Amphipathic helical ordering of the flagellar secretion signal of Salmonella flagellin

Orsolya Toke, F. Vonderviszt

Research output: Contribution to journalArticle

1 Citation (Scopus)


Export of external flagellar proteins requires a signal located within their N-terminal disordered part, however, these regions do not share any significant sequence similarity suggesting that the secondary/tertiary structure might be important for recognition by the export gate. NMR experiments were performed to reveal the conformational properties of the flagellin signal sequence in vitro. It assumed a largely disordered fluctuating structure in aqueous environment, but acquired a folded structure containing an amphipathic helical portion in 50% MeOH or upon addition of SDS micelles which are known to promote hydrophobic interactions. Our observations raise the possibility that the signal sequence may partially undergo amphipathic helical ordering upon interaction with the recognition unit of the flagellar export machinery in a similar way as revealed for protein import into intracellular eukaryotic organelles mediated by targeting signals of high diversity.

Original languageEnglish
JournalBiochemical and Biophysical Research Communications
Publication statusAccepted/In press - May 20 2016


  • Export signal
  • Flagellar export
  • Helical ordering
  • NMR
  • Type III secretion

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Molecular Biology

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