Bacterial cell division: assembly, maintenance and disassembly of the Z ring

Abstract

Bacterial cell division is orchestrated by a tubulin homologue, FtsZ, which polymerizes to form a ring-like structure that is both a scaffold for the assembly of the bacterial cytokinetic machinery and, at least in part, a source of the energy for constriction. FtsZ assembly is tightly regulated, and a diverse repertoire of accessory proteins contributes to the formation of a functional division machine that is responsive to cell cycle status and environmental stress. In this Review, we describe the interaction of these proteins with FtsZ and discuss recent advances in our understanding of Z ring assembly.

Characterization of CrgA, a New Partner of the Mycobacterium tuberculosis Peptidoglycan Polymerization Complexes

“…The FtsZ ring then serves as a scaffold for recruitment of other divisome proteins (2). Recent studies implicate a role for FtsZ in guiding septum and lateral cell wall synthesis in some bacterial species (1,48).…”

Modeling Three-Dimensional Spatial Regulation of Bacterial Cell Division (Dissertation)

“…We have extended Spatiocyte to model such membrane-bound polymerization dynamics of molecules although it has not been used to model the MinD polymerization dynamics. In future, in addition to modeling the polymerization dynamics in the MinDE system, Spatiocyte could also be used to elucidate the formation of the division septum at the middle of Escherichia coli (Lutkenhaus, 2007;Adams and Errington, 2009) since the process also involves multicompartmental RD and polymerizations. Importantly, the FtsZ protein forms a complex polymer structure that constricts in the middle of the cell to produce the two daughter cells.…”

“…Processes that are strongly dependent on the cell morphology, multicompartmental interaction and dynamic localization of molecules such as cell signaling Neves et al, 2008), bacterial cell division (Lutkenhaus, 2007;Adams and Errington, 2009) and chemotaxis (Greenfield et al, 2009;Rao and Ordal, 2009), require realistic models with spatial representation Ridgway et al, 2006;Morris and Jensen, 2008). The processes rely on intricately controlled reaction and diffusion of molecules in and between cytoplasm (or nucleoplasm) and membrane compartments to perform their functions.…”

“…The rod-shaped bacterium begins to divide when the tubulin-homolog FtsZ, polymerizes into a constricting annular structure (Z-ring) on the inner membrane (Adams and Errington, 2009;Lutkenhaus, 2007). To ensure equal distribution of cell contents to the two progeny cells, the constriction site is restricted to the middle of the cell long axis by two mechanisms: (i) nucleoid occlusion, which allows the Z-ring to assemble only at the midcell and the cell poles, locations that are devoid of the nucleoid mass (Woldringh et al, 1990(Woldringh et al, , 1991Bernhardt and de Boer, 2005), and (ii) carefully orchestrated RD of the minB operon encoded proteins, MinC, MinD, and MinE, in the cytoplasm and inner membrane, which suppresses polar Z-rings to avoid the minicelling phenotype (Lutkenhaus, 2007;Vats et al, 2009).…”

ClpXP and ClpAP control the Escherichia coli division protein ZapC by proteolysis

“…As FtsZ levels are essentially constant throughout the cell cycle, spatiotemporal control of division is exercised largely through the assembly/ disassembly of the Z-ring (Rueda et al, 2003;Weart & Levin, 2003). A number of proteins that interact with FtsZ contribute to its function by modulating the dynamics of FtsZassembly (Adams & Errington, 2009;Huang et al, 2013;Lutkenhaus et al, 2012;Ortiz et al, 2016). However, the precise molecular nature of the protein-protein interactions between FtsZ and FtsZ-regulators that yield a stable but dynamic Z-ring is not completely understood as yet.…”