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Versatile in vitro system to study translocation and functional integration of bacterial outer membrane proteins

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  • Derrick Norell

    (Institute of Biochemistry and Molecular Biology, Zentrum für Biochemie und Molekulare Zellforschung, University of Freiburg
    Faculty of Biology, University of Freiburg)

  • Alexander Heuck

    (Research Institute of Molecular Pathology)

  • Thuy-Anh Tran-Thi

    (Institute of Biochemistry and Molecular Biology, Zentrum für Biochemie und Molekulare Zellforschung, University of Freiburg)

  • Hansjörg Götzke

    (Center for Biomembrane Research, Stockholm University)

  • Françoise Jacob-Dubuisson

    (Center for Infection and Immunity of Lille, Institut Pasteur de Lille)

  • Tim Clausen

    (Research Institute of Molecular Pathology)

  • Daniel O. Daley

    (Center for Biomembrane Research, Stockholm University)

  • Volkmar Braun

    (Max Planck Institute for Developmental Biology)

  • Matthias Müller

    (Institute of Biochemistry and Molecular Biology, Zentrum für Biochemie und Molekulare Zellforschung, University of Freiburg)

  • Enguo Fan

    (Institute of Biochemistry and Molecular Biology, Zentrum für Biochemie und Molekulare Zellforschung, University of Freiburg)

Abstract

Gram-negative bacteria use the type-V secretion pathway to expose proteins at their cell surface, many of which have virulence functions. Translocation of those proteins across the outer membrane occurs either by means of dedicated translocator proteins (two-partner secretion) or covalently fused translocator domains (autotransporters). Translocator proteins and translocator domains are β-barrels requiring the β-barrel assembly machinery (BAM) for membrane integration. However, the molecular details of their passage across the envelope and insertion into the outer membrane remain enigmatic, owing in part to the fact that in vitro systems are not available. Here we describe a versatile in vitro reconstitution system that faithfully reproduces both branches of the type-V secretion pathway and the assembly of β-barrel outer membrane proteins. This system will allow an in-depth analysis of protein secretion across and integration into outer membranes.

Suggested Citation

  • Derrick Norell & Alexander Heuck & Thuy-Anh Tran-Thi & Hansjörg Götzke & Françoise Jacob-Dubuisson & Tim Clausen & Daniel O. Daley & Volkmar Braun & Matthias Müller & Enguo Fan, 2014. "Versatile in vitro system to study translocation and functional integration of bacterial outer membrane proteins," Nature Communications, Nature, vol. 5(1), pages 1-9, December.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms6396
    DOI: 10.1038/ncomms6396
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