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Volumn 18, Issue 8, 2010, Pages 348-356

Strong FtsZ is with the force: Mechanisms to constrict bacteria

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; FTSZ PROTEIN; GUANOSINE TRIPHOSPHATE; UNCLASSIFIED DRUG; ZAPA PROTEIN; ZIPA PROTEIN; CELL WALL SKELETON; CYTOSKELETON PROTEIN; FTSZ PROTEIN, BACTERIA; GUANOSINE TRIPHOSPHATASE;

EID: 77955271619     PISSN: 0966842X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tim.2010.06.001     Document Type: Review
Times cited : (111)

References (79)
  • 1
    • 0032492953 scopus 로고    scopus 로고
    • Cytoskeletal proteins: the evolution of cell division
    • Faguy D.M., Doolittle W.F. Cytoskeletal proteins: the evolution of cell division. Curr. Biol. 1998, 8:R338-R341.
    • (1998) Curr. Biol. , vol.8
    • Faguy, D.M.1    Doolittle, W.F.2
  • 2
    • 0031895073 scopus 로고    scopus 로고
    • Regulation of transcription of cell division genes in the Escherichia coli dcw cluster
    • Vicente M., et al. Regulation of transcription of cell division genes in the Escherichia coli dcw cluster. Cell Mol. Life Sci. 1998, 54:317-324.
    • (1998) Cell Mol. Life Sci. , vol.54 , pp. 317-324
    • Vicente, M.1
  • 3
    • 0035282861 scopus 로고    scopus 로고
    • Bringing gene order into bacterial shape
    • Tamames J., et al. Bringing gene order into bacterial shape. Trends Genet. 2001, 17:124-126.
    • (2001) Trends Genet. , vol.17 , pp. 124-126
    • Tamames, J.1
  • 4
    • 4544221748 scopus 로고    scopus 로고
    • Genomic channeling in bacterial cell division
    • Mingorance J., et al. Genomic channeling in bacterial cell division. J. Mol. Recognit. 2004, 17:481-487.
    • (2004) J. Mol. Recognit. , vol.17 , pp. 481-487
    • Mingorance, J.1
  • 5
    • 0036558591 scopus 로고    scopus 로고
    • Molecular evolution before the origin of the species
    • Davis B.K. Molecular evolution before the origin of the species. Prog. Biophys. Mol. Biol. 2002, 79:77-133.
    • (2002) Prog. Biophys. Mol. Biol. , vol.79 , pp. 77-133
    • Davis, B.K.1
  • 6
    • 50349088658 scopus 로고    scopus 로고
    • Investigating intracellular dynamics of FtsZ cytoskeleton with photo-activation single molecule tracking
    • Niu L., Yu J. Investigating intracellular dynamics of FtsZ cytoskeleton with photo-activation single molecule tracking. Biophys. J. 2008, 95:2009-2016.
    • (2008) Biophys. J. , vol.95 , pp. 2009-2016
    • Niu, L.1    Yu, J.2
  • 7
    • 0037022642 scopus 로고    scopus 로고
    • Rapid assembly dynamics of the Escherichia coli FtsZ-ring demonstrated by fluorescence recovery after photobleaching
    • Stricker J., et al. Rapid assembly dynamics of the Escherichia coli FtsZ-ring demonstrated by fluorescence recovery after photobleaching. Proc. Natl. Acad. Sci. U. S. A. 2002, 99:3171-3175.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 3171-3175
    • Stricker, J.1
  • 8
    • 0038191051 scopus 로고    scopus 로고
    • Concentration and assembly of the division ring proteins FtsZ, FtsA, and ZipA during the Escherichia coli cell cycle
    • Rueda S., et al. Concentration and assembly of the division ring proteins FtsZ, FtsA, and ZipA during the Escherichia coli cell cycle. J. Bacteriol. 2003, 185:3344-3351.
    • (2003) J. Bacteriol. , vol.185 , pp. 3344-3351
    • Rueda, S.1
  • 9
    • 3142602980 scopus 로고    scopus 로고
    • FtsZ exhibits rapid movement and oscillation waves in helix-like patterns in Escherichia coli
    • Thanedar S., Margolin W. FtsZ exhibits rapid movement and oscillation waves in helix-like patterns in Escherichia coli. Curr. Biol. 2004, 14:1167-1173.
    • (2004) Curr. Biol. , vol.14 , pp. 1167-1173
    • Thanedar, S.1    Margolin, W.2
  • 10
    • 33644778043 scopus 로고    scopus 로고
    • Trapping of a spiral-like intermediate of the bacterial cytokinetic protein FtsZ
    • Michie K.A., et al. Trapping of a spiral-like intermediate of the bacterial cytokinetic protein FtsZ. J. Bacteriol. 2006, 188:1680-1690.
    • (2006) J. Bacteriol. , vol.188 , pp. 1680-1690
    • Michie, K.A.1
  • 11
    • 36248938686 scopus 로고    scopus 로고
    • The structure of FtsZ filaments in vivo suggests a force-generating role in cell division
    • Li Z., et al. The structure of FtsZ filaments in vivo suggests a force-generating role in cell division. EMBO J. 2007, 26:4694-4708.
    • (2007) EMBO J. , vol.26 , pp. 4694-4708
    • Li, Z.1
  • 12
    • 33644920433 scopus 로고    scopus 로고
    • Septum enlightenment: assembly of bacterial division proteins
    • Vicente M., et al. Septum enlightenment: assembly of bacterial division proteins. J. Bacteriol. 2006, 188:19-27.
    • (2006) J. Bacteriol. , vol.188 , pp. 19-27
    • Vicente, M.1
  • 13
    • 77951562635 scopus 로고    scopus 로고
    • Role of the Escherichia coli FtsN protein in the assembly and stability of the division ring
    • Rico A.I., et al. Role of the Escherichia coli FtsN protein in the assembly and stability of the division ring. Mol. Microbiol. 2010, 76:760-771.
    • (2010) Mol. Microbiol. , vol.76 , pp. 760-771
    • Rico, A.I.1
  • 14
    • 0036843026 scopus 로고    scopus 로고
    • Effects of multiple deletions of murein hydrolases on viability, septum cleavage, and sensitivity to large toxic molecules in Escherichia coli
    • Heidrich C., et al. Effects of multiple deletions of murein hydrolases on viability, septum cleavage, and sensitivity to large toxic molecules in Escherichia coli. J. Bacteriol. 2002, 184:6093-6099.
    • (2002) J. Bacteriol. , vol.184 , pp. 6093-6099
    • Heidrich, C.1
  • 15
    • 33749605980 scopus 로고    scopus 로고
    • FtsZ from divergent foreign bacteria can function for cell division in Escherichia coli
    • Osawa M., Erickson H.P. FtsZ from divergent foreign bacteria can function for cell division in Escherichia coli. J. Bacteriol. 2006, 188:7132-7140.
    • (2006) J. Bacteriol. , vol.188 , pp. 7132-7140
    • Osawa, M.1    Erickson, H.P.2
  • 16
    • 0031780061 scopus 로고    scopus 로고
    • Tubulin and FtsZ form a distinct family of GTPases
    • Nogales E., et al. Tubulin and FtsZ form a distinct family of GTPases. Nat. Struct. Biol. 1998, 5:451-458.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 451-458
    • Nogales, E.1
  • 17
    • 52249120794 scopus 로고    scopus 로고
    • An inhibitor of FtsZ with potent and selective anti-staphylococcal activity
    • Haydon D.J., et al. An inhibitor of FtsZ with potent and selective anti-staphylococcal activity. Science 2008, 321:1673-1675.
    • (2008) Science , vol.321 , pp. 1673-1675
    • Haydon, D.J.1
  • 18
    • 0242693139 scopus 로고    scopus 로고
    • Assembly dynamics of the bacterial cell division protein FTSZ: poised at the edge of stability
    • Romberg L., Levin P.A. Assembly dynamics of the bacterial cell division protein FTSZ: poised at the edge of stability. Annu. Rev. Microbiol. 2003, 57:124-154.
    • (2003) Annu. Rev. Microbiol. , vol.57 , pp. 124-154
    • Romberg, L.1    Levin, P.A.2
  • 19
    • 0037080162 scopus 로고    scopus 로고
    • GTP hydrolysis of cell division protein FtsZ: evidence that the active site is formed by the association of monomers
    • Scheffers D.J., et al. GTP hydrolysis of cell division protein FtsZ: evidence that the active site is formed by the association of monomers. Biochemistry 2002, 41:521-529.
