dc.contributor.author | Siegrist, M. Sloan | |
dc.contributor.author | Steigedal, Magnus | |
dc.contributor.author | Ahmad, Rushdy | |
dc.contributor.author | Mehra, Alka | |
dc.contributor.author | Dragset, Marte Singsås | |
dc.contributor.author | Schuster, Brian M. | |
dc.contributor.author | Phillips, Jennifer A. | |
dc.contributor.author | Carr, Steven A. | |
dc.contributor.author | Rubin, Eric J | |
dc.date.accessioned | 2017-08-07T07:19:45Z | |
dc.date.available | 2017-08-07T07:19:45Z | |
dc.date.created | 2014-06-24T10:26:05Z | |
dc.date.issued | 2014 | |
dc.identifier.issn | 2150-7511 | |
dc.identifier.uri | http://hdl.handle.net/11250/2449958 | |
dc.description.abstract | 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. | nb_NO |
dc.language.iso | eng | nb_NO |
dc.publisher | American Society for Microbiology | nb_NO |
dc.rights | Navngivelse 4.0 Internasjonal | * |
dc.rights.uri | http://creativecommons.org/licenses/by/4.0/deed.no | * |
dc.title | Mycobacterial Esx-3 Requires Multiple Components for Iron Acquisition | nb_NO |
dc.type | Journal article | nb_NO |
dc.type | Peer reviewed | nb_NO |
dc.description.version | publishedVersion | nb_NO |
dc.source.volume | 5 | nb_NO |
dc.source.journal | mBio | nb_NO |
dc.source.issue | 3:e01073-14 | nb_NO |
dc.identifier.doi | 10.1128/mBio.01073-14 | |
dc.identifier.cristin | 1140246 | |
dc.relation.project | Norges forskningsråd: 223255 | nb_NO |
dc.relation.project | Norges forskningsråd: 220836 | nb_NO |
dc.description.localcode | © 2014 Siegrist et al. This is an open-access article distributed under the terms of the Creative Commons Attribution-Noncommercial-ShareAlike 3.0 Unportedlicense, which permits unrestricted noncommercial use, distribution, and reproduction in any medium, provided the original author and source are credited. | nb_NO |
cristin.unitcode | 194,65,15,0 | |
cristin.unitcode | 194,66,15,0 | |
cristin.unitname | Institutt for kreftforskning og molekylær medisin | |
cristin.unitname | Institutt for bioteknologi | |
cristin.ispublished | true | |
cristin.fulltext | original | |
cristin.qualitycode | 1 | |