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Curr Opin Cell Biol. 2014 Feb;26:19-27. doi: 10.1016/j.ceb.2013.08.006. Epub 2013 Sep 25.

Form and function of the bacterial cytokinetic ring.

Author information

1
Department of Biological Chemistry, Johns Hopkins University School of Medicine, 725 North Wolfe Street, 520 WBSB, Baltimore, MD 21205, USA.
2
Department of Biological Chemistry, Johns Hopkins University School of Medicine, 725 North Wolfe Street, 520 WBSB, Baltimore, MD 21205, USA. Electronic address: egoley1@jhmi.edu.

Erratum in

  • Curr Opin Cell Biol. 2014 Feb;26:147.

Abstract

Bacterial cytokinesis depends upon the tubulin-like GTPase FtsZ, which polymerizes into an annular structure at midcell (the Z-ring) that defines the division site. The Z-ring nucleates assembly of downstream machinery required for cell wall synthesis and membrane fission, but may also generate constrictive force. Recent high-resolution imaging of FtsZ in vivo has begun to illuminate the organization of filaments within the Z-ring. This in vivo work has been complemented by reconstitution of Z-rings in vitro to demonstrate the force-generating capacity of FtsZ and explore its mechanism of action. Despite these technical advances, whether FtsZ-mediated force generation is required for cytokinesis and how Z-ring structure and constriction are mechanistically linked to cell wall remodeling are open questions.

PMID:
24529242
DOI:
10.1016/j.ceb.2013.08.006
[Indexed for MEDLINE]

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