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Volumn 288, Issue 29, 2013, Pages 20830-20836

In the beginning, escherichia coli assembled the proto-ring: An initial phase of division

Author keywords

[No Author keywords available]

Indexed keywords

A-RINGS; CELL DIVISIONS; PEPTIDOGLYCANS; PROTEIN INTERACTION; TEMPORAL SEQUENCES;

EID: 84880563030     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.R113.479519     Document Type: Review
Times cited : (63)

References (98)
  • 2
    • 77950452960 scopus 로고    scopus 로고
    • Evolution of reduced prokaryotic genomes and the minimal cell concept: Variations on a theme
    • Delaye, L., andMoya, A. (2010) Evolution of reduced prokaryotic genomes and the minimal cell concept: variations on a theme. BioEssays 32, 281-287
    • (2010) BioEssays , vol.32 , pp. 281-287
    • Delaye, L.1    Moya, A.2
  • 4
    • 33745209434 scopus 로고    scopus 로고
    • The order of the ring: Assembly of Escherichia coli cell division components
    • Vicente, M., and Rico, A. I. (2006) The order of the ring: assembly of Escherichia coli cell division components. Mol. Microbiol. 61, 5-8
    • (2006) Mol. Microbiol. , vol.61 , pp. 5-8
    • Vicente, M.1    Rico, A.I.2
  • 5
    • 0031444158 scopus 로고    scopus 로고
    • Direct binding of FtsZ to ZipA, an essential component of the septal ring structure that mediates cell division in e
    • Hale, C. A., and de Boer, P. A. (1997) Direct binding of FtsZ to ZipA, an essential component of the septal ring structure that mediates cell division in E. coli. Cell 88, 175-185
    • (1997) Coli. Cell , vol.88 , pp. 175-185
    • Hale, C.A.1    De Boer, P.A.2
  • 6
    • 15744385269 scopus 로고    scopus 로고
    • Tethering the Z ring to the membrane through a conserved membrane targeting sequence in FtsA
    • Pichoff, S., and Lutkenhaus, J. (2005) Tethering the Z ring to the membrane through a conserved membrane targeting sequence in FtsA. Mol. Microbiol. 55, 1722-1734
    • (2005) Mol. Microbiol. , vol.55 , pp. 1722-1734
    • Pichoff, S.1    Lutkenhaus, J.2
  • 7
    • 79953208071 scopus 로고    scopus 로고
    • Reconstitution and organization of Escherichia coli proto-ring elements (FtsZ and FtsA) inside giant unilamellar vesicles obtained from bacterial inner membranes
    • Jimenez, M., Martos, A., Vicente, M., and Rivas, G. (2011) Reconstitution and organization of Escherichia coli proto-ring elements (FtsZ and FtsA) inside giant unilamellar vesicles obtained from bacterial inner membranes. J. Biol. Chem. 286, 11236 -11241
    • (2011) J. Biol. Chem. , vol.286 , pp. 11236-11241
    • Jimenez, M.1    Martos, A.2    Vicente, M.3    Rivas, G.4
  • 8
    • 0038191051 scopus 로고    scopus 로고
    • Concentration and assembly of the division ring proteins FtsZ, FtsA, and ZipA during the Esch-erichia coli cell cycle
    • Rueda, S., Vicente, M., and Mingorance, J. (2003) Concentration and assembly of the division ring proteins FtsZ, FtsA, and ZipA during the Esch-erichia coli cell cycle. J. Bacteriol. 185, 3344-3351
    • (2003) J. Bacteriol. , vol.185 , pp. 3344-3351
    • Rueda, S.1    Vicente, M.2    Mingorance, J.3
  • 9
    • 0037084109 scopus 로고    scopus 로고
    • Unique and overlapping roles for ZipA and FtsA in septal ring assembly in Escherichia coli
    • Pichoff, S., and Lutkenhaus, J. (2002) Unique and overlapping roles for ZipA and FtsA in septal ring assembly in Escherichia coli. EMBO J. 21, 685-693
    • (2002) EMBO J , vol.21 , pp. 685-693
    • Pichoff, S.1    Lutkenhaus, J.2
  • 11
    • 77951562635 scopus 로고    scopus 로고
    • Role of Escherichia coli FtsN protein in the assembly and stability of the cell division ring
    • Rico, A. I., Garcfa-Ovalle, M., Palacios, P., Casanova, M., and Vicente, M. (2010) Role of Escherichia coli FtsN protein in the assembly and stability of the cell division ring. Mol. Microbiol. 76, 760 -771
