ftsZ

Summary

Gene Symbol: ftsZ
Description: GTP-binding tubulin-like cell division protein
Alias: ECK0096, JW0093, sfiB, sulB
Species: Escherichia coli str. K-12 substr. MG1655

Top Publications

  1. Mukherjee A, Saez C, Lutkenhaus J. Assembly of an FtsZ mutant deficient in GTPase activity has implications for FtsZ assembly and the role of the Z ring in cell division. J Bacteriol. 2001;183:7190-7 pubmed
    b>FtsZ, the ancestral homologue of eukaryotic tubulins, assembles into the Z ring, which is required for cytokinesis in prokaryotic cells. Both FtsZ and tubulin have a GTPase activity associated with polymerization...
  2. de Boer P, Crossley R, Rothfield L. The essential bacterial cell-division protein FtsZ is a GTPase. Nature. 1992;359:254-6 pubmed
    ..The biochemical mechanisms responsible for this process are poorly understood. In bacteria, the ftsZ gene product, FtsZ, is required for cell division, playing a prominent role in cytokinesis...
  3. Durand Heredia J, Yu H, De Carlo S, Lesser C, Janakiraman A. Identification and characterization of ZapC, a stabilizer of the FtsZ ring in Escherichia coli. J Bacteriol. 2011;193:1405-13 pubmed publisher
    ..of cell division occurs at the level of the assembly/disassembly process of the essential cytoskeletal protein FtsZ. A number of regulators interact with FtsZ and modulate the dynamics of the assembled FtsZ ring at the midcell ..
  4. Jennings L, Foreman K, Rush T, Tsao D, Mosyak L, Kincaid S, et al. Combinatorial synthesis of substituted 3-(2-indolyl)piperidines and 2-phenyl indoles as inhibitors of ZipA-FtsZ interaction. Bioorg Med Chem. 2004;12:5115-31 pubmed
    The ZipA-FtsZ protein-protein interaction is a potential target for antibacterial therapy. The design and parallel synthesis of a combinatorial library of small molecules, which target the FtsZ binding area on ZipA are described...
  5. Pogliano J, Pogliano K, Weiss D, Losick R, Beckwith J. Inactivation of FtsI inhibits constriction of the FtsZ cytokinetic ring and delays the assembly of FtsZ rings at potential division sites. Proc Natl Acad Sci U S A. 1997;94:559-64 pubmed
    ..In the bacterium Escherichia coli, this ring is formed by the essential cell division protein FtsZ. We have used immunofluorescence microscopy to show that FtsZ assembles early in the division cycle, suggesting ..
  6. Beuria T, Shah J, Santra M, Kumar V, Panda D. Effects of pH and ionic strength on the assembly and bundling of FtsZ protofilaments: a possible role of electrostatic interactions in the bundling of protofilaments. Int J Biol Macromol. 2006;40:30-9 pubmed
    Assembly, bundling and stability of FtsZ protofilaments are important for the formation and functioning of the cytokinetic Z-ring during bacterial division...
  7. Nova E, Montecinos F, Brunet J, Lagos R, Monasterio O. 4',6-Diamidino-2-phenylindole (DAPI) induces bundling of Escherichia coli FtsZ polymers inhibiting the GTPase activity. Arch Biochem Biophys. 2007;465:315-9 pubmed
    b>FtsZ (Filamentous temperature sensitivity Z) cell division protein from Escherichia coli binds the fluorescence probe DAPI...
  8. Camberg J, Hoskins J, Wickner S. ClpXP protease degrades the cytoskeletal protein, FtsZ, and modulates FtsZ polymer dynamics. Proc Natl Acad Sci U S A. 2009;106:10614-9 pubmed publisher
    b>FtsZ is the major cytoskeletal protein in bacteria and a tubulin homologue. It polymerizes and forms a ring where constriction occurs to divide the cell. We found that FtsZ is degraded by E. coli ClpXP, an ATP-dependent protease...
  9. Diaz Espinoza R, Garcés A, Arbildua J, Montecinos F, Brunet J, Lagos R, et al. Domain folding and flexibility of Escherichia coli FtsZ determined by tryptophan site-directed mutagenesis. Protein Sci. 2007;16:1543-56 pubmed
    b>FtsZ has two domains, the amino GTPase domain with a Rossmann fold, and the carboxyl domain that resembles the chorismate mutase fold...

