Translocation path of a substrate protein through its Omp85 transporter

Catherine Baud, Jérémy Guérin, Emmanuelle Petit, Elodie Lesne, Elian Dupré, Camille Locht and Françoise Jacob-Dubuisson ()
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Catherine Baud: Center for Infection and Immunity of Lille, Institut Pasteur de Lille, 1 rue Calmette
Jérémy Guérin: Center for Infection and Immunity of Lille, Institut Pasteur de Lille, 1 rue Calmette
Emmanuelle Petit: Center for Infection and Immunity of Lille, Institut Pasteur de Lille, 1 rue Calmette
Elodie Lesne: Center for Infection and Immunity of Lille, Institut Pasteur de Lille, 1 rue Calmette
Elian Dupré: Center for Infection and Immunity of Lille, Institut Pasteur de Lille, 1 rue Calmette
Camille Locht: Center for Infection and Immunity of Lille, Institut Pasteur de Lille, 1 rue Calmette
Françoise Jacob-Dubuisson: Center for Infection and Immunity of Lille, Institut Pasteur de Lille, 1 rue Calmette

Nature Communications, 2014, vol. 5, issue 1, 1-9

Abstract: Abstract TpsB proteins are Omp85 superfamily members that mediate protein translocation across the outer membrane of Gram-negative bacteria. Omp85 transporters are composed of N-terminal POTRA domains and a C-terminal transmembrane β-barrel. In this work, we track the in vivo secretion path of the Bordetella pertussis filamentous haemagglutinin (FHA), the substrate of the model TpsB transporter FhaC, using site-specific crosslinking. The conserved secretion domain of FHA interacts with the POTRA domains, specific extracellular loops and strands of FhaC and the inner β-barrel surface. The interaction map indicates a funnel-like pathway, with conformationally flexible FHA entering the channel in a non-exclusive manner and exiting along a four-stranded β-sheet at the surface of the FhaC barrel. This sheet of FhaC guides the secretion domain of FHA along discrete steps of translocation and folding. This work demonstrates that the Omp85 barrel serves as a channel for translocation of substrate proteins.

Date: 2014
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DOI: 10.1038/ncomms6271

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