    • (2002) Biochemistry , vol.41 , pp. 521-529
    • Scheffers, D.J.1
  • 20
    • 13444274140 scopus 로고    scopus 로고
    • Structural insights into FtsZ protofilament formation
    • Oliva M.A., et al. Structural insights into FtsZ protofilament formation. Nat. Struct. Mol. Biol. 2004, 11:1243-1250.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 1243-1250
    • Oliva, M.A.1
  • 21
    • 0031968795 scopus 로고    scopus 로고
    • FtsZ from Escherichia coli, Azotobacter vinelandii, and Thermotoga maritime - quantitation, GTP hydrolysis, and assembly
    • Lu C., et al. FtsZ from Escherichia coli, Azotobacter vinelandii, and Thermotoga maritime - quantitation, GTP hydrolysis, and assembly. Cell Motil. Cytoskeleton 1998, 40:71-86.
    • (1998) Cell Motil. Cytoskeleton , vol.40 , pp. 71-86
    • Lu, C.1
  • 22
    • 0039374565 scopus 로고    scopus 로고
    • Self-activation of guanosine triphosphatase activity by oligomerization of the bacterial cell division protein FtsZ
    • Sossong T.M., et al. Self-activation of guanosine triphosphatase activity by oligomerization of the bacterial cell division protein FtsZ. Biochemistry 1999, 38:14843-14850.
    • (1999) Biochemistry , vol.38 , pp. 14843-14850
    • Sossong, T.M.1
  • 23
    • 33747868464 scopus 로고    scopus 로고
    • Activation of the Escherichia coli cell division protein FtsZ by a low-affinity interaction with monovalent cations
    • Tadros M., et al. Activation of the Escherichia coli cell division protein FtsZ by a low-affinity interaction with monovalent cations. FEBS Lett. 2006, 580:4941-4946.
    • (2006) FEBS Lett. , vol.580 , pp. 4941-4946
    • Tadros, M.1
  • 24
    • 67349175712 scopus 로고    scopus 로고
    • +) and pH dependence of GTPase activity and polymerization of FtsZ, the prokaryotic ortholog of tubulin
    • +) and pH dependence of GTPase activity and polymerization of FtsZ, the prokaryotic ortholog of tubulin. J. Mol. Biol. 2009, 390:17-25.
    • (2009) J. Mol. Biol. , vol.390 , pp. 17-25
    • Mendieta, J.1
  • 25
    • 0034932711 scopus 로고    scopus 로고
    • Escherichia coli FtsZ polymers contain mostly GTP and have a high nucleotide turnover
    • Mingorance J., et al. Escherichia coli FtsZ polymers contain mostly GTP and have a high nucleotide turnover. Mol. Microbiol. 2001, 41:83-91.
    • (2001) Mol. Microbiol. , vol.41 , pp. 83-91
    • Mingorance, J.1
  • 26
    • 3042545408 scopus 로고    scopus 로고
    • Polymerization of nucleotide-free, GDP- and GTP-bound cell division protein FtsZ: GDP makes the difference
    • Huecas S., Andreu J.M. Polymerization of nucleotide-free, GDP- and GTP-bound cell division protein FtsZ: GDP makes the difference. FEBS Lett. 2004, 569:43-48.
    • (2004) FEBS Lett. , vol.569 , pp. 43-48
    • Huecas, S.1    Andreu, J.M.2
  • 27
    • 38049120195 scopus 로고    scopus 로고
    • The interactions of cell division protein FtsZ with guanine nucleotides
    • Huecas S., et al. The interactions of cell division protein FtsZ with guanine nucleotides. J. Biol. Chem. 2007, 282:37515-37528.
    • (2007) J. Biol. Chem. , vol.282 , pp. 37515-37528
    • Huecas, S.1
  • 28
    • 0040735625 scopus 로고    scopus 로고
    • Magnesium-induced linear self-association of the FtsZ bacterial cell division protein monomer. The primary steps for FtsZ assembly
    • Rivas G., et al. Magnesium-induced linear self-association of the FtsZ bacterial cell division protein monomer. The primary steps for FtsZ assembly. J. Biol. Chem. 2000, 275:11740-11749.
    • (2000) J. Biol. Chem. , vol.275 , pp. 11740-11749
    • Rivas, G.1
  • 29
    • 0028274791 scopus 로고
    • Guanine nucleotide-dependent assembly of FtsZ into filaments
    • Mukherjee A., Lutkenhaus J. Guanine nucleotide-dependent assembly of FtsZ into filaments. J. Bacteriol. 1994, 176:2754-2758.
    • (1994) J. Bacteriol. , vol.176 , pp. 2754-2758
    • Mukherjee, A.1    Lutkenhaus, J.2
  • 30
    • 0032916717 scopus 로고    scopus 로고
    • Analysis of FtsZ assembly by light scattering and determination of the role of divalent metal cations
    • Mukherjee A., Lutkenhaus J. Analysis of FtsZ assembly by light scattering and determination of the role of divalent metal cations. J. Bacteriol. 1999, 181:823-832.
    • (1999) J. Bacteriol. , vol.181 , pp. 823-832
    • Mukherjee, A.1    Lutkenhaus, J.2
  • 31
    • 0042925532 scopus 로고    scopus 로고
    • Dynamic FtsZ polymerization is sensitive to the GTP to GDP ratio and can be maintained at steady state using a GTP-regeneration system
    • Small E., Addinall S.G. Dynamic FtsZ polymerization is sensitive to the GTP to GDP ratio and can be maintained at steady state using a GTP-regeneration system. Microbiology 2003, 149:2235-2242.
    • (2003) Microbiology , vol.149 , pp. 2235-2242
    • Small, E.1    Addinall, S.G.2
  • 32
    • 69249126551 scopus 로고    scopus 로고
    • Bacterial cell division: assembly, maintenance and disassembly of the Z ring
    • Adams D.W., Errington J. Bacterial cell division: assembly, maintenance and disassembly of the Z ring. Nat. Rev. Microbiol. 2009, 7:642-653.
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 642-653
    • Adams, D.W.1    Errington, J.2
  • 33
    • 0035853825 scopus 로고    scopus 로고
    • Polymerisation of FtsZ, a bacterial homolog of tubulin: is assembly cooperative?
    • Romberg L., et al. Polymerisation of FtsZ, a bacterial homolog of tubulin: is assembly cooperative?. J. Biol. Chem. 2001, 276:11743-11753.
    • (2001) J. Biol. Chem. , vol.276 , pp. 11743-11753
    • Romberg, L.1
  • 34
    • 13844312609 scopus 로고    scopus 로고
    • Cooperative behavior of Escherichia coli cell-division protein FtsZ assembly involves the preferential cyclization of long single-stranded fibrils
    • González J.M., 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, 102:1895-1900.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 1895-1900
    • González, J.M.1
  • 35
    • 41449086675 scopus 로고    scopus 로고
    • Energetics and geometry of FtsZ polymers: nucleated self-assembly of single protofilaments
    • Huecas S., et al. Energetics and geometry of FtsZ polymers: nucleated self-assembly of single protofilaments. Biophys. J. 2008, 94:1796-1806.
    • (2008) Biophys. J. , vol.94 , pp. 1796-1806
    • Huecas, S.1
  • 36
    • 0030815131 scopus 로고    scopus 로고
    • 2+-mediated GTP-dependent dynamic assembly of bacterial cell division protein FtsZ into asters and polymer networks in vitro
    • 2+-mediated GTP-dependent dynamic assembly of bacterial cell division protein FtsZ into asters and polymer networks in vitro. EMBO J. 1997, 16:5455-5463.
    • (1997) EMBO J. , vol.16 , pp. 5455-5463
    • Yu, X.C.1    Margolin, W.2
  • 37
    • 0033783149 scopus 로고    scopus 로고
    • Helical tubes of FtsZ from Methanococcus jannaschii
    • Löwe J., Amos L. Helical tubes of FtsZ from Methanococcus jannaschii. Biol. Chem. 2000, 381:993-999.
    • (2000) Biol. Chem. , vol.381 , pp. 993-999
    • Löwe, J.1    Amos, L.2
  • 38
    • 0242584670 scopus 로고    scopus 로고
    • Essential cell division protein FtsZ assembles into one monomer-thick ribbons under conditions resembling the crowded intracellular environment
    • González J.M., et al. Essential cell division protein FtsZ assembles into one monomer-thick ribbons under conditions resembling the crowded intracellular environment. J. Biol. Chem. 2003, 278:37664-37671.
    • (2003) J. Biol. Chem. , vol.278 , pp. 37664-37671
    • González, J.M.1
  • 39
    • 67249144043 scopus 로고    scopus 로고
    • FtsZ condensates: an in vitro electron microscopy study
    • Popp D., et al. FtsZ condensates: an in vitro electron microscopy study. Biopolymers 2009, 91:340-350.
    • (2009) Biopolymers , vol.91 , pp. 340-350
    • Popp, D.1
  • 40
    • 33751319265 scopus 로고    scopus 로고
    • 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
    • Beuria K., et al. 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, 40:30-39.
    • (2006) Int. J. Biol. Macromol. , vol.40 , pp. 30-39
    • Beuria, K.1
  • 41
    • 20144383298 scopus 로고    scopus 로고
    • Visualization of single Escherichia coli FtsZ filament dynamics with atomic force microscopy
    • Mingorance J., et al. Visualization of single Escherichia coli FtsZ filament dynamics with atomic force microscopy. J. Biol. Chem. 2005, 280:20909-20914.
    • (2005) J. Biol. Chem. , vol.280 , pp. 20909-20914
    • Mingorance, J.1
  • 42
    • 77949908054 scopus 로고    scopus 로고
    • AAA+ chaperone ClpX regulates dynamics of prokaryotic cytoskeletal protein FtsZ
    • Sugimoto S., et al. AAA+ chaperone ClpX regulates dynamics of prokaryotic cytoskeletal protein FtsZ. J. Biol. Chem. 2010, 285:6648-6657.
    • (2010) J. Biol. Chem. , vol.285 , pp. 6648-6657
    • Sugimoto, S.1
  • 43
    • 77951235277 scopus 로고    scopus 로고
    • Suprastructures and dynamic properties of Mycobacterium tuberculosis FtsZ
    • Popp, et al. Suprastructures and dynamic properties of Mycobacterium tuberculosis FtsZ. J. Biol. Chem. 2010, 285:11281-11289.
    • (2010) J. Biol. Chem. , vol.285 , pp. 11281-11289
    • Popp1
  • 44
    • 0033986992 scopus 로고    scopus 로고
    • Straight and curved conformations of FtsZ are regulated by GTP hydrolysis
    • Lu C., et al. Straight and curved conformations of FtsZ are regulated by GTP hydrolysis. J. Bacteriol. 2000, 182:164-170.
    • (2000) J. Bacteriol. , vol.182 , pp. 164-170
    • Lu, C.1
  • 45
    • 69249088090 scopus 로고    scopus 로고
    • Structural plasticity in actin and tubulin polymer dynamics
    • Kueh H.Y., Mitchison T.J. Structural plasticity in actin and tubulin polymer dynamics. Science 2009, 325:960-963.
    • (2009) Science , vol.325 , pp. 960-963
    • Kueh, H.Y.1    Mitchison, T.J.2
  • 46
    • 0242580189 scopus 로고    scopus 로고
    • Energetics of the cooperative assembly of cell division protein FtsZ and the nucleotide hydrolysis switch
    • Huecas S., Andreu J.M. Energetics of the cooperative assembly of cell division protein FtsZ and the nucleotide hydrolysis switch. J. Biol. Chem. 2003, 278:46146-46154.
    • (2003) J. Biol. Chem. , vol.278 , pp. 46146-46154
    • Huecas, S.1    Andreu, J.M.2
  • 47
    • 0347988122 scopus 로고    scopus 로고
    • Rate-limiting guanosine 5'-triphosphate hydrolysis during nucleotide turnover by FtsZ, a prokaryotic tubulin homologue involved in bacterial cell division
    • Romberg L., Mitchison T.J. Rate-limiting guanosine 5'-triphosphate hydrolysis during nucleotide turnover by FtsZ, a prokaryotic tubulin homologue involved in bacterial cell division. Biochemistry 2004, 43:282-288.
    • (2004) Biochemistry , vol.43 , pp. 282-288
    • Romberg, L.1    Mitchison, T.J.2
  • 48
    • 67650508425 scopus 로고    scopus 로고
    • FtsZ filament dynamics at steady state: subunit exchange with and without nucleotide hydrolysis
    • Chen Y., Erickson H.P. FtsZ filament dynamics at steady state: subunit exchange with and without nucleotide hydrolysis. Biochemistry 2009, 48:6664-6673.
