Form and function of the bacterial cytokinetic ring

Meier, Elizabeth L.; Goley, Erin D.

doi:10.1016/j.ceb.2013.08.006

Cited by 82 publications

(60 citation statements)

References 59 publications

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“…One possibility that has garnered much attention in the last decade is a 'Z-ring-centric' model in which the Z-ring is analogous to the contractile actomyosin ring in eukaryotic cells: the Z-ring is thought to actively pull the cytoplasmic membrane inward, and septal PG growth follows passively behind (28). Such a model predicts that Z-ring contraction limits the progression of septum closure and is distinct from a model in which new septal PG growth actively pushes from the outside of the cytoplasmic membrane (27). In this latter model, PG synthesis limits the rate of septum closure, and the Z-ring acts as a scaffold that passively follows the closing septum (29).…”

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confidence: 99%

“…In this latter model, PG synthesis limits the rate of septum closure, and the Z-ring acts as a scaffold that passively follows the closing septum (29). Alternatively, Z-ring contraction and septal cell wall synthesis may work together to drive constriction; in which case, progression of septum closure would be regulated by both processes (27).…”

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confidence: 99%

“…However, the divisome component responsible for generating such a force remains unclear (27). One possibility that has garnered much attention in the last decade is a 'Z-ring-centric' model in which the Z-ring is analogous to the contractile actomyosin ring in eukaryotic cells: the Z-ring is thought to actively pull the cytoplasmic membrane inward, and septal PG growth follows passively behind (28).…”

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confidence: 99%

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Defining the rate-limiting processes of bacterial cytokinesis

Coltharp

Buss

Plumer

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

161

216

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Bacterial cytokinesis is accomplished by the essential ‘divisome’ machinery. The most widely conserved divisome component, FtsZ, is a tubulin homolog that polymerizes into the ‘FtsZ-ring’ (‘Z-ring’). Previous in vitro studies suggest that Z-ring contraction serves as a major constrictive force generator to limit the progression of cytokinesis. Here, we applied quantitative superresolution imaging to examine whether and how Z-ring contraction limits the rate of septum closure during cytokinesis in Escherichia coli cells. Surprisingly, septum closure rate was robust to substantial changes in all Z-ring properties proposed to be coupled to force generation: FtsZ’s GTPase activity, Z-ring density, and the timing of Z-ring assembly and disassembly. Instead, the rate was limited by the activity of an essential cell wall synthesis enzyme and further modulated by a physical divisome–chromosome coupling. These results challenge a Z-ring–centric view of bacterial cytokinesis and identify cell wall synthesis and chromosome segregation as limiting processes of cytokinesis.

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confidence: 99%

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Defining the rate-limiting processes of bacterial cytokinesis

Coltharp

Buss

Plumer

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

161

216

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“…3 The essential cell division protein FtsZ assembles into the Z ring that determines the division plane and recruits the remainder of the cytokinetic machinery in most bacteria. 13,14 FtsZ is a structural homologue of eukaryotic tubulin, and both are distinct GTPases whose interfacial active site is formed by the association of consecutive monomers, upon assembly into similar polar protofilaments. 15 GTP binding is required for assembly, and its hydrolysis to GDP triggers disassembly, giving rise to microtubule dynamic instability 16 and FtsZ polymer dynamics.…”

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Beyond a Fluorescent Probe: Inhibition of Cell Division Protein FtsZ by mant-GTP Elucidated by NMR and Biochemical Approaches

et al. 2015

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FtsZ is the organizer of cell division in most bacteria and a target in the quest for new antibiotics. FtsZ is a tubulin-like GTPase, in which the active site is completed at the interface with the next subunit in an assembled FtsZ filament. Fluorescent mant-GTP has been extensively used for competitive binding studies of nucleotide analogs and synthetic GTPreplacing inhibitors possessing antibacterial activity. However, its mode of binding and whether the mant tag interferes with FtsZ assembly function were unknown. Mant-GTP exists in equilibrium as a mixture of C2′-and C3′-substituted isomers. We have unraveled the molecular recognition process of mant-GTP by FtsZ monomers. Both isomers bind in the anti glycosidic bond conformation: 2′-mant-GTP in two ribose puckering conformations and 3′-mant-GTP in the preferred C2′ endo conformation. In each case, the mant tag strongly interacts with FtsZ at an extension of the GTP binding site, which is also supported by molecular dynamics simulations. Importantly, mant-GTP binding induces archaeal FtsZ polymerization into inactive curved filaments that cannot hydrolyze the nucleotide, rather than straight GTP-hydrolyzing assemblies, and also inhibits normal assembly of FtsZ from the Gram-negative bacterium Escherichia coli but is hydrolyzed by FtsZ from Gram-positive Bacillus subtilis. Thus, the specific interactions provided by the fluorescent mant tag indicate a new way to search for synthetic FtsZ inhibitors that selectively suppress the cell division of bacterial pathogens.

