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dc.contributor.authorHockett, Kevin L.
dc.contributor.authorRenner, Tanya
dc.contributor.authorBaltrus, David A.
dc.date.accessioned2016-11-10T05:02:25Z
dc.date.available2016-11-10T05:02:25Z
dc.date.issued2015-08-11
dc.identifier.citationIndependent Co-Option of a Tailed Bacteriophage into a Killing Complex in Pseudomonas 2015, 6 (4):e00452-15 mBioen
dc.identifier.issn2150-7511
dc.identifier.doi10.1128/mBio.00452-15
dc.identifier.urihttp://hdl.handle.net/10150/621338
dc.descriptionUA Open Access Publishing Funden
dc.description.abstractCompetition between microbes is widespread in nature, especially among those that are closely related. To combat competitors, bacteria have evolved numerous protein-based systems (bacteriocins) that kill strains closely related to the producer. In characterizing the bacteriocin complement and killing spectra for the model strain Pseudomonas syringae B728a, we discovered that its activity was not linked to any predicted bacteriocin but is derived from a prophage. Instead of encoding an active prophage, this region encodes a bacteriophage-derived bacteriocin, termed an R-type syringacin. This R-type syringacin is striking in its convergence with the well-studied R-type pyocin of P. aeruginosa in both genomic location and molecular function. Genomic alignment, amino acid percent sequence identity, and phylogenetic inference all support a scenario where the R-type syringacin has been co-opted independently of the R-type pyocin. Moreover, the presence of this region is conserved among several other Pseudomonas species and thus is likely important for intermicrobial interactions throughout this important genus.
dc.language.isoenen
dc.publisherAmerican Society for Microbiologyen
dc.relation.urlhttp://mbio.asm.org/lookup/doi/10.1128/mBio.00452-15en
dc.rightsCopyright © 2015 Hockett et al. This is an open-access article distributed under the terms of the Creative Commons Attribution-Noncommercial-ShareAlike 3.0 Unported license.en
dc.rights.urihttps://creativecommons.org/licenses/by-nc-sa/3.0/
dc.titleIndependent Co-Option of a Tailed Bacteriophage into a Killing Complex in Pseudomonasen
dc.typeArticleen
dc.contributor.departmentSchool of Plant Sciences, University of Arizonaen
dc.contributor.departmentDepartment of Entomology and Center for Insect Science, University of Arizonaen
dc.identifier.journalmBioen
dc.description.noteOpen access journalen
dc.description.collectioninformationThis item from the UA Faculty Publications collection is made available by the University of Arizona with support from the University of Arizona Libraries. If you have questions, please contact us at repository@u.library.arizona.edu.en
dc.eprint.versionFinal published versionen
refterms.dateFOA2018-05-18T00:19:48Z
html.description.abstractCompetition between microbes is widespread in nature, especially among those that are closely related. To combat competitors, bacteria have evolved numerous protein-based systems (bacteriocins) that kill strains closely related to the producer. In characterizing the bacteriocin complement and killing spectra for the model strain Pseudomonas syringae B728a, we discovered that its activity was not linked to any predicted bacteriocin but is derived from a prophage. Instead of encoding an active prophage, this region encodes a bacteriophage-derived bacteriocin, termed an R-type syringacin. This R-type syringacin is striking in its convergence with the well-studied R-type pyocin of P. aeruginosa in both genomic location and molecular function. Genomic alignment, amino acid percent sequence identity, and phylogenetic inference all support a scenario where the R-type syringacin has been co-opted independently of the R-type pyocin. Moreover, the presence of this region is conserved among several other Pseudomonas species and thus is likely important for intermicrobial interactions throughout this important genus.


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Copyright © 2015 Hockett et al. This is an open-access article distributed under the terms of the Creative Commons Attribution-Noncommercial-ShareAlike 3.0 Unported license.
Except where otherwise noted, this item's license is described as Copyright © 2015 Hockett et al. This is an open-access article distributed under the terms of the Creative Commons Attribution-Noncommercial-ShareAlike 3.0 Unported license.