메뉴 건너뛰기




Volumn 40, Issue 1, 2015, Pages 57-67

The keepers of the ring: Regulators of FtsZ assembly

Author keywords

Bacterial division; Central hub; Divisome; FtsZ ring; Septum position

Indexed keywords

CLPXP PROTEASE; FTSA PROTEIN; FTSZ PROTEIN; MINCDE PROTEIN; PROTEASOME; PROTEIN; SLMA PROTEIN; UNCLASSIFIED DRUG; ZAP PROTEIN; ZIPA PROTEIN; BACTERIAL PROTEIN; CYTOSKELETON PROTEIN; ESCHERICHIA COLI PROTEIN; FTSZ PROTEIN, BACTERIA; PROTEIN BINDING;

EID: 84962013765     PISSN: 01686445     EISSN: 15746976     Source Type: Journal    
DOI: 10.1093/femsre/fuv040     Document Type: Review
Times cited : (114)

References (125)
  • 1
    • 84923083359 scopus 로고    scopus 로고
    • Nucleoid occlusion protein Noc recruits DNA to the bacterial cell membrane
    • Adams DW, Wu LJ, Errington J. Nucleoid occlusion protein Noc recruits DNA to the bacterial cell membrane. EMBO J 2015;34:491-501.
    • (2015) EMBO J , vol.34 , pp. 491-501
    • Adams, D.W.1    Wu, L.J.2    Errington, J.3
  • 2
    • 0030448723 scopus 로고    scopus 로고
    • FtsA is localized to the septum in an FtsZ-dependent manner
    • Addinall SG, Lutkenhaus J. FtsA is localized to the septum in an FtsZ-dependent manner. J Bacteriol 1996;178:7167-72.
    • (1996) J Bacteriol , vol.178 , pp. 7167-7172
    • Addinall, S.G.1    Lutkenhaus, J.2
  • 3
    • 4344652693 scopus 로고    scopus 로고
    • Assembly dynamics of FtsZ rings in Bacillus subtilis and Escherichia coli and effects of FtsZ-regulating proteins
    • Anderson DE, Gueiros-Filho FJ, Erickson HP. Assembly dynamics of FtsZ rings in Bacillus subtilis and Escherichia coli and effects of FtsZ-regulating proteins. J Bacteriol 2004;186:5775-81.
    • (2004) J Bacteriol , vol.186 , pp. 5775-5781
    • Anderson, D.E.1    Gueiros-Filho, F.J.2    Erickson, H.P.3
  • 4
    • 19444386428 scopus 로고    scopus 로고
    • SlmA, a nucleoid-associated, FtsZ binding protein required for blocking septal ring assembly over Chromosomes in E. coli
    • Bernhardt TG, de Boer PA. SlmA, a nucleoid-associated, FtsZ binding protein required for blocking septal ring assembly over Chromosomes in E. coli. Mol Cell 2005;18:555-64.
    • (2005) Mol Cell , vol.18 , pp. 555-564
    • Bernhardt, T.G.1    de Boer, P.A.2
  • 5
    • 56749185690 scopus 로고    scopus 로고
    • A novel component of the division-site selection system of Bacillus subtilis and a new mode of action for the division inhibitor MinCD
    • Bramkamp M, Emmins R, Weston L, et al. A novel component of the division-site selection system of Bacillus subtilis and a new mode of action for the division inhibitor MinCD. Mol Microbiol 2008;70:1556-69.
    • (2008) Mol Microbiol , vol.70 , pp. 1556-1569
    • Bramkamp, M.1    Emmins, R.2    Weston, L.3
  • 6
    • 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 KK, Eraso JM, Wang Y, et al. The early divisome protein FtsA interacts directly through its 1c subdomain with the cytoplasmic domain of the late divisome protein FtsN. J Bacteriol 2012;194:1989-2000.
    • (2012) J Bacteriol , vol.194 , pp. 1989-2000
    • Busiek, K.K.1    Eraso, J.M.2    Wang, Y.3
  • 7
    • 84859484529 scopus 로고    scopus 로고
    • Extreme C terminus of bacterial cytoskeletal protein FtsZ plays fundamental role in assembly independent of modulatory proteins
    • Buske PJ, Levin PA. Extreme C terminus of bacterial cytoskeletal protein FtsZ plays fundamental role in assembly independent of modulatory proteins. J Biol Chem 2012;287: 10945-57.
    • (2012) J Biol Chem , vol.287 , pp. 10945-10957
    • Buske, P.J.1    Levin, P.A.2
  • 8
    • 84880133681 scopus 로고    scopus 로고
    • A flexible C-terminal linker is required for proper FtsZ assembly in vitro and cytokinetic ring formation in vivo
    • Buske PJ, Levin PA. A flexible C-terminal linker is required for proper FtsZ assembly in vitro and cytokinetic ring formation in vivo. Mol Microbiol 2013;89:249-63.
    • (2013) Mol Microbiol , vol.89 , pp. 249-263
    • Buske, P.J.1    Levin, P.A.2
  • 9
    • 84930317836 scopus 로고    scopus 로고
