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dc.contributor.authorSiegrist, M. Sloanen_US
dc.contributor.authorSteigedal, Magnusen_US
dc.contributor.authorAhmad, Rushdyen_US
dc.contributor.authorMehra, Alkaen_US
dc.contributor.authorDragset, Marte S.en_US
dc.contributor.authorSchuster, Brian M.en_US
dc.contributor.authorPhilips, Jennifer A.en_US
dc.contributor.authorCarr, Steven A.en_US
dc.contributor.authorRubin, Eric J.en_US
dc.date.accessioned2014-07-07T18:13:13Z
dc.date.issued2014en_US
dc.identifier.citationSiegrist, M. Sloan, Magnus Steigedal, Rushdy Ahmad, Alka Mehra, Marte S. Dragset, Brian M. Schuster, Jennifer A. Philips, Steven A. Carr, and Eric J. Rubin. 2014. “Mycobacterial Esx-3 Requires Multiple Components for Iron Acquisition.” mBio 5 (3): e01073-14. doi:10.1128/mBio.01073-14. http://dx.doi.org/10.1128/mBio.01073-14.en
dc.identifier.issn2150-7511en
dc.identifier.urihttp://nrs.harvard.edu/urn-3:HUL.InstRepos:12406869
dc.description.abstractABSTRACT The type VII secretion systems are conserved across mycobacterial species and in many Gram-positive bacteria. While the well-characterized Esx-1 pathway is required for the virulence of pathogenic mycobacteria and conjugation in the model organism Mycobacterium smegmatis, Esx-3 contributes to mycobactin-mediated iron acquisition in these bacteria. Here we show that several Esx-3 components are individually required for function under low-iron conditions but that at least one, the membrane-bound protease MycP3 of M. smegmatis, is partially expendable. All of the esx-3 mutants tested, including the ΔmycP3ms mutant, failed to export the native Esx-3 substrates EsxHms and EsxGms to quantifiable levels, as determined by targeted mass spectrometry. Although we were able to restore low-iron growth to the esx-3 mutants by genetic complementation, we found a wide range of complementation levels for protein export. Indeed, minute quantities of extracellular EsxHms and EsxGms were sufficient for iron acquisition under our experimental conditions. The apparent separation of Esx-3 function in iron acquisition from robust EsxGms and EsxHms secretion in the ΔmycP3ms mutant and in some of the complemented esx-3 mutants compels reexamination of the structure-function relationships for type VII secretion systems.en
dc.language.isoen_USen
dc.publisherAmerican Society of Microbiologyen
dc.relation.isversionofdoi:10.1128/mBio.01073-14en
dc.relation.hasversionhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC4010830/pdf/en
dash.licenseLAAen_US
dc.titleMycobacterial Esx-3 Requires Multiple Components for Iron Acquisitionen
dc.typeJournal Articleen_US
dc.description.versionVersion of Recorden
dc.relation.journalmBioen
dash.depositing.authorRubin, Eric J.en_US
dc.date.available2014-07-07T18:13:13Z
dc.identifier.doi10.1128/mBio.01073-14*
dash.contributor.affiliatedRubin, Eric


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