More Information

Publications89

  1. Aarsman M, Piette A, Fraipont C, Vinkenvleugel T, Nguyen Distèche M, Den Blaauwen T. Maturation of the Escherichia coli divisome occurs in two steps. Mol Microbiol. 2005;55:1631-45 pubmed
    Cell division proteins FtsZ (FtsA, ZipA, ZapA), FtsE/X, FtsK, FtsQ, FtsL/B, FtsW, PBP3, FtsN and AmiC localize at mid cell in Escherichia coli in an interdependent order as listed...
  2. Hale C, de Boer P. Direct binding of FtsZ to ZipA, an essential component of the septal ring structure that mediates cell division in E. coli. Cell. 1997;88:175-85 pubmed
    b>FtsZ is a soluble, tubulin-like GTPase that forms a membrane-associated ring at the division site of bacterial cells...
  3. Flärdh K, Garrido T, Vicente M. Contribution of individual promoters in the ddlB-ftsZ region to the transcription of the essential cell-division gene ftsZ in Escherichia coli. Mol Microbiol. 1997;24:927-36 pubmed
    The essential cell-division gene ftsZ is transcribed in Escherichia coli from at least six promoters found within the coding regions of the upstream ddlB, ftsQ, and ftsA genes...
  4. Addinall S, Small E, Whitaker D, Sturrock S, Donachie W, Khattar M. New temperature-sensitive alleles of ftsZ in Escherichia coli. J Bacteriol. 2005;187:358-65 pubmed
    We isolated five new temperature-sensitive alleles of the essential cell division gene ftsZ in Escherichia coli, using P1-mediated, localized mutagenesis...
  5. RayChaudhuri D. ZipA is a MAP-Tau homolog and is essential for structural integrity of the cytokinetic FtsZ ring during bacterial cell division. EMBO J. 1999;18:2372-83 pubmed
    The first visible event in prokaryotic cell division is the assembly of the soluble, tubulin-like FtsZ GTPase into a membrane-associated cytokinetic ring that defines the division plane in bacterial and archaeal cells...
  6. Tsao D, Sutherland A, Jennings L, Li Y, Rush T, Alvarez J, et al. Discovery of novel inhibitors of the ZipA/FtsZ complex by NMR fragment screening coupled with structure-based design. Bioorg Med Chem. 2006;14:7953-61 pubmed
    ZipA is a membrane anchored protein in Escherichia coli that interacts with FtsZ, a homolog of eukaryotic tubulins, forming a septal ring structure that mediates bacterial cell division...
  7. Dajkovic A, Mukherjee A, Lutkenhaus J. Investigation of regulation of FtsZ assembly by SulA and development of a model for FtsZ polymerization. J Bacteriol. 2008;190:2513-26 pubmed publisher
    In Escherichia coli FtsZ organizes into a cytoskeletal ring structure, the Z ring, which effects cell division...
  8. Tadros M, Gonzalez J, Rivas G, Vicente M, Mingorance J. Activation of the Escherichia coli cell division protein FtsZ by a low-affinity interaction with monovalent cations. FEBS Lett. 2006;580:4941-6 pubmed
    We have investigated the activation of FtsZ by monovalent cations. FtsZ polymerization was dependent on the concentrations of protein and monovalent salts, and was accompanied by the uptake of a single ion per monomer added...
  9. Koppelman C, Aarsman M, Postmus J, Pas E, Muijsers A, Scheffers D, et al. R174 of Escherichia coli FtsZ is involved in membrane interaction and protofilament bundling, and is essential for cell division. Mol Microbiol. 2004;51:645-57 pubmed
    We investigated the interaction between FtsZ and the cytoplasmic membrane using inside-out vesicles...
  10. Liu Z, Mukherjee A, Lutkenhaus J. Recruitment of ZipA to the division site by interaction with FtsZ. Mol Microbiol. 1999;31:1853-61 pubmed
    ..As it is anchored to the membrane and interacts with FtsZ, it is a candidate for tethering FtsZ filaments to the membrane during the formation of the Z ring...
  11. Cho H, McManus H, Dove S, Bernhardt T. Nucleoid occlusion factor SlmA is a DNA-activated FtsZ polymerization antagonist. Proc Natl Acad Sci U S A. 2011;108:3773-8 pubmed publisher
    The tubulin-like FtsZ protein initiates assembly of the bacterial cytokinetic machinery by polymerizing into a ring structure, the Z ring, at the prospective site of division...
