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

Current Opinion in Cell Biology
Jordan M Barrows, Erin D Goley

Abstract

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.

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Citations

Jan 10, 2021·Current Opinion in Cell Biology·Pierre A Coulombe, Pekka Lappalainen
Dec 30, 2020·Chemical Reviews·Jed F Fisher, Shahriar Mobashery
Jul 3, 2021·Antibiotics·Angela Di SommaAngela Duilio
Sep 8, 2021·Frontiers in Microbiology·Jiawei SunKerwyn Casey Huang

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