyo chelin and a compound in the large and diverse pyoverdine family. Using high-resolution mass spectroscopy, we determined the structure of the pyoverdine produced by Pf-5. In addition to producing its own siderophores, Pf-5 also utilizes ferric complexes of some pyoverdines produced by other strains of Pseudomonas spp. as sources of iron. Previously, phylogenetic analysis of the 45 TonB-dependent outer membrane proteins in Pf-5 indicated that six are in a well-supported clade with ferric-pyoverdine re ceptors (Fpvs) from other Pseudomonas spp. We used a combination of phylogenetics, bioinformatics, mutagenesis, pyoverdine structural determinations, and cross-feeding bioassays to assign specific ferric-pyoverdine substrates to each of the six Fpvs of Pf-5. We identified at least one ferric-pyoverdine that was taken up by each of the six Fpvs of Pf-5. Functional redundancy of the Pf-5 Fpvs was also apparent, with some ferric-pyoverdines taken up by all mutants with a single Fpv deletion but not by a mutant having deletions in two of the Fpv-encoding genes. Finally, we demonstrated that phylogenetically related Fpvs take up ferric complexes of structurally related pyoverdines, thereby establishing structure-function relationships that can be employed in the future to predict the pyoverdine substrates of Fpvs in other Pseudomonas spp. | en_US |
dc.language.iso | en | en_US |
dc.publisher | Journals.ASM.org | en_US |
dc.relation.ispartofseries | J. Bacteriol. 2013, 195(4):765.; | - |
dc.subject | Proteins | en_US |
dc.subject | Pseudomonas | en_US |
dc.subject | Ferric-Pyoverdine | en_US |
dc.subject | protegens | en_US |
dc.title | Ferric-Pyoverdine Recognition by Fpv Outer Membrane Proteins of Pseudomonas protegens Pf-5 | en_US |
dc.type | Article | en_US |
Appears in Collections: | School of Life Sciences |
Files in This Item:
File | Description | Size | Format | |
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Pyoverdin. J Bacteriology.2013.pdf | 1.65 MB | Adobe PDF | View/Open |
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