  12. Dai K, Lutkenhaus J. The proper ratio of FtsZ to FtsA is required for cell division to occur in Escherichia coli. J Bacteriol. 1992;174:6145-51 pubmed
    ..in Escherichia coli were investigated by examining the effect on cell division of increasing the expression of the ftsZ, ftsA, or ftsQ genes...
  13. Anderson D, Gueiros Filho F, Erickson H. Assembly dynamics of FtsZ rings in Bacillus subtilis and Escherichia coli and effects of FtsZ-regulating proteins. J Bacteriol. 2004;186:5775-81 pubmed
    b>FtsZ is the major cytoskeletal component of the bacterial cell division machinery. It forms a ring-shaped structure (the Z ring) that constricts as the bacterium divides...
  14. Santra M, Beuria T, Banerjee A, Panda D. Ruthenium red-induced bundling of bacterial cell division protein, FtsZ. J Biol Chem. 2004;279:25959-65 pubmed
    The assembly of FtsZ plays a major role in bacterial cell division, and it is thought that the assembly dynamics of FtsZ is a finely regulated process. Here, we show that ruthenium red is able to modulate FtsZ assembly in vitro...
  15. Mosyak L, Zhang Y, Glasfeld E, Haney S, Stahl M, Seehra J, et al. The bacterial cell-division protein ZipA and its interaction with an FtsZ fragment revealed by X-ray crystallography. EMBO J. 2000;19:3179-91 pubmed
    In Escherichia coli, FtsZ, a homologue of eukaryotic tubulins, and ZipA, a membrane-anchored protein that binds to FtsZ, are two essential components of the septal ring structure that mediates cell division...
  16. Erickson H. Modeling the physics of FtsZ assembly and force generation. Proc Natl Acad Sci U S A. 2009;106:9238-43 pubmed publisher
    The tubulin homolog FtsZ is the major cytoskeletal protein in bacterial cytokinesis. It can generate a constriction force on the bacterial membrane or inside tubular liposomes...
  17. Gonzalez J, Velez M, Jimenez M, Alfonso C, Schuck P, Mingorance J, et al. Cooperative behavior of Escherichia coli cell-division protein FtsZ assembly involves the preferential cyclization of long single-stranded fibrils. Proc Natl Acad Sci U S A. 2005;102:1895-900 pubmed
    ..to explain the previously posed question of how a single-stranded filament of the bacterial cell-division protein FtsZ can assemble in an apparently cooperative manner...
  18. Huecas S, Llorca O, Boskovic J, Martín Benito J, Valpuesta J, Andreu J. Energetics and geometry of FtsZ polymers: nucleated self-assembly of single protofilaments. Biophys J. 2008;94:1796-806 pubmed
    Essential cell division protein FtsZ is an assembling GTPase which directs the cytokinetic ring formation in dividing bacterial cells...
  19. Bernhardt T, de Boer P. SlmA, a nucleoid-associated, FtsZ binding protein required for blocking septal ring assembly over Chromosomes in E. coli. Mol Cell. 2005;18:555-64 pubmed
    Cell division in Escherichia coli begins with assembly of the tubulin-like FtsZ protein into a ring structure just underneath the cell membrane...
  20. Mukherjee A, Lutkenhaus J. Dynamic assembly of FtsZ regulated by GTP hydrolysis. EMBO J. 1998;17:462-9 pubmed
    b>FtsZ forms a cytokinetic ring, designated the Z ring, that directs cytokinesis in prokaryotes...
  21. Tonthat N, Milam S, Chinnam N, Whitfill T, Margolin W, Schumacher M. SlmA forms a higher-order structure on DNA that inhibits cytokinetic Z-ring formation over the nucleoid. Proc Natl Acad Sci U S A. 2013;110:10586-91 pubmed publisher
    The spatial and temporal control of Filamenting temperature sensitive mutant Z (FtsZ) Z-ring formation is crucial for proper cell division in bacteria...
  22. Hu Z, Lutkenhaus J. Analysis of MinC reveals two independent domains involved in interaction with MinD and FtsZ. J Bacteriol. 2000;182:3965-71 pubmed
    In Escherichia coli FtsZ assembles into a Z ring at midcell while assembly at polar sites is prevented by the min system...
