title: Form and function of the bacterial cytokinetic ring.
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.
authors: Department of Biological Chemistry, Johns Hopkins University School of Medicine, 725 North Wolfe Street, 520 WBSB, Baltimore, MD 21205, USA.
authors: Elizabeth L
authors: EL
authors: Meier
authors: 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.
authors: Erin D
authors: ED
authors: Goley
mesh_terms: D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D002473:Cell Wall / Q000737:chemistry / Q000378:metabolism; D048749:Cytokinesis; D003598:Cytoskeletal Proteins / Q000737:chemistry / Q000378:metabolism; D003599:Cytoskeleton / Q000378:metabolism; D011485:Protein Binding
chemical_list: D001426:Bacterial Proteins; D003598:Cytoskeletal Proteins