    • (2009) Biochemistry , vol.48 , pp. 6664-6673
    • Chen, Y.1    Erickson, H.P.2
  • 49
    • 20444457941 scopus 로고    scopus 로고
    • Rapid in vitro assembly dynamics and subunit turnover of FtsZ demonstrated by fluorescence resonance energy transfer
    • Chen Y., Erickson H.P. Rapid in vitro assembly dynamics and subunit turnover of FtsZ demonstrated by fluorescence resonance energy transfer. J. Biol. Chem. 2005, 280:22549-22554.
    • (2005) J. Biol. Chem. , vol.280 , pp. 22549-22554
    • Chen, Y.1    Erickson, H.P.2
  • 50
    • 0032518656 scopus 로고    scopus 로고
    • Dynamic assembly of FtsZ regulated by GTP hydrolysis
    • Mukherjee A., Lutkenhaus J. Dynamic assembly of FtsZ regulated by GTP hydrolysis. EMBO J. 1998, 17:462-469.
    • (1998) EMBO J. , vol.17 , pp. 462-469
    • Mukherjee, A.1    Lutkenhaus, J.2
  • 51
    • 33746358181 scopus 로고    scopus 로고
    • Dynamic filaments of the bacterial cytoskeleton
    • Michie K.A., Löwe J. Dynamic filaments of the bacterial cytoskeleton. Annu. Rev. Biochem. 2006, 75:467-492.
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 467-492
    • Michie, K.A.1    Löwe, J.2
  • 53
    • 51649125772 scopus 로고    scopus 로고
    • Allosteric models for cooperative polymerization of linear polymers
    • Miraldi E.R., et al. Allosteric models for cooperative polymerization of linear polymers. Biophys. J. 2008, 95:2470-2486.
    • (2008) Biophys. J. , vol.95 , pp. 2470-2486
    • Miraldi, E.R.1
  • 54
    • 35148840132 scopus 로고    scopus 로고
    • Structural insights into the conformational variability of FtsZ
    • Oliva M.A., et al. Structural insights into the conformational variability of FtsZ. J. Mol. Biol. 2007, 373:1229-1242.
    • (2007) J. Mol. Biol. , vol.373 , pp. 1229-1242
    • Oliva, M.A.1
  • 55
    • 65249138400 scopus 로고    scopus 로고
    • Mica surface promotes the assembly of cytoskeletal proteins
    • Hamon, et al. Mica surface promotes the assembly of cytoskeletal proteins. Langmuir 2009, 25:3331-3335.
    • (2009) Langmuir , vol.25 , pp. 3331-3335
    • Hamon1
  • 56
    • 48249089312 scopus 로고    scopus 로고
    • Kinetic modeling of the assembly, dynamic steady state, and contraction of the FtsZ ring in prokaryotic cytokinesis
    • Surovtsev I.V., et al. Kinetic modeling of the assembly, dynamic steady state, and contraction of the FtsZ ring in prokaryotic cytokinesis. PloS Comput. Biol. 2008, 4:e1000102.
    • (2008) PloS Comput. Biol. , vol.4
    • Surovtsev, I.V.1
  • 57
    • 58549106648 scopus 로고    scopus 로고
    • Force generation by a dynamic Z-ring in Escherichia coli cell division
    • Allard J.F., Cytrynbaum E.N. Force generation by a dynamic Z-ring in Escherichia coli cell division. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:145-150.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 145-150
    • Allard, J.F.1    Cytrynbaum, E.N.2
  • 58
    • 56049110001 scopus 로고    scopus 로고
    • Polymerization and bundling kinetics of FtsZ filaments
    • Lan G., et al. Polymerization and bundling kinetics of FtsZ filaments. Biophys. J. 2008, 95:4045-4056.