  23. Dai K, Lutkenhaus J. ftsZ is an essential cell division gene in Escherichia coli. J Bacteriol. 1991;173:3500-6 pubmed
    The ftsZ gene is thought to be an essential cell division gene in Escherichia coli. We constructed a null allele of ftsZ in a strain carrying additional copies of ftsZ on a plasmid with a temperature-sensitive replication defect...
  24. Geissler B, Shiomi D, Margolin W. The ftsA* gain-of-function allele of Escherichia coli and its effects on the stability and dynamics of the Z ring. Microbiology. 2007;153:814-25 pubmed
    Formation of the FtsZ ring (Z ring) in Escherichia coli is the first step in the assembly of the divisome, a protein machine required for cell division...
  25. Hale C, Rhee A, de Boer P. ZipA-induced bundling of FtsZ polymers mediated by an interaction between C-terminal domains. J Bacteriol. 2000;182:5153-66 pubmed
    b>FtsZ and ZipA are essential components of the septal ring apparatus, which mediates cell division in Escherichia coli. FtsZ is a cytoplasmic tubulin-like GTPase that forms protofilament-like homopolymers in vitro...
  26. Romberg L, Levin P. Assembly dynamics of the bacterial cell division protein FTSZ: poised at the edge of stability. Annu Rev Microbiol. 2003;57:125-54 pubmed
    b>FtsZ is a prokaryotic tubulin homolog that assembles into a ring at the future site of cell division...
  27. Hu Z, Mukherjee A, Pichoff S, Lutkenhaus J. The MinC component of the division site selection system in Escherichia coli interacts with FtsZ to prevent polymerization. Proc Natl Acad Sci U S A. 1999;96:14819-24 pubmed
    ..We find that MalE-MinC interacts with FtsZ and prevents polymerization without inhibiting FtsZ's GTPase activity...
  28. Mendieta J, Rico A, López Viñas E, Vicente M, Mingorance J, Gomez Puertas P. Structural and functional model for ionic (K(+)/Na(+)) and pH dependence of GTPase activity and polymerization of FtsZ, the prokaryotic ortholog of tubulin. J Mol Biol. 2009;390:17-25 pubmed publisher
    Bacterial cell division occurs through the formation of a protein ring (division ring) at the site of division, with FtsZ being its main component in most bacteria...
  29. Raskin D, de Boer P. The MinE ring: an FtsZ-independent cell structure required for selection of the correct division site in E. coli. Cell. 1997;91:685-94 pubmed
    E. coli cell division is mediated by the FtsZ ring and associated factors...
  30. Jennings L, Foreman K, Rush T, Tsao D, Mosyak L, Li Y, et al. Design and synthesis of indolo[2,3-a]quinolizin-7-one inhibitors of the ZipA-FtsZ interaction. Bioorg Med Chem Lett. 2004;14:1427-31 pubmed
    The binding of FtsZ to ZipA is a potential target for antibacterial therapy...
  31. RayChaudhuri D, Park J. Escherichia coli cell-division gene ftsZ encodes a novel GTP-binding protein. Nature. 1992;359:251-4 pubmed
    ..coli cell division, ftsZ plays a central role at the earliest known step of septation...
  32. Herring C, Blattner F. Conditional lethal amber mutations in essential Escherichia coli genes. J Bacteriol. 2004;186:2673-81 pubmed
    ..We were unable to isolate an amber mutation in ftsZ. Kinetics of cell death and morphological changes were measured following removal of arabinose...
  33. Buss J, Coltharp C, Huang T, Pohlmeyer C, Wang S, Hatem C, et al. In vivo organization of the FtsZ-ring by ZapA and ZapB revealed by quantitative super-resolution microscopy. Mol Microbiol. 2013;89:1099-120 pubmed publisher
    In most bacterial cells, cell division is dependent on the polymerization of the FtsZ protein to form a ring-like structure (Z-ring) at the midcell. Despite its essential role, the molecular architecture of the Z-ring remains elusive...
  34. Pla J, Sanchez M, Palacios P, Vicente M, Aldea M. Preferential cytoplasmic location of FtsZ, a protein essential for Escherichia coli septation. Mol Microbiol. 1991;5:1681-6 pubmed
    An ftsZ thermonull mutant has been constructed in which the ftsZ gene has been deleted from the Escherichia coli chromosome while maintaining a wild-type copy of the gene in a thermosensitive plasmid...
  35. Sun Q, Yu X, Margolin W. Assembly of the FtsZ ring at the central division site in the absence of the chromosome. Mol Microbiol. 1998;29:491-503 pubmed
    The FtsZ ring assembles between segregated daughter chromosomes in prokaryotic cells and is essential for cell division...
  36. Lan G, Daniels B, Dobrowsky T, Wirtz D, Sun S. Condensation of FtsZ filaments can drive bacterial cell division. Proc Natl Acad Sci U S A. 2009;106:121-6 pubmed publisher
    ..Instead, a division ring (Z-ring) consists of mostly FtsZ, FtsA, and ZipA is used to exerting a contractile force...
  37. Errington J, Daniel R, Scheffers D. Cytokinesis in bacteria. Microbiol Mol Biol Rev. 2003;67:52-65, table of contents pubmed
    ..b>FtsZ is a cytosolic tubulin-like protein that polymerizes into an oligomeric structure that forms the initial ring at ..
  38. Pichoff S, Lutkenhaus J. Escherichia coli division inhibitor MinCD blocks septation by preventing Z-ring formation. J Bacteriol. 2001;183:6630-5 pubmed publisher
    ..MinCD prevented the localization of both FtsZ-GFP and ZipA-GFP, consistent with it preventing Z-ring assembly...
  39. Begg K, Nikolaichik Y, Crossland N, Donachie W. Roles of FtsA and FtsZ in activation of division sites. J Bacteriol. 1998;180:881-4 pubmed
    Increasing FtsZ induces the formation of minicells at cell poles but does not increase the frequency or timing of central divisions...
  40. Chen Y, Erickson H. FtsZ filament dynamics at steady state: subunit exchange with and without nucleotide hydrolysis. Biochemistry. 2009;48:6664-73 pubmed publisher
    We have measured three aspects of FtsZ filament dynamics at steady state: rates of GTP hydrolysis, subunit exchange between protofilaments, and disassembly induced by dilution or excess GDP...
  41. Osawa M, Anderson D, Erickson H. Curved FtsZ protofilaments generate bending forces on liposome membranes. EMBO J. 2009;28:3476-84 pubmed publisher
    We have created FtsZ-YFP-mts where an amphipathic helix on the C-terminus tethers FtsZ to the membrane. When incorporated inside multi-lamellar tubular liposomes, FtsZ-YFP-mts can assemble Z rings that generate a constriction force...
  42. Shiomi D, Margolin W. Dimerization or oligomerization of the actin-like FtsA protein enhances the integrity of the cytokinetic Z ring. Mol Microbiol. 2007;66:1396-415 pubmed
    In bacteria, the actin-like FtsA protein interacts with the tubulin-like FtsZ protein, helping to assemble the cytokinetic Z ring, anchor it to the cytoplasmic membrane and recruit other essential divisome proteins...
  43. Dajkovic A, Pichoff S, Lutkenhaus J, Wirtz D. Cross-linking FtsZ polymers into coherent Z rings. Mol Microbiol. 2010;78:651-68 pubmed publisher
    ..Here we report that a widely conserved FtsZ binding protein, ZapA, has cytological, biochemical and biophysical properties that argue for the importance of ..
  44. Den Blaauwen T, de Pedro M, Nguyen Distèche M, Ayala J. Morphogenesis of rod-shaped sacculi. FEMS Microbiol Rev. 2008;32:321-44 pubmed publisher
    ..Although this multifunctionality and flexibility form a barrier to the functional elucidation of its individual subunits, it helps the cells to survive a variety of emergency situations and to proliferate securely. ..
  45. Hale C, Shiomi D, Liu B, Bernhardt T, Margolin W, Niki H, et al. Identification of Escherichia coli ZapC (YcbW) as a component of the division apparatus that binds and bundles FtsZ polymers. J Bacteriol. 2011;193:1393-404 pubmed publisher
    ..This process involves the accumulation of FtsZ polymers at midcell and their interaction with several FtsZ-binding proteins that collectively organize the ..
  46. Vicente M, Rico A. The order of the ring: assembly of Escherichia coli cell division components. Mol Microbiol. 2006;61:5-8 pubmed
    ..In addition, back-recruitment of all late proteins except FtsN into the division ring occurs even in the absence of proteins incorporated at earlier stages, i.e. FtsA or FtsQ. ..
  47. Dajkovic A, Lan G, Sun S, Wirtz D, Lutkenhaus J. MinC spatially controls bacterial cytokinesis by antagonizing the scaffolding function of FtsZ. Curr Biol. 2008;18:235-44 pubmed publisher
    ..The Z ring is composed of FtsZ filaments, but their organization in the Z ring is poorly understood...
  48. Osawa M, Anderson D, Erickson H. Reconstitution of contractile FtsZ rings in liposomes. Science. 2008;320:792-4 pubmed publisher
    b>FtsZ is a tubulin homolog and the major cytoskeletal protein in bacterial cell division. It assembles into the Z ring, which contains FtsZ and a dozen other division proteins, and constricts to divide the cell...
  49. Popp D, Iwasa M, Narita A, Erickson H, Maeda Y. FtsZ condensates: an in vitro electron microscopy study. Biopolymers. 2009;91:340-50 pubmed publisher
    In vivo cell division protein FtsZ from E. coli forms rings and spirals which have only been observed by low resolution light microscopy...
  50. Wang X, Possoz C, Sherratt D. Dancing around the divisome: asymmetric chromosome segregation in Escherichia coli. Genes Dev. 2005;19:2367-77 pubmed
    ..By mid-S phase, FtsZ forms a ring at mid-cell at the time of initiation of nucleoid separation; ter remains polar...
  51. Yu X, Margolin W. FtsZ ring clusters in min and partition mutants: role of both the Min system and the nucleoid in regulating FtsZ ring localization. Mol Microbiol. 1999;32:315-26 pubmed
    ..To understand further the role of the nucleoid and the min system in selection of the cell division site, we examined FtsZ localization in Escherichia coli cells lacking MinCDE and in parC mutants defective in chromosome segregation...
  52. Ma X, Margolin W. Genetic and functional analyses of the conserved C-terminal core domain of Escherichia coli FtsZ. J Bacteriol. 1999;181:7531-44 pubmed
    In Escherichia coli, FtsZ is required for the recruitment of the essential cell division proteins FtsA and ZipA to the septal ring. Several C-terminal deletions of E...
  53. Shen B, Lutkenhaus J. Examination of the interaction between FtsZ and MinCN in E. coli suggests how MinC disrupts Z rings. Mol Microbiol. 2010;75:1285-98 pubmed publisher
    ..The MinC protein has two domains of equal size and both domains can target FtsZ and block cell division in the proper context...
  54. Durand Heredia J, Rivkin E, Fan G, Morales J, Janakiraman A. Identification of ZapD as a cell division factor that promotes the assembly of FtsZ in Escherichia coli. J Bacteriol. 2012;194:3189-98 pubmed publisher
    The tubulin homolog FtsZ forms a polymeric membrane-associated ring structure (Z ring) at midcell that establishes the site of division and provides an essential framework for the localization of a multiprotein molecular machine that ..
  55. Chen Y, Bjornson K, Redick S, Erickson H. A rapid fluorescence assay for FtsZ assembly indicates cooperative assembly with a dimer nucleus. Biophys J. 2005;88:505-14 pubmed
    b>FtsZ is the major cytoskeletal protein operating in bacterial cell division. FtsZ assembles into protofilaments in vitro, and there has been some controversy over whether the assembly is isodesmic or cooperative...
  56. Jaffe A, D Ari R, Norris V. SOS-independent coupling between DNA replication and cell division in Escherichia coli. J Bacteriol. 1986;165:66-71 pubmed
    ..was used to evaluate the efficiency of this coupling mechanism, which seems to involve the cell division protein FtsZ (SulB), also known to be the target of the division inhibitors SfiA and SfiC...
  57. Bramhill D, Thompson C. GTP-dependent polymerization of Escherichia coli FtsZ protein to form tubules. Proc Natl Acad Sci U S A. 1994;91:5813-7 pubmed
    The FtsZ protein is a GTPase that is essential for cell division in Escherichia coli. During cytokinesis, FtsZ localizes to a ring at the leading edge of septum synthesis...
  58. Mukherjee A, Lutkenhaus J. Guanine nucleotide-dependent assembly of FtsZ into filaments. J Bacteriol. 1994;176:2754-8 pubmed
    b>FtsZ is an essential cell division protein that is localized to the leading edge of the bacterial septum in a cytokinetic ring. It contains the tubulin signature motif and is a GTP binding protein with a GTPase activity...