    • (2010) Mol. Microbiol. , vol.76 , pp. 760-771
    • Rico, A.I.1    Garcfa-Ovalle, M.2    Palacios, P.3    Casanova, M.4    Vicente, M.5
  • 12
    • 19444386428 scopus 로고    scopus 로고
    • SlmA, a nucleoid-associated, FtsZ binding protein required for blocking septal ring assembly over chromosomes in E. coli
    • Bernhardt, T. G., and de Boer, P. A. (2005) SlmA, a nucleoid-associated, FtsZ binding protein required for blocking septal ring assembly over chromosomes in E. coli. Mol. Cell 18, 555-564
    • (2005) Mol. Cell , vol.18 , pp. 555-564
    • Bernhardt, T.G.1    De Boer, P.A.2
  • 14
    • 79952741894 scopus 로고    scopus 로고
    • Nucle-oid occlusion factor SlmA is a DNA-activated FtsZ polymerization antagonist
    • Cho, H., McManus, H. R., Dove, S. L., and Bernhardt, T. G. (2011) Nucle-oid occlusion factor SlmA is a DNA-activated FtsZ polymerization antagonist. Proc. Natl. Acad. Sci. U.S.A. 108, 3773-3778
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 3773-3778
    • Cho, H.1    McManus, H.R.2    Dove, S.L.3    Bernhardt, T.G.4
  • 15
    • 33845932662 scopus 로고    scopus 로고
    • The C-terminal domain of MinC inhibits assembly of the Z ring in Escherichia coli
    • Shiomi, D., and Margolin, W. (2007) The C-terminal domain of MinC inhibits assembly of the Z ring in Escherichia coli. J. Bacterial. 189, 236-243
    • (2007) J. Bacterial. , vol.189 , pp. 236-243
    • Shiomi, D.1    Margolin, W.2
  • 16
    • 39249085850 scopus 로고    scopus 로고
    • MinC spatially controls bacterial cytokinesis by antagonizing the scaffolding function of FtsZ
    • Dajkovic, A., Lan, G., Sun, S. X., Wirtz, D., and Lutkenhaus, J. (2008) MinC spatially controls bacterial cytokinesis by antagonizing the scaffolding function of FtsZ. Curr. Biol. 18, 235-244
    • (2008) Curr. Biol. , vol.18 , pp. 235-244
    • Dajkovic, A.1    Lan, G.2    Sun, S.X.3    Wirtz, D.4    Lutkenhaus, J.5
  • 17
    • 77349085366 scopus 로고    scopus 로고
    • Examination of the interaction between FtsZ and MinCN in E. coli suggests how MinC disrupts Z rings
    • Shen, B., and Lutkenhaus, J. (2010) Examination of the interaction between FtsZ and MinCN in E. coli suggests how MinC disrupts Z rings. Mol. Microbiol. 75, 1285-1298
    • (2010) Mol. Microbiol. , vol.75 , pp. 1285-1298
    • Shen, B.1    Lutkenhaus, J.2
  • 18
    • 71549130716 scopus 로고    scopus 로고
    • Division site selection in rod-shaped bacteria
    • Bramkamp, M., and van Baarle, S. (2009) Division site selection in rod-shaped bacteria. Curr. Opin. Microbiol. 12, 683-688
    • (2009) Curr. Opin. Microbiol. , vol.12 , pp. 683-688
    • Bramkamp, M.1    Van Baarle, S.2
  • 19
    • 78650865197 scopus 로고    scopus 로고
    • Differences in MinC/MinD sensitivity between polar and internal Z rings in Escherichia coli
    • Shen, B., and Lutkenhaus, J. (2011) Differences in MinC/MinD sensitivity between polar and internal Z rings in Escherichia coli. J. Bacteriol. 193, 367-376
    • (2011) J. Bacteriol. , vol.193 , pp. 367-376
    • Shen, B.1    Lutkenhaus, J.2
  • 20
    • 77955932270 scopus 로고    scopus 로고
    • Changes in the Min oscillation pattern before and after cell birth
    • Juarez, J. R., and Margolin, W. (2010) Changes in the Min oscillation pattern before and after cell birth. J. Bacteriol. 192, 4134-4142
    • (2010) J. Bacteriol. , vol.192 , pp. 4134-4142
    • Juarez, J.R.1    Margolin, W.2
  • 22
    • 84862815508 scopus 로고    scopus 로고
    • Isolation and identification of new inner membrane-associated proteins that localize to cell poles in Escherichia coli
    • Li, G., and Young, K. D. (2012) Isolation and identification of new inner membrane-associated proteins that localize to cell poles in Escherichia coli. Mol. Microbiol. 84, 276-295
    • (2012) Mol. Microbiol. , vol.84 , pp. 276-295
    • Li, G.1    Young, K.D.2
  • 23
    • 0028872562 scopus 로고
    • FtsZ, a prokaryotic homologue of tubulin?
    • Erickson, H. P. (1995) FtsZ, a prokaryotic homologue of tubulin? Cell 80, 367-370
    • (1995) Cell , vol.80 , pp. 367-370
    • Erickson, H.P.1
  • 24
    • 0030829601 scopus 로고    scopus 로고
    • FtsZ, a tubulin homologue in prokaryote cell division
    • Erickson, H. P. (1997) FtsZ, a tubulin homologue in prokaryote cell division. Trends Cell Biol. 7, 362-367
    • (1997) Trends Cell Biol. , vol.7 , pp. 362-367
    • Erickson, H.P.1
  • 25
    • 2642593025 scopus 로고    scopus 로고
    • Crystal structure of the bacterial celldivision protein FtsZ
    • Löwe, J., and Amos, L. A. (1998) Crystal structure of the bacterial celldivision protein FtsZ. Nature 391, 203-206
    • (1998) Nature , vol.391 , pp. 203-206
    • Löwe, J.1    Amos, L.A.2
  • 26
    • 78650078263 scopus 로고    scopus 로고
    • FtsZ in bacterial cytokinesis: Cytoskeleton and force generator all in one
    • Erickson, H. P., Anderson, D. E., and Osawa, M. (2010) FtsZ in bacterial cytokinesis: cytoskeleton and force generator all in one. Microbiol. Mol. Biol. Rev. 74, 504-528
    • (2010) Microbiol. Mol. Biol. Rev. , vol.74 , pp. 504-528
    • Erickson, H.P.1    Anderson, D.E.2    Osawa, M.3
  • 28
    • 20144383298 scopus 로고    scopus 로고
    • Visualization of single Escherichia coli FtsZ filament dynamics with atomic force microscopy
    • Mingorance, J., Tadros, M., Vicente, M., González, J. M., Rivas, G., and Vélez, M. (2005) Visualization of single Escherichia coli FtsZ filament dynamics with atomic force microscopy. J. Biol. Chem. 280, 20909 -20914
    • (2005) J. Biol. Chem. , vol.280 , pp. 20909-20914
    • Mingorance, J.1    Tadros, M.2    Vicente, M.3    González, J.M.4    Rivas, G.5    Vélez, M.6
  • 30
    • 0032916717 scopus 로고    scopus 로고
    • Analysis of FtsZ assembly by light scattering and determination of the role of divalent metal cations
    • Mukherjee, A., and Lutkenhaus, J. (1999) Analysis of FtsZ assembly by light scattering and determination of the role of divalent metal cations. J. Bacteriol. 181, 823-832
    • (1999) J. Bacteriol. , vol.181 , pp. 823-832
    • Mukherjee, A.1    Lutkenhaus, J.2
  • 32
    • 0036791675 scopus 로고    scopus 로고
    • A widely conserved bacterial cell division protein that promotes assembly of the tubulin-like protein FtsZ
    • Gueiros-Filho, F. J., and Losick, R. (2002) A widely conserved bacterial cell division protein that promotes assembly of the tubulin-like protein FtsZ. Genes Dev. 16, 2544-2556
    • (2002) Genes Dev. , vol.16 , pp. 2544-2556
    • Gueiros-Filho, F.J.1    Losick, R.2
  • 33
    • 67249144043 scopus 로고    scopus 로고
    • FtsZ condensates: An in vitro electron microscopy study
    • Popp, D., Iwasa, M., Narita, A., Erickson, H. P., and Maéda, Y. (2009) FtsZ condensates: an in vitro electron microscopy study. Biopolymers. 91, 340-350
    • (2009) Biopolymers. , vol.91 , pp. 340-350
    • Popp, D.1    Iwasa, M.2    Narita, A.3    Erickson, H.P.4    Maéda, Y.5
  • 35
    • 84863500867 scopus 로고    scopus 로고
    • Negative-stain electron microscopy of inside-out FtsZ rings reconstituted on artificial membrane tubules show ribbons of protofilaments
    • Milam, S. L., Osawa, M., and Erickson, H. P. (2012) Negative-stain electron microscopy of inside-out FtsZ rings reconstituted on artificial membrane tubules show ribbons of protofilaments. Biophys J. 103, 59-68
    • (2012) Biophys J. , vol.103 , pp. 59-68
    • Milam, S.L.1    Osawa, M.2    Erickson, H.P.3
  • 36
    • 0037022642 scopus 로고    scopus 로고
    • Rapid assembly dynamics of the Escherichia coli FtsZ-ring demonstrated by fluorescence recovery after photobleaching
    • Stricker, J., Maddox, P., Salmon, E. D., and Erickson, H. P. (2002) Rapid assembly dynamics of the Escherichia coli FtsZ-ring demonstrated by fluorescence recovery after photobleaching. Proc. Natl. Acad. Sci. U.S.A. 99, 3171-3175
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 3171-3175
    • Stricker, J.1    Maddox, P.2    Salmon, E.D.3    Erickson, H.P.4
  • 37
    • 84859055009 scopus 로고    scopus 로고
    • Three-dimensional super-resolution imaging ofthe midplane protein FtsZ in live Caulobacter crescentus cells using astigmatism
    • Biteen, J. S., Goley, E. D., Shapiro, L., and Moerner, W. E. (2012) Three-dimensional super-resolution imaging ofthe midplane protein FtsZ in live Caulobacter crescentus cells using astigmatism. ChemPhysChem 13, 1007-1012
    • (2012) ChemPhysChem , vol.13 , pp. 1007-1012
    • Biteen, J.S.1    Goley, E.D.2    Shapiro, L.3    Moerner, W.E.4
  • 38
    • 36248938686 scopus 로고    scopus 로고
    • The structure of FtsZ filaments in vivo suggests a force-generating role in cell division
    • Li, Z., Trimble, M. J., Brun, Y. V., and Jensen, G. J. (2007) The structure of FtsZ filaments in vivo suggests a force-generating role in cell division. EMBOJ. 26, 4694-4708
    • (2007) EMBOJ , vol.26 , pp. 4694-4708
    • Li, Z.1    Trimble, M.J.2    Brun, Y.V.3    Jensen, G.J.4
  • 39
    • 77958525927 scopus 로고    scopus 로고
    • In vivo structure of the E. coli FtsZ-ring revealed by photoactivated localization microscopy (PALM)
    • Fu, G., Huang, T., Buss, J., Coltharp, C., Hensel, Z., and Xiao, J. (2010) In vivo structure of the E. coli FtsZ-ring revealed by photoactivated localization microscopy (PALM). PLoS ONE 5, e12682
    • (2010) PLoS ONE , vol.5
    • Fu, G.1    Huang, T.2    Buss, J.3    Coltharp, C.4    Hensel, Z.5    Xiao, J.6
  • 40
    • 84864018985 scopus 로고    scopus 로고
    • Identification of ZapD as a cell division factor that promotes the assembly of FtsZ in Escherichia coli
    • Durand-Heredia, J., Rivkin, E., Fan, G., Morales, J., and Janakiraman, A. (2012) Identification of ZapD as a cell division factor that promotes the assembly of FtsZ in Escherichia coli. J. Bacteriol. 194, 3189-3198
    • (2012) J. Bacteriol. , vol.194 , pp. 3189-3198
    • Durand-Heredia, J.1    Rivkin, E.2    Fan, G.3    Morales, J.4    Janakiraman, A.5
  • 41
    • 79952401787 scopus 로고    scopus 로고
    • Identification of Escherichia coli ZapC (YcbW) as a component of the division apparatus that binds and bundles FtsZ polymers
    • Hale, C. A., Shiomi, D., Liu, B., Bernhardt, T. G., Margolin, W., Niki, H., and de Boer, P.A. (2011) Identification of Escherichia coli ZapC (YcbW) as a component of the division apparatus that binds and bundles FtsZ polymers. J. Bacteriol. 193,1393-1404
    • (2011) J. Bacteriol. , vol.193 , pp. 1393-1404
    • Hale, C.A.1    Shiomi, D.2    Liu, B.3    Bernhardt, T.G.4    Margolin, W.5    Niki, H.6    De Boer, P.A.7
  • 42
    • 79952403634 scopus 로고    scopus 로고
    • Identification and characterization of ZapC, a stabilizer of the FtsZ ring in Escherichia coli
    • Durand-Heredia, J. M., Yu, H. H., De Carlo, S., Lesser, C. F., and Janakira-man, A. (2011) Identification and characterization of ZapC, a stabilizer of the FtsZ ring in Escherichia coli. J. Bacteriol. 193,1405-1413
    • (2011) J. Bacteriol. , vol.193 , pp. 1405-1413
    • Durand-Heredia, J.M.1    Yu, H.H.2    De Carlo, S.3    Lesser, C.F.4    Janakira-Man, A.5
  • 43
    • 41749083933 scopus 로고    scopus 로고
    • Novel coiled-coil cell division factor ZapB stimulates Z ring assembly and cell division
    • Ebersbach, G., Galli, E., Moller-Jensen, J., Löwe, J., and Gerdes, K. (2008) Novel coiled-coil cell division factor ZapB stimulates Z ring assembly and cell division. Mol. Microbiol. 68, 720-735
    • (2008) Mol. Microbiol. , vol.68 , pp. 720-735
    • Ebersbach, G.1    Galli, E.2    Moller-Jensen, J.3    Löwe, J.4    Gerdes, K.5
  • 44
    • 77953494296 scopus 로고    scopus 로고
    • Spatial resolution of two bacterial cell division proteins: ZapA recruits ZapB to the inner face of the Z-ring
    • Galli, E., and Gerdes, K. (2010) Spatial resolution of two bacterial cell division proteins: ZapA recruits ZapB to the inner face of the Z-ring. Mol. Microbiol. 76, 1514-1526
    • (2010) Mol. Microbiol. , vol.76 , pp. 1514-1526
    • Galli, E.1    Gerdes, K.2
  • 45
    • 4344620117 scopus 로고    scopus 로고
    • The crystal structure of ZapA and its modulation of FtsZ polymerisation
    • Low, H. H., Moncrieffe, M. C., and Löwe, J. (2004) The crystal structure of ZapA and its modulation of FtsZ polymerisation. J. Mol. Biol. 341, 839-852
    • (2004) J. Mol. Biol. , vol.341 , pp. 839-852
    • Low, H.H.1    Moncrieffe, M.C.2    Löwe, J.3
  • 47
    • 70449586634 scopus 로고    scopus 로고
    • Lateral FtsZ association and the assembly of the cytokinetic Z ring in bacteria
    • Monahan, L. G., Robinson, A., and Harry, E. J. (2009) Lateral FtsZ association and the assembly of the cytokinetic Z ring in bacteria. Mol. Micro-biol. 74, 1004-1017
    • (2009) Mol. Micro-biol. , vol.74 , pp. 1004-1017
    • Monahan, L.G.1    Robinson, A.2    Harry, E.J.3
  • 50
    • 0035853803 scopus 로고    scopus 로고
    • Genetic analysis of the E. coli FtsZ-ZipA interaction in the yeast two-hybrid system. Characterization of FtsZ residues essential for the interactions with ZipA and with FtsA
    • Haney, S. A., Glasfeld, E., Hale, C., Keeney, D., He, Z., and de Boer, P. (2001) Genetic analysis of the E. coli FtsZ-ZipA interaction in the yeast two-hybrid system. Characterization of FtsZ residues essential for the interactions with ZipA and with FtsA. J.Biol. Chem. 276, 11980-11987