    • (2008) Biophys. J. , vol.95 , pp. 4045-4056
    • Lan, G.1
  • 59
    • 58549096090 scopus 로고    scopus 로고
    • Condensation of FtsZ filaments can drive bacterial cell division
    • Lan G., et al. Condensation of FtsZ filaments can drive bacterial cell division. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:121-126.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 121-126
    • Lan, G.1
  • 60
    • 64449085394 scopus 로고    scopus 로고
    • Analyses of mechanisms for force generation during cell septation in Escherichia coli
    • Drew, et al. Analyses of mechanisms for force generation during cell septation in Escherichia coli. Bull. Math. Biol. 2009, 71:980-1005.
    • (2009) Bull. Math. Biol. , vol.71 , pp. 980-1005
    • Drew1
  • 61
    • 70349296873 scopus 로고    scopus 로고
    • Self-organization of curved living polymers: FtsZ protein filaments
    • Páez A., et al. Self-organization of curved living polymers: FtsZ protein filaments. Soft Matter 2009, 5:2625-2637.
    • (2009) Soft Matter , vol.5 , pp. 2625-2637
    • Páez, A.1
  • 62
    • 77950168727 scopus 로고    scopus 로고
    • Simple modeling of FtsZ polymers on flat and curved surfaces: correlation with experimental in vitro observations
    • Páez A., et al. Simple modeling of FtsZ polymers on flat and curved surfaces: correlation with experimental in vitro observations. PMC Biophys. 2009, 2:8.
    • (2009) PMC Biophys. , vol.2 , pp. 8
    • Páez, A.1
  • 63
    • 70449586634 scopus 로고    scopus 로고
    • Lateral FtsZ association and the assembly of the cytokinetic Z ring in bacteria
    • Monahan L.G., et al. Lateral FtsZ association and the assembly of the cytokinetic Z ring in bacteria. Mol. Microbiol. 2009, 74:1004-1017.
    • (2009) Mol. Microbiol. , vol.74 , pp. 1004-1017
    • Monahan, L.G.1
  • 64
    • 55049117823 scopus 로고    scopus 로고
    • Origin of contractile force during cell division of bacteria
    • Ghosh B., Sain A. Origin of contractile force during cell division of bacteria. Phys. Rev. Lett. 2008, 101:178101.
    • (2008) Phys. Rev. Lett. , vol.101 , pp. 178101
    • Ghosh, B.1    Sain, A.2
  • 65
    • 40749098614 scopus 로고    scopus 로고
    • Langevin computer simulations of bacterial protein filaments and the force-generating mechanism during cell division
    • Hörger I., et al. Langevin computer simulations of bacterial protein filaments and the force-generating mechanism during cell division. Phys. Rev. E Stat. Nonlin. Soft Matter Phys. 2008, 77:011902.
    • (2008) Phys. Rev. E Stat. Nonlin. Soft Matter Phys. , vol.77 , pp. 011902
    • Hörger, I.1
  • 66
    • 75649148825 scopus 로고    scopus 로고
    • Membrane-mediated interactions drive the condensation and coalescence of FtsZ rings
    • Shlomovitz R., Gov N.S. Membrane-mediated interactions drive the condensation and coalescence of FtsZ rings. Phys. Biol. 2009, 6:46017.
    • (2009) Phys. Biol. , vol.6 , pp. 46017
    • Shlomovitz, R.1    Gov, N.S.2
  • 67
    • 55349102644 scopus 로고    scopus 로고
    • In vitro reconstitution of the initial stages of the bacterial cell division machinery
    • Navajas P.L., et al. In vitro reconstitution of the initial stages of the bacterial cell division machinery. J. Biol. Phys. 2008, 34:237-247.
    • (2008) J. Biol. Phys. , vol.34 , pp. 237-247
    • Navajas, P.L.1
  • 68
    • 44049091371 scopus 로고    scopus 로고
    • Reconstitution of contractile FtsZ rings in liposomes
    • Osawa M., et al. Reconstitution of contractile FtsZ rings in liposomes. Science 2008, 320:792-794.
    • (2008) Science , vol.320 , pp. 792-794
    • Osawa, M.1
  • 69
    • 70450224670 scopus 로고    scopus 로고
    • Curved FtsZ protofilaments generate bending forces on liposome membranes
    • Osawa M., et al. Curved FtsZ protofilaments generate bending forces on liposome membranes. EMBO J. 2009, 28:3476-3484.