    • A multi-layered protein network stabilizes the Escherichia coli FtsZ-ring and modulates constriction dynamics
    • Buss J, Coltharp C, Shtengel G, et al. A multi-layered protein network stabilizes the Escherichia coli FtsZ-ring and modulates constriction dynamics. PLoS Genet 2015;11: e1005128.
    • (2015) PLoS Genet , vol.11 , pp. e1005128
    • Buss, J.1    Coltharp, C.2    Shtengel, G.3
  • 10
    • 84929379297 scopus 로고    scopus 로고
    • The nucleoid occlusion SlmA protein accelerates the disassembly of the FtsZ protein polymers without affecting their GTPase activity
    • Cabre EJ, Monterroso B, Alfonso C, et al. The nucleoid occlusion SlmA protein accelerates the disassembly of the FtsZ protein polymers without affecting their GTPase activity. PLoS One 2015;10:e0126434.
    • (2015) PLoS One , vol.10 , pp. e0126434
    • Cabre, E.J.1    Monterroso, B.2    Alfonso, C.3
  • 11
    • 84884200102 scopus 로고    scopus 로고
    • Bacterial division proteins FtsZ and ZipA induce vesicle shrinkage and cell membrane invagination
    • Cabre EJ, Sanchez-Gorostiaga A, Carrara P, et al. Bacterial division proteins FtsZ and ZipA induce vesicle shrinkage and cell membrane invagination. J Biol Chem 2013;288:26625-34.
    • (2013) J Biol Chem , vol.288 , pp. 26625-26634
    • Cabre, E.J.1    Sanchez-Gorostiaga, A.2    Carrara, P.3
  • 12
    • 67649811066 scopus 로고    scopus 로고
    • ClpXP protease degrades the cytoskeletal protein, FtsZ, and modulates FtsZ polymer dynamics
    • Camberg JL, Hoskins JR, Wickner S. ClpXP protease degrades the cytoskeletal protein, FtsZ, and modulates FtsZ polymer dynamics. P Natl Acad Sci USA 2009;106:10614-19.
    • (2009) P Natl Acad Sci USA , vol.106 , pp. 10614-10619
    • Camberg, J.L.1    Hoskins, J.R.2    Wickner, S.3
  • 13
    • 84859270357 scopus 로고    scopus 로고
    • Identification of a region in the N-terminus of Escherichia coli Lon that affects ATPase, substrate translocation and proteolytic activity
    • Cheng I, Mikita N, Fishovitz J, et al. Identification of a region in the N-terminus of Escherichia coli Lon that affects ATPase, substrate translocation and proteolytic activity. J Mol Biol 2012;418:208-25.
    • (2012) J Mol Biol , vol.418 , pp. 208-225
    • Cheng, I.1    Mikita, N.2    Fishovitz, J.3
  • 14
    • 84874784097 scopus 로고    scopus 로고
    • Identification of the SlmA active site responsible for blocking bacterial cytokinetic ring assembly over the chromosome
    • Cho H, Bernhardt TG. Identification of the SlmA active site responsible for blocking bacterial cytokinetic ring assembly over the chromosome. PLoS Genet 2013;9:e1003304.
    • (2013) PLoS Genet , vol.9 , pp. e1003304
    • Cho, H.1    Bernhardt, T.G.2
  • 15
    • 79952741894 scopus 로고    scopus 로고
    • Nucleoid occlusion factor SlmA is a DNA-activated FtsZ polymerization antagonist
    • Cho H, McManus HR, Dove SL, et al. Nucleoid occlusion factor SlmA is a DNA-activated FtsZ polymerization antagonist. P Natl Acad Sci USA 2011;108:3773-8.
    • (2011) P Natl Acad Sci USA , vol.108 , pp. 3773-3778
    • Cho, H.1    McManus, H.R.2    Dove, S.L.3
  • 16
    • 0035873567 scopus 로고    scopus 로고
    • Crystal structure of the bacterial cell division inhibitor MinC
    • Cordell SC, Anderson RE, Lowe J. Crystal structure of the bacterial cell division inhibitor MinC. EMBO J 2001;20:2454-61.
    • (2001) EMBO J , vol.20 , pp. 2454-2461
    • Cordell, S.C.1    Anderson, R.E.2    Lowe, J.3
  • 17
    • 0038610624 scopus 로고    scopus 로고
    • Crystal structure of the SOS cell division inhibitor SulA and in complex with FtsZ
    • Cordell SC, Robinson EJ, Löwe J. Crystal structure of the SOS cell division inhibitor SulA and in complex with FtsZ. P Natl Acad Sci USA 2003;100:7889-94.
    • (2003) P Natl Acad Sci USA , vol.100 , pp. 7889-7894
    • Cordell, S.C.1    Robinson, E.J.2    Löwe, J.3
  • 18
    • 0026697767 scopus 로고
    • The proper ratio of FtsZ to FtsA is required for cell division to occur in Escherichia coli
    • 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.
    • (1992) J Bacteriol , vol.174 , pp. 6145-6151
