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A dynamic and adaptive network of cytosolic interactions governs protein export by the T3SS injectisome

Author

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  • Andreas Diepold

    (University of Oxford
    Present address: Department of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Karl-von-Frisch-Straße 10, 35043 Marburg, Germany)

  • Erdinc Sezgin

    (MRC Human Immunology Unit, Weatherall Institute of Molecular Medicine, University of Oxford)

  • Miles Huseyin

    (University of Oxford)

  • Thomas Mortimer

    (University of Oxford
    Present address: The Francis Crick Institute, 1 Midland Road, Kings Cross, London NW1 1AT, UK)

  • Christian Eggeling

    (MRC Human Immunology Unit, Weatherall Institute of Molecular Medicine, University of Oxford)

  • Judith P. Armitage

    (University of Oxford)

Abstract

Many bacteria use a type III secretion system (T3SS) to inject effector proteins into host cells. Selection and export of the effectors is controlled by a set of soluble proteins at the cytosolic interface of the membrane spanning type III secretion ‘injectisome’. Combining fluorescence microscopy, biochemical interaction studies and fluorescence correlation spectroscopy, we show that in live Yersinia enterocolitica bacteria these soluble proteins form complexes both at the injectisome and in the cytosol. Binding to the injectisome stabilizes these cytosolic complexes, whereas the free cytosolic complexes, which include the type III secretion ATPase, constitute a highly dynamic and adaptive network. The extracellular calcium concentration, which triggers activation of the T3SS, directly influences the cytosolic complexes, possibly through the essential component SctK/YscK, revealing a potential mechanism involved in the regulation of type III secretion.

Suggested Citation

  • Andreas Diepold & Erdinc Sezgin & Miles Huseyin & Thomas Mortimer & Christian Eggeling & Judith P. Armitage, 2017. "A dynamic and adaptive network of cytosolic interactions governs protein export by the T3SS injectisome," Nature Communications, Nature, vol. 8(1), pages 1-12, August.
  • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms15940
    DOI: 10.1038/ncomms15940
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    Cited by:

    1. Dominic Gilzer & Madeleine Schreiner & Hartmut H. Niemann, 2022. "Direct interaction of a chaperone-bound type III secretion substrate with the export gate," Nature Communications, Nature, vol. 13(1), pages 1-13, December.

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