Comparative analysis of the secretion capability of early and late flagellar type III secretion substrates.
Average rating
Cast your vote
You can rate an item by clicking the amount of stars they wish to award to this item.
When enough users have cast their vote on this item, the average rating will also be shown.
Star rating
Your vote was cast
Thank you for your feedback
Thank you for your feedback
Issue Date
2014-08
Metadata
Show full item recordAbstract
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.Citation
Comparative analysis of the secretion capability of early and late flagellar type III secretion substrates. 2014, 93 (3):505-20 Mol. Microbiol.Affiliation
Helmholtz Centre for ifection research, Innhoffenstr. 7, D38124 Braunschweig, Germany.Journal
Molecular microbiologyPubMed ID
24946091Type
ArticleLanguage
enISSN
1365-2958ae974a485f413a2113503eed53cd6c53
10.1111/mmi.12675
Scopus Count
The following license files are associated with this item: