TY  - JOUR
ID  - open3211
UR  - http://crdd.osdd.net/open/3211/
IS  - 7
A1  - Choudhury, Jagrity
A1  - Chaudhuri, Barnali N
Y1  - 2025/07//
N2  - 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.
PB  - Wiley
JF  - Cytoskeleton (Hoboken)
VL  - 82
KW  - FtsZ bundling; SepF; SepF-FtsZ interaction; bacterial cell division; bacterial cytoskeleton
TI  - Tubules, rods, and spirals: Diverse modes of SepF-FtsZ assembling
SP  - 432
EP  - 443
ER  -