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“…Uma questão ainda não resolvida é a origem da força que promove o invaginamento da membrana plasmática e o crescimento interno da parede celular. As evidencias que FtsZ é capaz de gerar essa força constritora in vitro são convincentes (Meier e Goley, 2014). Os dados atuais demostraram que a reciclagem de subunidades de FtsZ no filamento é 17 fundamental para a constrição acontecer (Osawa e Erickson, 2011).…”

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Caracterização da interação entre o regulador espacial MinC e seu alvo FtsZ em Bacillus subtilis

Blasios¹

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VALDIR BLASIOS JUNIOR Caracterização da interação entre o regulador espacial MinC e seu alvo FtsZ em Bacillus subtilisBacterial cell division is orchestrated by FtsZ, a protein homologous to eukaryotic tubulin that has the ability to polymerize and generate a cytoplasmic structure called the Z ring. The subcellular location where this cytoskeletal structure is formed determines the future division site. The MinCD complex is one of the main regulators of the position of cell division, driving the assembly of Z-ring precisely at the medial region of the cell. MinCD acts as a site-specific inhibitor of FtsZ polymerization, blocking Z ring formation at the cell poles. MinC is the protein of the complex that acts directly on FtsZ and inhibits its polymerization. This thesis elucidates the interaction between FtsZ and MinC and suggests the MinC mechanism in Bacillus subtilis. An ftsZ randomly mutagenized library was screened to identify mutants that are resistant to MinC action. Using right-angle light scattering and fluorescence spectroscopy we showed that substitutions K243R and D287V lost the interaction to MinC. These substituted residues clustered around the H-9 and H-10 helices in the C-terminal domain of FtsZ, thus, we conclude that this region is the binding site for MinC.In addition to mapping the MinC binding site on FtsZ, we also identified the FtsZ binding site in MinC. Based on residue conservation, NMR experiments and exposure to solvent, we chose residues of MinC for mutagenesis and characterization. The substituted residues that disrupted MinC ability to inhibit FtsZ polymerization in vitro were: Y8 and K12 (β-1), K15 (turn-2), H55 (β-3), H84 (β-4) and K149 (C-terminal). Thus, we conclude that the binding site of MinC for FtsZ is located on the only β sheet at the N-terminal domain of MinC from B. subtilis.Finally, based on the binding sites of the two proteins mapped experimentally, we created a model of the complex between MinC and FtsZ by molecular docking.According to the generated model, MinC interacts with the lateral portion of FtsZ polymers. This indicates that MinC should inhibit assembly of higher order FtsZ polymers, thereby preventing the formation of a functional Z-ring. This mechanism of Min is different from that proposed in E. coli, in which MinC interacts with FtsZ polymerization interface and inhibits FtsZ protofilament formation.Keywords: Cell division, FtsZ, MinC, Z-ring, cytoskeleton, protein-protein interaction. (Oliva, et al., 2004). Os contatos longitudinais do filamento são similares entre FtsZ e tubulina (Erickson et al., 1996). A semelhança estrutural e dos polímeros de FtsZ, quando comparado à tubulina eucariótica, se devem ao fato dessas duas proteínas derivarem de um ancestral comum (Erickson et al., 1996) (Lowe e Amos, 1998). LISTA DE ABREVIATURAS E SIGLAS Reguladores negativosDentre os reguladores negativos da polimerização de FtsZ que foram identificados até o momento, SulA e MinC são os melhores estudados. Porém, alguns inibidores como Noc/SlmA e EzrA tem destaque...

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Form and function of the bacterial cytokinetic ring

Cited by 82 publications

References 59 publications

Defining the rate-limiting processes of bacterial cytokinesis

Defining the rate-limiting processes of bacterial cytokinesis

Beyond a Fluorescent Probe: Inhibition of Cell Division Protein FtsZ by mant-GTP Elucidated by NMR and Biochemical Approaches

Caracterização da interação entre o regulador espacial MinC e seu alvo FtsZ em Bacillus subtilis

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