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

Adrià Sogues, Mariano Martinez, Quentin Gaday, Mathilde Ben Assaya, Martin Graña, Alexis Voegele, Michael VanNieuwenhze, Patrick England, Ahmed Haouz, Alexandre Chenal, Sylvain Trépout, Rosario Duran, Anne Marie Wehenkel () and Pedro M. Alzari ()
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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

Nature Communications, 2020, vol. 11, issue 1, 1-14

Abstract: 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.

Date: 2020
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DOI: 10.1038/s41467-020-15490-8

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