Bacterial cell division proteins (Fts)

Bacterial cell division proteins, collectively known as the divisome, constitute a complex molecular machine responsible for cytokinesis in prokaryotes [3, 9]. The process is initiated by the assembly of FtsZ, a tubulin-like GTPase, into a contractile Z-ring at the mid-cell, which then recruits a suite of accessory proteins including FtsA, ZipA, and the transpeptidase FtsI (also known as PBP3) [1, 6]. These proteins are essential for the formation of the division septum and the synthesis of new cell wall material during binary fission [2, 5]. Because the divisome components are highly conserved across bacterial species and largely absent or structurally distinct in eukaryotes, they are prime targets for the development of novel antibiotics [11, 15]. Drugs targeting these proteins, such as FtsZ inhibitors or PBP3-binding beta-lactams, cause the cessation of cell division, leading to the formation of long, non-dividing filaments and eventual cell death [8, 20]. This target class is particularly valuable for combating multidrug-resistant pathogens like MRSA and various Gram-negative bacteria [5, 19].

Other names

Bacterial cell division genesDivisomeFts proteinsBacterial cytokinesis machinerydcw cluster

Inhibition of FtsZ polymerization, inhibition of GTPase activity, inhibition of septal peptidoglycan synthesis, and activation of ClpP-mediated protein degradation