Form and function of the bacterial cytokinetic ring

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

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.

Publication types

  • Review

MeSH terms

  • Animals
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism
  • Cell Wall / chemistry
  • Cell Wall / metabolism
  • Cytokinesis*
  • Cytoskeletal Proteins / chemistry
  • Cytoskeletal Proteins / metabolism
  • Cytoskeleton / metabolism
  • Protein Binding

Substances

  • Bacterial Proteins
  • Cytoskeletal Proteins