Cell division protein FtsZ (FtsZ)

Cell division protein FtsZ is a highly conserved prokaryotic protein that plays an essential role in the process of binary fission, particularly in bacteria and archaea, and is also found in chloroplasts of plants[1][2][3][4]. It is the bacterial homologue of eukaryotic tubulin, and functions as a GTPase[4]. FtsZ polymerizes in a GTP-dependent manner to form dynamic protofilaments that assemble at the future division site of the cell, creating a structure known as the Z-ring[1][3][5]. The Z-ring serves as a scaffold for the assembly of more than 30 divisome proteins, channels cell wall synthesis enzymes to the division site, and orchestrates cytokinesis[1][3][5]. FtsZ treadmills around the division site, coordinating septal cell wall synthesis and the constriction of the cell membrane—processes that are critical to the production of two daughter cells[3][5]. FtsZ has two principal domains: a GTPase domain structurally related to tubulin and a C-terminal domain involved in protein–protein interactions[4]. Pharmacologically, FtsZ is considered a validated antibacterial target because inhibition of FtsZ function blocks bacterial cell division[2]. Several experimental antibiotics exploit this mechanism and offer the potential for treating antibiotic-resistant bacteria[2]. However, clinical development requires careful consideration of potential toxicity in host cells with FtsZ-homologous structures (e.g., in chloroplasts or mitochondria)[1][2].

Other names

Filamenting temperature-sensitive mutant Z proteinZ ring proteinTubulin-like protein FtsZ

Inhibition of FtsZ polymerization (prevents Z-ring formation and hence cell division) - Disruption of Z-ring dynamics (interferes with treadmilling and septum formation)