  59. Bi E, Lutkenhaus J. Isolation and characterization of ftsZ alleles that affect septal morphology. J Bacteriol. 1992;174:5414-23 pubmed
    The ftsZ gene encodes an essential cell division protein that specifically localizes to the septum of dividing cells. In this study we characterized the effects of the ftsZ2(Rsa) mutation on cell physiology...
  60. Mingorance J, Tadros M, Vicente M, Gonzalez J, Rivas G, Velez M. Visualization of single Escherichia coli FtsZ filament dynamics with atomic force microscopy. J Biol Chem. 2005;280:20909-14 pubmed
    b>FtsZ, the prokaryotic homologue of tubulin, is an essential cell division protein. In the cell, it localizes at the center, forming a ring that constricts during division...
  61. Addinall S, Holland B. The tubulin ancestor, FtsZ, draughtsman, designer and driving force for bacterial cytokinesis. J Mol Biol. 2002;318:219-36 pubmed
    We discuss in this review the regulation of synthesis and action of FtsZ, its structure in relation to tubulin and microtubules, and the mechanism of polymerization and disassembly (contraction) of FtsZ rings from a specific nucleation ..
  62. Thanedar S, Margolin W. FtsZ exhibits rapid movement and oscillation waves in helix-like patterns in Escherichia coli. Curr Biol. 2004;14:1167-73 pubmed
    Prokaryotes contain cytoskeletal proteins such as the tubulin-like FtsZ, which forms the Z ring at the cell center for cytokinesis, and the actin-like MreB, which forms a helix along the long axis of the cell and is required for shape ..
  63. Rueda S, Vicente M, Mingorance J. Concentration and assembly of the division ring proteins FtsZ, FtsA, and ZipA during the Escherichia coli cell cycle. J Bacteriol. 2003;185:3344-51 pubmed
    The concentration of the cell division proteins FtsZ, FtsA, and ZipA and their assembly into a division ring during the Escherichia coli B/r K cell cycle have been measured in synchronous cultures obtained by the membrane elution ..
  64. Romberg L, Mitchison T. Rate-limiting guanosine 5'-triphosphate hydrolysis during nucleotide turnover by FtsZ, a prokaryotic tubulin homologue involved in bacterial cell division. Biochemistry. 2004;43:282-8 pubmed
    b>FtsZ is a prokaryotic tubulin homologue that polymerizes into a dynamic ring during cell division. GTP binding and hydrolysis provide the energy for FtsZ dynamics...
  65. Weart R, Levin P. Growth rate-dependent regulation of medial FtsZ ring formation. J Bacteriol. 2003;185:2826-34 pubmed
    b>FtsZ is an essential cell division protein conserved throughout the bacteria and archaea. In response to an unknown cell cycle signal, FtsZ polymerizes into a ring that establishes the future division site...
  66. Shiomi D, Margolin W. The C-terminal domain of MinC inhibits assembly of the Z ring in Escherichia coli. J Bacteriol. 2007;189:236-43 pubmed
    In Escherichia coli, the Min system, consisting of three proteins, MinC, MinD, and MinE, negatively regulates FtsZ assembly at the cell poles, helping to ensure that the Z ring will assemble only at midcell...
  67. Fu G, Huang T, Buss J, Coltharp C, Hensel Z, Xiao J. In vivo structure of the E. coli FtsZ-ring revealed by photoactivated localization microscopy (PALM). PLoS ONE. 2010;5:e12682 pubmed publisher
    The FtsZ protein, a tubulin-like GTPase, plays a pivotal role in prokaryotic cell division. In vivo it localizes to the midcell and assembles into a ring-like structure-the Z-ring...
  68. Geissler B, Elraheb D, Margolin W. A gain-of-function mutation in ftsA bypasses the requirement for the essential cell division gene zipA in Escherichia coli. Proc Natl Acad Sci U S A. 2003;100:4197-202 pubmed
    ZipA and FtsA are recruited independently to the FtsZ cytokinetic ring (Z ring) and are essential for cell division of Escherichia coli...
  69. Mohammadi T, Ploeger G, Verheul J, Comvalius A, Martos A, Alfonso C, et al. The GTPase activity of Escherichia coli FtsZ determines the magnitude of the FtsZ polymer bundling by ZapA in vitro. Biochemistry. 2009;48:11056-66 pubmed publisher
    b>FtsZ polymerizes in a ring-like structure at mid cell to initiate cell division in Escherichia coli. The ring is stabilized by a number of proteins among which the widely conserved ZapA protein...
