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    Arch Microbiol. 2006 Oct;186(4):307-16. Epub 2006 Aug 9.

    Characterization of the type III export signal of the flagellar hook scaffolding protein FlgD of Escherichia coli.

    Weber-Sparenberg C, Pöplau P, Brookman H, Rochón M, Möckel C, Nietschke M, Jung H.

    Source

    Fachbereich Biologie/Chemie, Abteilung Mikrobiologie, Universität Osnabrück, Barbarastrasse 11, 49069 Osnabrück, Germany.

    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.

    PMID:
    16897036
    [PubMed - indexed for MEDLINE]

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