@article{open3211,
          volume = {82},
          number = {7},
           month = {July},
          author = {Jagrity Choudhury and Barnali N Chaudhuri},
           title = {Tubules, rods, and spirals: Diverse modes of SepF-FtsZ assembling},
       publisher = {Wiley},
            year = {2025},
         journal = {Cytoskeleton (Hoboken)},
           pages = {432--443},
        keywords = {FtsZ bundling; SepF; SepF-FtsZ interaction; bacterial cell division; bacterial cytoskeleton},
             url = {http://crdd.osdd.net/open/3211/},
        abstract = {Z-ring formation by FtsZ, the master assembler of the divisome, is a key step in bacterial cell division. Membrane anchoring of the Z-ring requires the assistance of dedicated Z-ring binding proteins, such as SepF and FtsA. SepF participates in bundling and membrane anchoring of FtsZ in gram-positive bacteria. We report in vitro biophysical studies of the interactions between FtsZ and a cytoplasmic component of cognate SepF from three different bacteria: Mycobacterium tuberculosis, Staphylococcus aureus, and Enterococcus gallinarum. While the cytosolic domain of SepF from M. tuberculosis is primarily a dimer, those from S. aureus and E. gallinarum polymerize to form ring-like structures. Mycobacterial SepF helps in the bundling of FtsZ filaments to form thick filaments and large spirals. On the other hand, ring-forming SepF from the Firmicutes bundle FtsZ into tubules. Our results suggest that the oligomeric form of SepF directs how it bundles FtsZ filaments.}
}