Ferric-Pyoverdine Recognition by Fpv Outer Membrane Proteins of Pseudomonas protegens Pf-5 Public Deposited

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  • The soil bacterium Pseudomonas protegens Pf-5 (previously called P. fluorescens Pf-5) produces two siderophores, enantio-pyochelin 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 receptors (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.
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  • Hartney, S. L., Mazurier, S., Girard, M. K., Mehnaz, S., Davis, 2., Edward W, Gross, H., . . . Loper, J. E. (2013). Ferric-pyoverdine recognition by fpv outer membrane proteins of pseudomonas protegens pf-5. Journal of Bacteriology, 195(4), 765-776. doi:10.1128/JB.01639-12
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  • description.provenance : Submitted by Deborah Campbell (deborah.campbell@oregonstate.edu) on 2013-05-06T17:08:07Z No. of bitstreams: 1 HartneySierraLBotanyPlantPathologyFerricPyoverdineRecognition.pdf: 1624545 bytes, checksum: 467669f6c9996554108964cf63cc15d3 (MD5)
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