  70. Small E, Marrington R, Rodger A, Scott D, Sloan K, Roper D, et al. FtsZ polymer-bundling by the Escherichia coli ZapA orthologue, YgfE, involves a conformational change in bound GTP. J Mol Biol. 2007;369:210-21 pubmed
    ..driven by a dynamic, ring-shaped, cytoskeletal element (the Z-ring) made up of polymers of the tubulin-like protein FtsZ. It is thought that lateral associations between FtsZ polymers are important for function of the Z-ring in vivo, ..
  71. Weiss D. Bacterial cell division and the septal ring. Mol Microbiol. 2004;54:588-97 pubmed
    ..The foundation of the septal ring is a polymer of the tubulin-like protein FtsZ. Recently, experiments using fluorescence recovery after photobleaching have revealed that the Z ring is extremely ..
  72. Sun Q, Margolin W. Influence of the nucleoid on placement of FtsZ and MinE rings in Escherichia coli. J Bacteriol. 2001;183:1413-22 pubmed
    ..but unsegregated nucleoids, along with the Min system, act as topological inhibitors to restrict assembly of the FtsZ ring (Z ring) to discrete sites in the cell...
  73. Ebersbach G, Galli E, Møller Jensen J, Lowe J, Gerdes K. Novel coiled-coil cell division factor ZapB stimulates Z ring assembly and cell division. Mol Microbiol. 2008;68:720-35 pubmed publisher
    ..Localization of ZapB to the divisome depended on FtsZ but not FtsA, ZipA or FtsI, and ZapB interacted with FtsZ in a bacterial two-hybrid analysis...
  74. Varma A, Young K. FtsZ collaborates with penicillin binding proteins to generate bacterial cell shape in Escherichia coli. J Bacteriol. 2004;186:6768-74 pubmed
    ..certain ftsZ84 strains lyse at the nonpermissive temperature instead of filamenting, and inhibition of wild-type FtsZ forces some mutants into tightly wound spirillum-like morphologies...
  75. Allard J, Cytrynbaum E. Force generation by a dynamic Z-ring in Escherichia coli cell division. Proc Natl Acad Sci U S A. 2009;106:145-50 pubmed publisher
    b>FtsZ, a bacterial homologue of tubulin, plays a central role in bacterial cell division...
  76. Kenny C, Ding W, Kelleher K, Benard S, Dushin E, Sutherland A, et al. Development of a fluorescence polarization assay to screen for inhibitors of the FtsZ/ZipA interaction. Anal Biochem. 2003;323:224-33 pubmed
    A fluorescence polarization competition assay has been developed to screen for inhibitors of the Escherichia coli FtsZ/ZipA protein-protein interaction...
  77. Ma X, Ehrhardt D, Margolin W. Colocalization of cell division proteins FtsZ and FtsA to cytoskeletal structures in living Escherichia coli cells by using green fluorescent protein. Proc Natl Acad Sci U S A. 1996;93:12998-3003 pubmed
    In the current model for bacterial cell division, FtsZ protein forms a ring that marks the division plane, creating a cytoskeletal framework for the subsequent action of other proteins such as FtsA...
  78. Niu L, Yu J. Investigating intracellular dynamics of FtsZ cytoskeleton with photoactivation single-molecule tracking. Biophys J. 2008;95:2009-16 pubmed publisher
    ..the technique of photoactivation single-molecule tracking by investigating the mobility dynamics of intracellular FtsZ protein molecules in live Escherichia coli cells...
  79. Söderström B, Skoog K, Blom H, Weiss D, von Heijne G, Daley D. Disassembly of the divisome in Escherichia coli: evidence that FtsZ dissociates before compartmentalization. Mol Microbiol. 2014;92:1-9 pubmed publisher
    ..b>FtsZ is the first of the divisome proteins to accumulate at the division site and is widely thought to function as a ..
  80. Chen Y, Erickson H. Rapid in vitro assembly dynamics and subunit turnover of FtsZ demonstrated by fluorescence resonance energy transfer. J Biol Chem. 2005;280:22549-54 pubmed
    We have developed an assay for the assembly of FtsZ based on fluorescence resonance energy transfer (FRET)...