    • (2001) J.Biol. Chem. , vol.276 , pp. 11980-11987
    • Haney, S.A.1    Glasfeld, E.2    Hale, C.3    Keeney, D.4    He, Z.5    De Boer, P.6
  • 51
    • 67649811066 scopus 로고    scopus 로고
    • ClpXP protease degrades the cytoskeletal protein, FtsZ, and modulates FtsZ polymer dynamics
    • Camberg, J. L., Hoskins, J. R., and Wickner, S. (2009) ClpXP protease degrades the cytoskeletal protein, FtsZ, and modulates FtsZ polymer dynamics. Proc. Natl. Acad. Sci. U.S.A. 106,10614-10619
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 10614-10619
    • Camberg, J.L.1    Hoskins, J.R.2    Wickner, S.3
  • 52
    • 46749098901 scopus 로고    scopus 로고
    • The effect of MinC on FtsZ polymerization is pH dependent and can be counteracted by ZapA
    • Scheffers, D. J. (2008) The effect of MinC on FtsZ polymerization is pH dependent and can be counteracted by ZapA. FEBS Lett. 582, 2601-2608
    • (2008) FEBS Lett. , vol.582 , pp. 2601-2608
    • Scheffers, D.J.1
  • 53
    • 84873286335 scopus 로고    scopus 로고
    • A specific role for the ZipA protein in cell division: Stabilization of the FtsZ protein
    • Pazos, M., Natale, P., and Vicente, M. (2013) A specific role for the ZipA protein in cell division: stabilization of the FtsZ protein. J.Biol. Chem. 288, 3219-3226
    • (2013) J.Biol. Chem. , vol.288 , pp. 3219-3226
    • Pazos, M.1    Natale, P.2    Vicente, M.3
  • 54
    • 84859484529 scopus 로고    scopus 로고
    • Extreme C terminus of bacterial cyto-skeletal protein FtsZ plays fundamental role in assembly independent of modulatoryproteins
    • Buske, P. J., and Levin, P. A. (2012) Extreme C terminus of bacterial cyto-skeletal protein FtsZ plays fundamental role in assembly independent of modulatoryproteins.J.Biol. Chem. 287,10945-10957
    • (2012) J. Biol. Chem. , vol.287 , pp. 10945-10957
    • Buske, P.J.1    Levin, P.A.2
  • 55
    • 0034675921 scopus 로고    scopus 로고
    • Crystal structure of the cell division protein FtsA from Thermotoga maritima
    • van den Ent, F., and Löwe, J. (2000) Crystal structure of the cell division protein FtsA from Thermotoga maritima. EMBO J. 19, 5300-5307
    • (2000) EMBO J , vol.19 , pp. 5300-5307
    • Van Den Ent, F.1    Löwe, J.2
  • 57
    • 4444300864 scopus 로고    scopus 로고
    • Role of two essential domains of Escherichia coli FtsA in localization and progression of the division ring
    • Rico, A. I., Garcia-Ovalle, M., Mingorance, J., and Vicente, M. (2004) Role of two essential domains of Escherichia coli FtsA in localization and progression of the division ring. Mol. Microbiol. 53, 1359-1371
    • (2004) Mol. Microbiol. , vol.53 , pp. 1359-1371
    • Rico, A.I.1    Garcia-Ovalle, M.2    Mingorance, J.3    Vicente, M.4
  • 59
    • 84857738215 scopus 로고    scopus 로고
    • Key role of two terminal domains in the bidirectional polymerization of FtsA protein
    • Krupka, M., Rivas, G., Rico, A. I., and Vicente, M. (2012) Key role of two terminal domains in the bidirectional polymerization of FtsA protein. J.Biol. Chem. 287, 7756 -7765
    • (2012) J.Biol. Chem. , vol.287 , pp. 7756-7765
    • Krupka, M.1    Rivas, G.2    Rico, A.I.3    Vicente, M.4
  • 60
    • 84861151969 scopus 로고    scopus 로고
    • FtsA forms actin-like protofilaments
    • Szwedziak, P., Wang, Q., Freund, S. M., and Löwe, J. (2012) FtsA forms actin-like protofilaments. EMBO J. 31, 2249 -2260
    • (2012) EMBO J , vol.31 , pp. 2249-2260
    • Szwedziak, P.1    Wang, Q.2    Freund, S.M.3    Löwe, J.4
  • 61
    • 84862988236 scopus 로고    scopus 로고
    • Isolation, characterization and lipid-binding properties of the recalcitrant FtsA division protein from Escherichia coli
    • Martos, A., Monterroso, B., Zorrilla, S., Reija, B., Alfonso, C., Mingorance, J., Rivas, G., and Jiménez, M. (2012) Isolation, characterization and lipid-binding properties of the recalcitrant FtsA division protein from Escherichia coli. PLoS ONE 7, e39829
    • (2012) PLoS ONE , vol.7
    • Martos, A.1    Monterroso, B.2    Zorrilla, S.3    Reija, B.4    Alfonso, C.5    Mingorance, J.6    Rivas, G.7    Jiménez, M.8
  • 62
    • 36549087126 scopus 로고    scopus 로고
    • Dimerization or oligomerization of the actin-like FtsA protein enhances the integrity of the cytokinetic Z ring
    • Shiomi, D., and Margolin, W. (2007) Dimerization or oligomerization of the actin-like FtsA protein enhances the integrity of the cytokinetic Z ring. Mol. Microbiol. 66,1396-1415
    • (2007) Mol. Microbiol. , vol.66 , pp. 1396-1415
    • Shiomi, D.1    Margolin, W.2
  • 63
    • 7744230898 scopus 로고    scopus 로고
