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  • Title: Fluorescence imaging of GFP-fused periplasmic components of Na+-driven flagellar motor using Tat pathway in Vibrio alginolyticus.
    Author: Takekawa N, Kojima S, Homma M.
    Journal: J Biochem; 2013 Jun; 153(6):547-53. PubMed ID: 23457404.
    Abstract:
    The twin-arginine translocation (Tat) system works to export folded proteins across the cytoplasmic membrane via specific signal peptides harbouring a twin-arginine motif. In Escherichia coli, a functional GFP is exported to the periplasm through the Tat pathway by fusion of the signal peptide of TorA, which is one of the periplasmic proteins exported by the Tat pathway. In this study, we fused the signal peptide of Vibrio alginolyticus TorA (TorASP) to GFP and demonstrate the export of functional GFP to the periplasm of V. alginolyticus. We also made fusions of TorASP-GFP with MotX, MotY and FlgT, which are periplasmic components of the Na(+)-driven flagellar motor. Those fusion proteins were localized to the flagellar motor independent of the Na(+) concentration in the environment.
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