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dc.contributor.authorSinger, Hanna M
dc.contributor.authorErhardt, Marc
dc.contributor.authorHughes, Kelly T
dc.date.accessioned2015-01-09T09:52:50Z
dc.date.available2015-01-09T09:52:50Z
dc.date.issued2014-08
dc.identifier.citationComparative analysis of the secretion capability of early and late flagellar type III secretion substrates. 2014, 93 (3):505-20 Mol. Microbiol.en
dc.identifier.issn1365-2958
dc.identifier.pmid24946091
dc.identifier.doi10.1111/mmi.12675
dc.identifier.urihttp://hdl.handle.net/10033/337963
dc.description.abstractA remarkable feature of the flagellar-specific type III secretion system (T3SS) is the selective recognition of a few substrate proteins among the many thousand cytoplasmic proteins. Secretion substrates are divided into two specificity classes: early substrates secreted for hook-basal body (HBB) construction and late substrates secreted after HBB completion. Secretion was reported to require a disordered N-terminal secretion signal, mRNA secretion signals within the 5'-untranslated region (5'-UTR) and for late substrates, piloting proteins known as the T3S chaperones. Here, we utilized translational β-lactamase fusions to probe the secretion efficacy of the N-terminal secretion signal of fourteen secreted flagellar substrates in Salmonella enterica. We observed a surprising variety in secretion capability between flagellar proteins of the same secretory class. The peptide secretion signals of the early-type substrates FlgD, FlgF, FlgE and the late-type substrate FlgL were analysed in detail. Analysing the role of the 5'-UTR in secretion of flgB and flgE revealed that the native 5'-UTR substantially enhanced protein translation and secretion. Based on our data, we propose a multicomponent signal that drives secretion via the flagellar T3SS. Both mRNA and peptide signals are recognized by the export apparatus and together with substrate-specific chaperones allowing for targeted secretion of flagellar substrates.
dc.language.isoenen
dc.titleComparative analysis of the secretion capability of early and late flagellar type III secretion substrates.en
dc.typeArticleen
dc.contributor.departmentHelmholtz Centre for ifection research, Innhoffenstr. 7, D38124 Braunschweig, Germany.en
dc.identifier.journalMolecular microbiologyen
refterms.dateFOA2015-08-15T00:00:00Z
html.description.abstractA remarkable feature of the flagellar-specific type III secretion system (T3SS) is the selective recognition of a few substrate proteins among the many thousand cytoplasmic proteins. Secretion substrates are divided into two specificity classes: early substrates secreted for hook-basal body (HBB) construction and late substrates secreted after HBB completion. Secretion was reported to require a disordered N-terminal secretion signal, mRNA secretion signals within the 5'-untranslated region (5'-UTR) and for late substrates, piloting proteins known as the T3S chaperones. Here, we utilized translational β-lactamase fusions to probe the secretion efficacy of the N-terminal secretion signal of fourteen secreted flagellar substrates in Salmonella enterica. We observed a surprising variety in secretion capability between flagellar proteins of the same secretory class. The peptide secretion signals of the early-type substrates FlgD, FlgF, FlgE and the late-type substrate FlgL were analysed in detail. Analysing the role of the 5'-UTR in secretion of flgB and flgE revealed that the native 5'-UTR substantially enhanced protein translation and secretion. Based on our data, we propose a multicomponent signal that drives secretion via the flagellar T3SS. Both mRNA and peptide signals are recognized by the export apparatus and together with substrate-specific chaperones allowing for targeted secretion of flagellar substrates.


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