    • Z-ring-independent interaction between a subdomain of FtsA and late septation proteins as revealed by a polar recruitment assay
    • Corbin, B. D., Geissler, B., Sadasivam, M., and Margolin, W. (2004) Z-ring-independent interaction between a subdomain of FtsA and late septation proteins as revealed by a polar recruitment assay. J. Bacteriol. 186, 7736-7744
    • (2004) J. Bacteriol. , vol.186 , pp. 7736-7744
    • Corbin, B.D.1    Geissler, B.2    Sadasivam, M.3    Margolin, W.4
  • 64
    • 84861204197 scopus 로고    scopus 로고
    • The early divisome protein FtsA interacts directly through its 1c subdomain with the cytoplasmic domain of the late divisome protein FtsN
    • Busiek, K. K., Eraso, J. M., Wang, Y., and Margolin, W. (2012) The early divisome protein FtsA interacts directly through its 1c subdomain with the cytoplasmic domain of the late divisome protein FtsN. J. Bacteriol. 194,1989-2000
    • (2012) J. Bacteriol. , vol.194 , pp. 1989-2000
    • Busiek, K.K.1    Eraso, J.M.2    Wang, Y.3    Margolin, W.4
  • 65
    • 84155167132 scopus 로고    scopus 로고
    • FtsA mutants impaired for self-interaction bypass ZipA suggesting a model in which FtsA's self-interaction competes with its ability to recruit downstream division proteins
    • Pichoff, S., Shen, B., Sullivan, B., and Lutkenhaus, J. (2012) FtsA mutants impaired for self-interaction bypass ZipA suggesting a model in which FtsA's self-interaction competes with its ability to recruit downstream division proteins. Mol. Microbiol. 83, 151-167
    • (2012) Mol. Microbiol. , vol.83 , pp. 151-167
    • Pichoff, S.1    Shen, B.2    Sullivan, B.3    Lutkenhaus, J.4
  • 66
    • 84857375148 scopus 로고    scopus 로고
    • The Escherichia coli cell division protein ZipA forms homodimers prior to association with FtsZ
    • Skoog, K., and Daley, D. O. (2012) The Escherichia coli cell division protein ZipA forms homodimers prior to association with FtsZ. Biochemistry 51, 1407-1415
    • (2012) Biochemistry , vol.51 , pp. 1407-1415
    • Skoog, K.1    Daley, D.O.2
  • 67
    • 0034600952 scopus 로고    scopus 로고
    • The bacterial cell-division protein ZipA and its interaction with an FtsZ fragment revealed by X-ray crystallography
    • Mosyak, L., Zhang, Y., Glasfeld, E., Haney, S., Stahl, M., Seehra, J., and Somers, W. S. (2000) The bacterial cell-division protein ZipA and its interaction with an FtsZ fragment revealed by X-ray crystallography. EMBO J. 19, 3179-3191
    • (2000) EMBO J , vol.19 , pp. 3179-3191
    • Mosyak, L.1    Zhang, Y.2    Glasfeld, E.3    Haney, S.4    Stahl, M.5    Seehra, J.6    Somers, W.S.7
  • 68
    • 84868326175 scopus 로고    scopus 로고
    • ZipA is required for FtsZ-dependent preseptal peptidoglycan synthesis prior to invagination during cell division
    • Potluri, L. P., Kannan, S., and Young, K. D. (2012) ZipA is required for FtsZ-dependent preseptal peptidoglycan synthesis prior to invagination during cell division. J. Bacteriol. 194, 5334-5342
    • (2012) J. Bacteriol. , vol.194 , pp. 5334-5342
    • Potluri, L.P.1    Kannan, S.2    Young, K.D.3
  • 69
    • 0037386678 scopus 로고    scopus 로고
    • A gain-of-function mutation in ftsA bypasses the requirement for the essential cell division gene zipA in Escherichia coli
    • Geissler, B., Elraheb, D., and Margolin, W. (2003) 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. 100, 4197-4202
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 4197-4202
    • Geissler, B.1    Elraheb, D.2    Margolin, W.3
  • 72
    • 84870297573 scopus 로고    scopus 로고
    • Membrane reconstitution of FtsZ-ZipA complex inside giant spherical vesicles made of E. coli lipids: Large membrane dilation and analysis of membrane plasticity
    • López-Montero, I., López-Navajas, P., Mingorance, J., Vélez, M., Vicente, M., and Monroy, F. (2013) Membrane reconstitution of FtsZ-ZipA complex inside giant spherical vesicles made of E. coli lipids: large membrane dilation and analysis of membrane plasticity. Biochimica et biophysica acta. 1828, 687-698
    • (2013) Biochimica et Biophysica Acta , vol.1828 , pp. 687-698
    • López-Montero, I.1    López-Navajas, P.2    Mingorance, J.3    Vélez, M.4    Vicente, M.5    Monroy, F.6
  • 73
    • 84880526897 scopus 로고    scopus 로고
    • Intrinsic disorder of the bacterial cell division protein ZipA: Coil-to-brush conformational transition
    • 10.1096/fj.12-224337
    • López-Montero, I., López-Navajas, P., Mingorance, J., Rivas, G., Vélez, M., Vicente, M., and Monroy, F. (2013) Intrinsic disorder of the bacterial cell division protein ZipA: coil-to-brush conformational transition. FASEB J. 10.1096/fj.12-224337
    • (2013) FASEB J
