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Essential dynamic interdependence of FtsZ and SepF for Z-ring and septum formation in Corynebacterium glutamicum

Author

Listed:
  • Adrià Sogues

    (Université de Paris)

  • Mariano Martinez

    (Université de Paris)

  • Quentin Gaday

    (Université de Paris)

  • Mathilde Ben Assaya

    (Université de Paris)

  • Martin Graña

    (Bioinformatics Unit, Institut Pasteur de Montevideo)

  • Alexis Voegele

    (Unité de Biochimie des Interactions Moléculaires, Institut Pasteur, CNRS, UMR 3528)

  • Michael VanNieuwenhze

    (Indiana University)

  • Patrick England

    (Plate-forme de biophysique moléculaire, C2RT-Institut Pasteur, CNRS, UMR 3528)

  • Ahmed Haouz

    (Plate-forme de cristallographie, C2RT-Institut Pasteur, CNRS, UMR 3528)

  • Alexandre Chenal

    (Unité de Biochimie des Interactions Moléculaires, Institut Pasteur, CNRS, UMR 3528)

  • Sylvain Trépout

    (Institut Curie, INSERM U1196, CNRS, UMR 9187, Université Paris-Sud, Université Paris-Saclay)

  • Rosario Duran

    (Analytical Biochemistry and Proteomics Unit, Institut Pasteur de Montevideo & Instituto de Investigaciones Biológicas Clemente Estable)

  • Anne Marie Wehenkel

    (Université de Paris)

  • Pedro M. Alzari

    (Université de Paris)

Abstract

The mechanisms of Z-ring assembly and regulation in bacteria are poorly understood, particularly in non-model organisms. Actinobacteria, a large bacterial phylum that includes the pathogen Mycobacterium tuberculosis, lack the canonical FtsZ-membrane anchors and Z-ring regulators described for E. coli. Here we investigate the physiological function of Corynebacterium glutamicum SepF, the only cell division-associated protein from Actinobacteria known to interact with the conserved C-terminal tail of FtsZ. We show an essential interdependence of FtsZ and SepF for formation of a functional Z-ring in C. glutamicum. The crystal structure of the SepF–FtsZ complex reveals a hydrophobic FtsZ-binding pocket, which defines the SepF homodimer as the functional unit, and suggests a reversible oligomerization interface. FtsZ filaments and lipid membranes have opposing effects on SepF polymerization, indicating that SepF has multiple roles at the cell division site, involving FtsZ bundling, Z-ring tethering and membrane reshaping activities that are needed for proper Z-ring assembly and function.

Suggested Citation

  • Adrià Sogues & Mariano Martinez & Quentin Gaday & Mathilde Ben Assaya & Martin Graña & Alexis Voegele & Michael VanNieuwenhze & Patrick England & Ahmed Haouz & Alexandre Chenal & Sylvain Trépout & Ros, 2020. "Essential dynamic interdependence of FtsZ and SepF for Z-ring and septum formation in Corynebacterium glutamicum," Nature Communications, Nature, vol. 11(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-15490-8
    DOI: 10.1038/s41467-020-15490-8
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    Cited by:

    1. Zachary R. Fox & Steven Fletcher & Achille Fraisse & Chetan Aditya & Sebastián Sosa-Carrillo & Julienne Petit & Sébastien Gilles & François Bertaux & Jakob Ruess & Gregory Batt, 2022. "Enabling reactive microscopy with MicroMator," Nature Communications, Nature, vol. 13(1), pages 1-8, December.

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