1. Characterization of the type III export signal of the flagellar hook scaffolding protein FlgD of Escherichia coli
- Author
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Corinna Weber-Sparenberg, Heinrich Jung, Petra Pöplau, Heiner Brookman, Carolin Möckel, Maike Rochon, and Monika Nietschke
- Subjects
Scaffold protein ,Recombinant Fusion Proteins ,Protein Sorting Signals ,Biology ,Flagellum ,medicine.disease_cause ,Biochemistry ,Microbiology ,Type three secretion system ,Escherichia coli ,Genetics ,medicine ,Molecular Biology ,Secretory pathway ,chemistry.chemical_classification ,Escherichia coli Proteins ,Nucleic acid sequence ,Biological Transport ,General Medicine ,Alkaline Phosphatase ,Amino acid ,chemistry ,Flagella ,Cytoplasm ,Periplasm - 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.
- Published
- 2006
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