    • López-Montero, I.1    López-Navajas, P.2    Mingorance, J.3    Rivas, G.4    Vélez, M.5    Vicente, M.6    Monroy, F.7
  • 74
    • 33646573759 scopus 로고    scopus 로고
    • Bacterial mor-phogenes
    • (Vicente, M., Tamames, J., Valencia, A., and Mingorance, J., eds) , Kluwer Academic/Plenum Publishers, New York
    • Mingorance, J., Rico, A. I., and Gómez-Puertas, P. (2004) Bacterial mor-phogenes. in Molecules in Time and Space: Bacterial Shape, Division and Phylogeny (Vicente, M., Tamames, J., Valencia, A., and Mingorance, J., eds) pp. 173-194, Kluwer Academic/Plenum Publishers, New York
    • (2004) Molecules in Time and Space: Bacterial Shape, Division and Phylogeny , pp. 173-194
    • Mingorance, J.1    Rico, A.I.2    Gómez-Puertas, P.3
  • 75
    • 33745195461 scopus 로고    scopus 로고
    • Premature targeting ofcell division proteins to midcell reveals hierarchies ofprotein interactions involved in divisome assembly
    • Goehring, N. W., Gonzalez, M. D., and Beckwith, J. (2006) Premature targeting ofcell division proteins to midcell reveals hierarchies ofprotein interactions involved in divisome assembly. Mol. Microbiol. 61, 33- 45
    • (2006) Mol. Microbiol. , vol.61 , pp. 33-45
    • Goehring, N.W.1    Gonzalez, M.D.2    Beckwith, J.3
  • 76
    • 76349104603 scopus 로고    scopus 로고
    • Fully efficient chromosome dimer resolution in Escherichia coli cells lacking the integral membrane domain of FtsK
    • Dubarry, N., and Barre, F. X. (2010) Fully efficient chromosome dimer resolution in Escherichia coli cells lacking the integral membrane domain of FtsK. EMBO J. 29, 597-605
    • (2010) EMBO J , vol.29 , pp. 597-605
    • Dubarry, N.1    Barre, F.X.2
  • 77
    • 78649592020 scopus 로고    scopus 로고
    • Multiple regions along the Escherichia coli FtsK protein are implicated in cell division
    • Dubarry, N., Possoz, C., and Barre, F. X. (2010) Multiple regions along the Escherichia coli FtsK protein are implicated in cell division. Mol. Micro-biol. 78,1088-1100
    • (2010) Mol. Micro-biol. , vol.78 , pp. 1088-1100
    • Dubarry, N.1    Possoz, C.2    Barre, F.X.3
  • 78
    • 34247859209 scopus 로고    scopus 로고
    • Interaction between cell division proteins FtsE and FtsZ
    • Corbin, B. D., Wang, Y., Beuria, T. K., and Margolin, W. (2007) Interaction between cell division proteins FtsE and FtsZ. J. Bacteriol. 189, 3026-3035
    • (2007) J. Bacteriol. , vol.189 , pp. 3026-3035
    • Corbin, B.D.1    Wang, Y.2    Beuria, T.K.3    Margolin, W.4
  • 79
  • 80
    • 77952577603 scopus 로고    scopus 로고
    • Multiple interaction domains in FtsL, a protein component of the widely conserved bacterial FtsLBQ cell division complex
    • Gonzalez, M. D., Akbay, E. A., Boyd, D., and Beckwith, J. (2010) Multiple interaction domains in FtsL, a protein component of the widely conserved bacterial FtsLBQ cell division complex. J. Bacteriol. 192, 2757-2768
    • (2010) J. Bacteriol. , vol.192 , pp. 2757-2768
    • Gonzalez, M.D.1    Akbay, E.A.2    Boyd, D.3    Beckwith, J.4
  • 81
    • 65249155295 scopus 로고    scopus 로고
    • Divisome under construction: Distinct domains of the small membrane protein FtsB are necessary for interaction with multiple cell division proteins
    • Gonzalez, M. D., and Beckwith, J. (2009) Divisome under construction: distinct domains of the small membrane protein FtsB are necessary for interaction with multiple cell division proteins. J. Bacteriol. 191, 2815-2825
    • (2009) J. Bacteriol. , vol.191 , pp. 2815-2825
    • Gonzalez, M.D.1    Beckwith, J.2
  • 86
    • 39749105962 scopus 로고    scopus 로고
    • The monofunctional glycosyltransferase of Esche-richia coli localizes to the cell division site and interacts with penicillin-binding protein 3, FtsW, and FtsN
    • Derouaux, A., Wolf, B., Fraipont, C., Breukink, E., Nguyen-Disteche, M., and Terrak, M. (2008) The monofunctional glycosyltransferase of Esche-richia coli localizes to the cell division site and interacts with penicillin-binding protein 3, FtsW, and FtsN. J. Bacteriol. 190, 1831-1834
    • (2008) J. Bacteriol. , vol.190 , pp. 1831-1834
    • Derouaux, A.1    Wolf, B.2    Fraipont, C.3    Breukink, E.4    Nguyen-Disteche, M.5    Terrak, M.6
  • 87
    • 33846650968 scopus 로고    scopus 로고
    • The trans-envelope Tol-Pal complex is part of the cell division machinery and required for proper outer-membrane invagination during cell constriction in E. coli
    • Gerding, M. A., Ogata, Y., Pecora, N. D., Niki, H., and de Boer, P. A. (2007) The trans-envelope Tol-Pal complex is part of the cell division machinery and required for proper outer-membrane invagination during cell constriction in E. coli. Mol. Microbiol. 63,1008 -1025
