FtsZ polymerizes into protofilaments to form the Z-ring that acts as a scaffold for accessory
proteins during cell division. Structures of FtsZ have been previously solved, but detailed …

Bacteria are surrounded by a complex cell envelope made up of one or two membranes
supplemented with a layer of peptidoglycan (PG). The envelope is responsible for the …

To generate two cells from one, bacteria such as Escherichia coli use a complex of
membrane-embedded proteins called the divisome that synthesize the division septum. The …

FtsZ is a self-assembling GTPase that forms, below the inner membrane, the mid-cell Z-ring
guiding bacterial division. FtsZ monomers polymerize head to tail forming tubulin-like …

ZipA is an essential cell division protein in Escherichia coli. Together with FtsA, ZipA tethers
dynamic polymers of FtsZ to the cytoplasmic membrane, and these polymers are required to …

The bacterial tubulin FtsZ polymerizes to form a discontinuous ring that drives bacterial cell
division by directing local cell wall synthesis. FtsZ comprises a polymerizing GTPase …

Bacterial cell division requires the assembly of a multiprotein division machinery, or
divisome, that remodels the cell envelope to cause constriction. The cytoskeletal protein FtsZ …

Cell division of rod-shaped bacteria requires the Z ring, a ring of FtsZ filaments associated
with the inner-membrane wall. The MinCDE proteins help localize the Z ring to the center of …

The assembly and disassembly of the FtsZ ring drives the division of bacteria cells, including
Streptococcus pneumoniae, which causes pneumonia and meningitis. In contrast to FtsZ …

The tubulin homolog FtsZ is the major cytoskeletal protein in the bacterial cell division
machinery, conserved in almost all bacteria, archaea, and chloroplasts. Bacterial FtsZ …