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

Derrick Norell, Alexander Heuck, Thuy-Anh Tran-Thi, Hansjörg Götzke, Françoise Jacob-Dubuisson, Tim Clausen, Daniel O. Daley, Volkmar Braun, Matthias Müller () and Enguo Fan ()
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Derrick Norell: Institute of Biochemistry and Molecular Biology, Zentrum für Biochemie und Molekulare Zellforschung, 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

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

Abstract: 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.

Date: 2014
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DOI: 10.1038/ncomms6396

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