    • (2007) Mol. Microbiol. , vol.63 , pp. 1008-1025
    • Gerding, M.A.1    Ogata, Y.2    Pecora, N.D.3    Niki, H.4    De Boer, P.A.5
  • 88
    • 34249811807 scopus 로고    scopus 로고
    • An altered FtsA can compensate for the loss of essential cell division protein FtsN in Escherichia coli
    • Bernard, C. S., Sadasivam, M., Shiomi, D., and Margolin, W. (2007) An altered FtsA can compensate for the loss of essential cell division protein FtsN in Escherichia coli. Mol. Microbiol. 64,1289 -1305
    • (2007) Mol. Microbiol. , vol.64 , pp. 1289-1305
    • Bernard, C.S.1    Sadasivam, M.2    Shiomi, D.3    Margolin, W.4
  • 89
    • 80052525834 scopus 로고    scopus 로고
    • A fail-safe mechanism in the septal ring assembly pathway generated by the sequential recruitment of cell separation amidases and their activators
    • Peters, N. T., Dinh, T., and Bernhardt, T. G. (2011) A fail-safe mechanism in the septal ring assembly pathway generated by the sequential recruitment of cell separation amidases and their activators. J. Bacteriol. 193, 4973-4983
    • (2011) J. Bacteriol. , vol.193 , pp. 4973-4983
    • Peters, N.T.1    Dinh, T.2    Bernhardt, T.G.3
  • 90
    • 44049091371 scopus 로고    scopus 로고
    • Reconstitution of contractile FtsZ rings in liposomes
    • Osawa, M., Anderson, D. E., and Erickson, H. P. (2008) Reconstitution of contractile FtsZ rings in liposomes. Science 320, 792-794
    • (2008) Science , vol.320 , pp. 792-794
    • Osawa, M.1    Anderson, D.E.2    Erickson, H.P.3
  • 91
    • 0033986992 scopus 로고    scopus 로고
    • Straight and curved conformations of FtsZ are regulated by GTP hydrolysis
    • Lu, C., Reedy, M., and Erickson, H. P. (2000) Straight and curved conformations of FtsZ are regulated by GTP hydrolysis. J. Bacteriol. 182, 164-170
    • (2000) J. Bacteriol. , vol.182 , pp. 164-170
    • Lu, C.1    Reedy, M.2    Erickson, H.P.3
  • 92
    • 0035907236 scopus 로고    scopus 로고
    • Activation of cell division protein FtsZ. Control of switch loop T3 conformation by the nucleotide 7-phosphate
    • Díaz, J. F., Kralicek, A., Mingorance, J., Palacios, J. M., Vicente, M., and Andreu, J. M. (2001) Activation of cell division protein FtsZ. Control of switch loop T3 conformation by the nucleotide 7-phosphate. J. Biol. Chem. 276,17307-17315
    • (2001) J. Biol. Chem. , vol.276 , pp. 17307-17315
    • Díaz, J.F.1    Kralicek, A.2    Mingorance, J.3    Palacios, J.M.4    Vicente, M.5    Andreu, J.M.6
  • 94
    • 55049117823 scopus 로고    scopus 로고
    • Origin of contractile force during cell division of bacteria
    • Ghosh, B., and Sain, A. (2008) Origin of contractile force during cell division of bacteria. Phys. Rev. Lett. 101,178101
    • (2008) Phys. Rev. Lett. , vol.101 , pp. 178101
    • Ghosh, B.1    Sain, A.2
  • 95
    • 79961066637 scopus 로고    scopus 로고
    • Force generation in bacteria without nucle-otide-dependent bending ofcytoskeletal filaments
    • Ghosh, B., and Sain, A. (2011) Force generation in bacteria without nucle-otide-dependent bending ofcytoskeletal filaments. Phys. Rev. EStat. Non-lin. Soft Matter Phys. 83, 051924
    • (2011) Phys. Rev. EStat. Non-lin. Soft Matter Phys. , vol.83 , pp. 051924
    • Ghosh, B.1    Sain, A.2
  • 96
    • 34247495145 scopus 로고    scopus 로고
    • FtsZ polymer-bundling by the Escherichia coli ZapA orthologue, YgfE, involves a conformational change in bound GTP
    • Small, E., Marrington, R., Rodger, A., Scott, D. J., Sloan, K., Roper, D., Dafforn, T. R., and Addinall, S. G. (2007) FtsZ polymer-bundling by the Escherichia coli ZapA orthologue, YgfE, involves a conformational change in bound GTP. J. Mol. Biol. 369, 210-221
    • (2007) J. Mol. Biol. , vol.369 , pp. 210-221
    • Small, E.1    Marrington, R.2    Rodger, A.3    Scott, D.J.4    Sloan, K.5    Roper, D.6    Dafforn, T.R.7    Addinall, S.G.8
  • 97
    • 84869868586 scopus 로고    scopus 로고
    • Superresolution microscopy for microbiology
    • Coltharp, C., and Xiao, J. (2012) Superresolution microscopy for microbiology. Cell. Microbiol. 14,1808-1818
    • (2012) Cell. Microbiol. , vol.14 , pp. 1808-1818
    • Coltharp, C.1    Xiao, J.2
  • 98
    • 84869878393 scopus 로고    scopus 로고
    • Towards a bottom-up reconstitution of bacterial cell division
    • Martos, A., Jiménez, M., Rivas, G., and Schwille, P. (2012) Towards a bottom-up reconstitution of bacterial cell division. Trends Cell Biol. 22, 634-643
    • (2012) Trends Cell Biol. , vol.22 , pp. 634-643
    • Martos, A.1    Jiménez, M.2    Rivas, G.3    Schwille, P.4


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