Comparative analysis of the secretion capability of early and late flagellar type III secretion substrates.
dc.contributor.author | Singer, Hanna M | |
dc.contributor.author | Erhardt, Marc | |
dc.contributor.author | Hughes, Kelly T | |
dc.date.accessioned | 2015-01-09T09:52:50Z | |
dc.date.available | 2015-01-09T09:52:50Z | |
dc.date.issued | 2014-08 | |
dc.identifier.citation | Comparative analysis of the secretion capability of early and late flagellar type III secretion substrates. 2014, 93 (3):505-20 Mol. Microbiol. | en |
dc.identifier.issn | 1365-2958 | |
dc.identifier.pmid | 24946091 | |
dc.identifier.doi | 10.1111/mmi.12675 | |
dc.identifier.uri | http://hdl.handle.net/10033/337963 | |
dc.description.abstract | A 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.iso | en | en |
dc.title | Comparative analysis of the secretion capability of early and late flagellar type III secretion substrates. | en |
dc.type | Article | en |
dc.contributor.department | Helmholtz Centre for ifection research, Innhoffenstr. 7, D38124 Braunschweig, Germany. | en |
dc.identifier.journal | Molecular microbiology | en |
refterms.dateFOA | 2015-08-15T00:00:00Z | |
html.description.abstract | A 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. |