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

Authors
  • Barrows, Jordan M1
  • Goley, Erin D2
  • 1 Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD, USA.
  • 2 Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD, USA. Electronic address: [email protected]
Type
Published Article
Journal
Current opinion in cell biology
Publication Date
Nov 18, 2020
Volume
68
Pages
163–172
Identifiers
DOI: 10.1016/j.ceb.2020.10.013
PMID: 33220539
Source
Medline
Keywords
Language
English
License
Unknown

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. Copyright © 2020 Elsevier Ltd. All rights reserved.

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