    • (2009) EMBO J. , vol.28 , pp. 3476-3484
    • Osawa, M.1
  • 70
    • 67249097621 scopus 로고    scopus 로고
    • Modeling the physics of FtsZ assembly and force generation
    • Erickson H.P. Modeling the physics of FtsZ assembly and force generation. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:9238-9243.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 9238-9243
    • Erickson, H.P.1
  • 71
    • 0015910158 scopus 로고
    • Process of cellular division in Escherichia coli: physiology study on thermosensitive mutants defective in cell division
    • Ricard M., Hirota Y. Process of cellular division in Escherichia coli: physiology study on thermosensitive mutants defective in cell division. J. Bacteriol. 1973, 116:314-320.
    • (1973) J. Bacteriol. , vol.116 , pp. 314-320
    • Ricard, M.1    Hirota, Y.2
  • 72
    • 0023104990 scopus 로고
    • Characterization of the ftsB gene as an allele of the nrdB gene in Escherichia coli
    • Kren B., Fuchs J.A. Characterization of the ftsB gene as an allele of the nrdB gene in Escherichia coli. J. Bacteriol. 1987, 169:14-18.
    • (1987) J. Bacteriol. , vol.169 , pp. 14-18
    • Kren, B.1    Fuchs, J.A.2
  • 73
    • 0023147125 scopus 로고
    • Genetic and morphological characterization of ftsB and nrdB mutants of Escherichia coli
    • Taschner P.E., et al. Genetic and morphological characterization of ftsB and nrdB mutants of Escherichia coli. J. Bacteriol. 1987, 169:19-25.
    • (1987) J. Bacteriol. , vol.169 , pp. 19-25
    • Taschner, P.E.1
  • 74
    • 2942570076 scopus 로고    scopus 로고
    • A complex of the Escherichia coli cell division proteins FtsL, FtsB and FtsQ forms independently of its localization to the septal region
    • Buddelmeijer N., Beckwith J. A complex of the Escherichia coli cell division proteins FtsL, FtsB and FtsQ forms independently of its localization to the septal region. Mol. Microbiol. 2004, 52:1315-1327.
    • (2004) Mol. Microbiol. , vol.52 , pp. 1315-1327
    • Buddelmeijer, N.1    Beckwith, J.2
  • 75
    • 0018972825 scopus 로고
    • Organization of genes in the ftsA-envA region of the Escherichia coli genetic map and identification of a new fts locus: ftsZ
    • Lutkenhaus J.F., et al. Organization of genes in the ftsA-envA region of the Escherichia coli genetic map and identification of a new fts locus: ftsZ. J. Bacteriol. 1980, 142:615-620.
    • (1980) J. Bacteriol. , vol.142 , pp. 615-620
    • Lutkenhaus, J.F.1
  • 76
    • 0012435704 scopus 로고
    • The selection of mutants of Escherichia coli with impaired cell division at elevated temperature
    • van de Putte P., et al. The selection of mutants of Escherichia coli with impaired cell division at elevated temperature. Mutat. Res. 1964, 106:121-128.
    • (1964) Mutat. Res. , vol.106 , pp. 121-128
    • van de Putte, P.1
  • 77
    • 77956818245 scopus 로고
    • Molecular biology of bacterial septation
    • Elsevier Science, J.M. Ghuysen, R. Habenbeck (Eds.)
    • Ayala J.A., et al. Molecular biology of bacterial septation. Bacterial Cell Wall 1994, Elsevier Science, pp.73-101. J.M. Ghuysen, R. Habenbeck (Eds.).
    • (1994) Bacterial Cell Wall , pp. 73-101
    • Ayala, J.A.1
  • 78
    • 1242275397 scopus 로고    scopus 로고
    • Initiation of intracellular offspring in Epulopiscium
    • Angert E.R., Clements K.D. Initiation of intracellular offspring in Epulopiscium. Mol. Microbiol. 2004, 51:827-835.
    • (2004) Mol. Microbiol. , vol.51 , pp. 827-835
    • Angert, E.R.1    Clements, K.D.2
  • 79
    • 0027176669 scopus 로고
    • Transcription of ftsZ oscillates during the cell cycle of Escherichia coli
    • Garrido T., et al. Transcription of ftsZ oscillates during the cell cycle of Escherichia coli. EMBO J. 1993, 12:3957-3965.
    • (1993) EMBO J. , vol.12 , pp. 3957-3965
    • Garrido, T.1


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