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

Autor(en): Weber-Sparenberg, Corinna
Poeplau, Petra
Brookman, Heiner
Rochon, Maike
Moeckel, Carolin
Nietschke, Monika
Jung, Heinrich
Stichwörter: ALKALINE-PHOSPHATASE; APPARATUS; BACTERIAL FLAGELLUM; flagella assembly; FlgD; MESSENGER-RNA; Microbiology; MUTATIONAL ANALYSIS; protein export; SALMONELLA-TYPHIMURIUM; SECRETION SIGNAL; SEQUENCE; type III protein secretion; YERSINIA-ENTEROCOLITICA; YOPE
Erscheinungsdatum: 2006
Herausgeber: SPRINGER
Journal: ARCHIVES OF MICROBIOLOGY
Volumen: 186
Ausgabe: 4
Startseite: 307
Seitenende: 316
Zusammenfassung: 
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.
ISSN: 03028933
DOI: 10.1007/s00203-006-0146-0

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