Treadmilling by FtsZ filaments drives peptidoglycan synthesis and bacterial cell division

Abstract

The mechanism by which bacteria divide is not well understood. Cell division is mediated by filaments of FtsZ and FtsA (FtsAZ) that recruit septal peptidoglycan synthesizing enzymes to the division site. To understand how these components coordinate to divide cells, we visualized their movements relative to the dynamics of cell wall synthesis during cytokinesis. We found that the division septum was built at discrete sites that moved around the division plane. FtsAZ filaments treadmilled circumferentially around the division ring, driving the motions of the peptidoglycan synthesizing enzymes. The FtsZ treadmilling rate controlled both the rate of peptidoglycan synthesis and cell division. Thus, FtsZ treadmilling guides the progressive insertion of new cell wall, building increasingly smaller concentric rings of peptidoglycan to divide the cell.

Lessons from bacterial homolog of tubulin, FtsZ for microtubule dynamics

“…In a recent work, FtsZ treadmilling has been suggested as a mechanism to explain the recruitment of enzymes at the division site (Bisson-Filho et al 2017). A large body of evidence points toward the similarity of the dynamics of FtsZ and tubulin, thereby providing a platform to study the basic mechanism of the assembly of microtubules through FtsZ.…”

“…The septum was found to be constructed discontinuously around the division plane. The treadmilling of FtsZ and FtsA filaments around the division plane in a circular fashion led to the relative motions of the enzymes required for PG synthesis, thereby controlling the rate of PG synthesis and cell division (Bisson-Filho et al 2017).…”

“…The filaments of FtsZ and FtsA are involved in positioning enzymes required for septal peptidoglycan (PG) synthesis for cell division process. To understand septal PG synthesis, the dynamic movements of FtsA and FtsZ filaments with respect to the enzymes recruited to the division site were examined using pulse-labeling and 3D illumination microscopy (Bisson-Filho et al 2017). The septum was found to be constructed discontinuously around the division plane.…”

Small molecules targeting at the bacterial cell division protein FtsZ as potential antimicrobial agents

“…The function of FtsZ is to polymerize to form Z-ring for controlling the division of a bacterial mother cell into daughter cells [26,28,29]. Furthermore, just as the microtubule assembly is influenced by microtubule associated proteins, the stability of FtsZ polymerization is controlled in vivo by bacterial cell division proteins such as FtsA, ZipA, and ZapA [28,[30][31][32][33][34].…”

A model of cell-wall dynamics during sporulation inBacillus subtilis

“…To survive starvation, this bacterium forms robust and dormant endospores in several steps ( Fig. 1): during DNA replication, septation is initiated asymmetrically by FtsZ (a), followed by pumping of one of the DNA molecules through the forespore's closing septum by ATP hydrolysis (b) [2][3][4][5]. Subsequently, the septum (made of PG) is remodeled and grows around the forespore (c), allowing the mother cell to engulf the forespore by its membrane for spore maturation (d) [6][7][8].…”