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The flagellar substrate specificity switch protein FlhB assembles onto the extra-membrane export gate to regulate type three secretion

Lucas Kuhlen, Steven Johnson, Andreas Zeitler, Sandra Bäurle, Justin C. Deme, Rebecca Debo, Joseph Fisher, Samuel Wagner, Susan M. Lea
doi: https://doi.org/10.1101/686782
Lucas Kuhlen
1Sir William Dunn School of Pathology, University of Oxford, Oxford OX13RE, UK
2Department of Chemistry, University of Oxford, Oxford, UK
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Steven Johnson
1Sir William Dunn School of Pathology, University of Oxford, Oxford OX13RE, UK
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Andreas Zeitler
3University of Tübingen, Interfaculty Institute of Microbiology and Infection Medicine (IMIT), Elfriede-Aulhorn-Str. 6, 72076 Tübingen, Germany
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Sandra Bäurle
3University of Tübingen, Interfaculty Institute of Microbiology and Infection Medicine (IMIT), Elfriede-Aulhorn-Str. 6, 72076 Tübingen, Germany
6University Hospital Tübingen, Department of Thoracic & Cardiovascular Surgery, 72076 Tübingen, Germany
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Justin C. Deme
1Sir William Dunn School of Pathology, University of Oxford, Oxford OX13RE, UK
4Central Oxford Structural Microscopy and Imaging Centre, University of Oxford, Oxford OX1 3RE, UK
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Rebecca Debo
3University of Tübingen, Interfaculty Institute of Microbiology and Infection Medicine (IMIT), Elfriede-Aulhorn-Str. 6, 72076 Tübingen, Germany
7University of Tübingen Department of Geosciences, Centre for Applied Geosciences (ZAG), 72076 Tübingen, Germany
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Joseph Fisher
1Sir William Dunn School of Pathology, University of Oxford, Oxford OX13RE, UK
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Samuel Wagner
3University of Tübingen, Interfaculty Institute of Microbiology and Infection Medicine (IMIT), Elfriede-Aulhorn-Str. 6, 72076 Tübingen, Germany
5German Center for Infection Research (DZIF), partner-site Tübingen, Elfriede-Aulhorn-Str. 6, 72076 Tübingen, Germany
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Susan M. Lea
1Sir William Dunn School of Pathology, University of Oxford, Oxford OX13RE, UK
4Central Oxford Structural Microscopy and Imaging Centre, University of Oxford, Oxford OX1 3RE, UK
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  • For correspondence: susan.lea@path.ox.ac.uk
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Abstract

Export of proteins through type three secretion systems (T3SS) is critical for motility and virulence of many major bacterial pathogens. Proteins are transported through an export gate complex consisting of three proteins (FliPQR in flagellar systems, SctRST in virulence systems) that were initially annotated as membrane proteins, but which we have recently shown assemble into an extra-membranous helical assembly. A fourth putative membrane protein (FlhB/SctU) is essential to the export process, and also functions to “switch” secretion substrate specificity once the growing hook/needle structures reach their determined length. Here we present the structure of an export gate containing the switch protein from a Vibrio polar flagellar system at 3.2 Å resolution by cryo-electron microscopy. The structure reveals that the FlhB/SctU further extends the helical export gate assembly with its four putative transmembrane helices adopting an out-of-membrane location, wrapped around the other export gate components at the base of the structure. The unusual topology of the switch protein helices creates a loop that wraps around the bottom of the closed export gate complex. Structure-informed mutagenesis suggests that this loop is critical in gating secretion and we propose that a series of conformational changes in the type 3 secretion system trigger opening of the export gate through the interactions between FlhB/SctU and FliPQR/SctRST.

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Posted July 04, 2019.
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The flagellar substrate specificity switch protein FlhB assembles onto the extra-membrane export gate to regulate type three secretion
Lucas Kuhlen, Steven Johnson, Andreas Zeitler, Sandra Bäurle, Justin C. Deme, Rebecca Debo, Joseph Fisher, Samuel Wagner, Susan M. Lea
bioRxiv 686782; doi: https://doi.org/10.1101/686782
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The flagellar substrate specificity switch protein FlhB assembles onto the extra-membrane export gate to regulate type three secretion
Lucas Kuhlen, Steven Johnson, Andreas Zeitler, Sandra Bäurle, Justin C. Deme, Rebecca Debo, Joseph Fisher, Samuel Wagner, Susan M. Lea
bioRxiv 686782; doi: https://doi.org/10.1101/686782

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