FtsZ dynamics in bacterial division: What, how, and why?

Bacterial cell division is orchestrated by the divisome, a protein complex centered on the tubulin homolog FtsZ. FtsZ polymerizes into a dynamic ring that defines the division site, recruits downstream proteins, and directs peptidoglycan synthesis to drive constriction. Recent studies have documented treadmilling of FtsZ polymer clusters both in cells and in vitro. Emerging evidence suggests that FtsZ dynamics are regulated largely by intrinsic properties of FtsZ itself and by the membrane anchoring protein FtsA. Although FtsZ dynamics are broadly required for Z-ring assembly, their role(s) during constriction may vary among bacterial species. These recent advances set the stage for future studies to investigate how FtsZ dynamics are physically and/or functionally coupled to peptidoglycan metabolic enzymes to direct efficient division.

Automated summary

Bacterial cell division is coordinated by the divisome, with FtsZ playing a central role. Recent studies have shown that the dynamics of FtsZ are regulated by intrinsic properties of FtsZ and the membrane anchoring protein FtsA. While FtsZ dynamics are broadly required for Z-ring assembly, their role during constriction may vary among bacterial species.