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  • Title: Characterization of the type III export signal of the flagellar hook scaffolding protein FlgD of Escherichia coli.
    Author: Weber-Sparenberg C, Pöplau P, Brookman H, Rochón M, Möckel C, Nietschke M, Jung H.
    Journal: Arch Microbiol; 2006 Oct; 186(4):307-16. PubMed ID: 16897036.
    Abstract:
    Transport of flagellar structural proteins beyond the cytoplasmic membrane is accomplished by a type III secretory pathway [flagellar type III secretion system (fTTSS)]. The mechanism of substrate recognition by the fTTSS is still enigmatic. Using the hook scaffolding protein FlgD of Escherichia coli as a model substrate, it is demonstrated that the export signal is contained within the N-terminal 71 amino acids of FlgD. Analysis of frame-shift mutations and alterations of the nucleotide sequence suggest a proteinaceous nature of the signal. Furthermore, the physicochemical properties of the first about eight amino acids are crucial for export.
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