Characterization of the type III export signal of the flagellar hook scaffolding protein FlgD of Escherichia coli
| Autor: | Corinna Weber-Sparenberg, Heinrich Jung, Petra Pöplau, Heiner Brookman, Carolin Möckel, Maike Rochon, Monika Nietschke |
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| Rok vydání: | 2006 |
| Předmět: |
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 |
| Zdroj: | Archives of Microbiology. 186:307-316 |
| ISSN: | 1432-072X 0302-8933 |
| DOI: | 10.1007/s00203-006-0146-0 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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