title: Tubules, rods, and spirals: Diverse modes of SepF-FtsZ assembling
creator: Choudhury, Jagrity
creator: Chaudhuri, Barnali N
description: 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.
publisher: Wiley
date: 2025-07
type: Article
type: NonPeerReviewed
identifier:   Choudhury, Jagrity and Chaudhuri, Barnali N  (2025) Tubules, rods, and spirals: Diverse modes of SepF-FtsZ assembling.  Cytoskeleton (Hoboken), 82 (7).  pp. 432-443.      
relation: http://crdd.osdd.net/open/3211/