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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.

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