    • Dai, K.1    Lutkenhaus, J.2
  • 19
    • 41549109871 scopus 로고    scopus 로고
    • Investigation of regulation of FtsZ assembly by SulA and development of a model for FtsZ polymerization
    • 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.
    • (2008) J Bacteriol , vol.190 , pp. 2513-2526
    • Dajkovic, A.1    Mukherjee, A.2    Lutkenhaus, J.3
  • 20
    • 0024977391 scopus 로고
    • A division inhibitor and a topological specificity factor coded for by the minicell locus determine proper placement of the division septum in E. coli
    • de Boer PA, Crossley RE, Rothfield LI. A division inhibitor and a topological specificity factor coded for by the minicell locus determine proper placement of the division septum in E. coli. Cell 1989;56:641-9.
    • (1989) Cell , vol.56 , pp. 641-649
    • de Boer, P.A.1    Crossley, R.E.2    Rothfield, L.I.3
  • 21
    • 0026585155 scopus 로고
    • Roles of MinC and MinD in the site-specific septation block mediated by the MinCDE system of Escherichia coli
    • de Boer PA, Crossley RE, Rothfield LI. Roles of MinC and MinD in the site-specific septation block mediated by the MinCDE system of Escherichia coli. J Bacteriol 1992;174:63-70.
    • (1992) J Bacteriol , vol.174 , pp. 63-70
    • de Boer, P.A.1    Crossley, R.E.2    Rothfield, L.I.3
  • 22
    • 84905483299 scopus 로고    scopus 로고
    • SlmA antagonism of FtsZ assembly employs a two-pronged mechanism like MinCD
    • Du S, Lutkenhaus J. SlmA antagonism of FtsZ assembly employs a two-pronged mechanism like MinCD. PLoS Genet 2014;10:e1004460.
    • (2014) PLoS Genet , vol.10 , pp. e1004460
    • Du, S.1    Lutkenhaus, J.2
  • 23
    • 84920656474 scopus 로고    scopus 로고
    • Oligomerization of FtsZ converts the FtsZ tailmotif (conserved carboxy-terminal peptide) into a multivalent ligand with high avidity for partners ZipA and SlmA
    • Du S, Park KT, Lutkenhaus J. Oligomerization of FtsZ converts the FtsZ tailmotif (conserved carboxy-terminal peptide) into a multivalent ligand with high avidity for partners ZipA and SlmA. Mol Microbiol 2015;95:173-88.
    • (2015) Mol Microbiol , vol.95 , pp. 173-188
    • Du, S.1    Park, K.T.2    Lutkenhaus, J.3
  • 24
    • 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, et al. Identification of ZapD as a cell division factor that promotes the assembly of FtsZ in Escherichia coli. J Bacteriol 2012;194:3189-98.
    • (2012) J Bacteriol , vol.194 , pp. 3189-3198
    • Durand-Heredia, J.1    Rivkin, E.2    Fan, G.3
  • 25
    • 41749083933 scopus 로고    scopus 로고
    • Novel coiled-coil cell division factor ZapB stimulates Z ring assembly and cell division
    • Ebersbach G, Galli E, Møller-Jensen J, et al. Novel coiled-coil cell division factor ZapB stimulates Z ring assembly and cell division. Mol Microbiol 2008;68:720-35.
    • (2008) Mol Microbiol , vol.68 , pp. 720-735
    • Ebersbach, G.1    Galli, E.2    Møller-Jensen, J.3
  • 26
    • 0035146299 scopus 로고    scopus 로고
    • The FtsZ protofilament and attachment of ZipA-structural constraints on the FtsZ power stroke
    • Erickson HP. The FtsZ protofilament and attachment of ZipA-structural constraints on the FtsZ power stroke. Curr Opin Cell Biol 2001;13:55-60.
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 55-60
    • Erickson, H.P.1
  • 27
    • 78650078263 scopus 로고    scopus 로고
    • FtsZ in bacterial cytokinesis: cytoskeleton and force generator all in one
    • Erickson HP, Anderson DE, Osawa M. FtsZ in bacterial cytokinesis: cytoskeleton and force generator all in one. Microbiol Mol Biol R 2010;74:504-28.
    • (2010) Microbiol Mol Biol R , vol.74 , pp. 504-528
    • Erickson, H.P.1    Anderson, D.E.2    Osawa, M.3
  • 28
    • 84864147092 scopus 로고    scopus 로고
    • A MatP-divisome interaction coordinates chromosome segregation with cell division in E. coli
    • Espeli O, Borne R, Dupaigne P, et al. A MatP-divisome interaction coordinates chromosome segregation with cell division in E. coli. EMBO J 2012;31:3198-211.
    • (2012) EMBO J , vol.31 , pp. 3198-3211
    • Espeli, O.1    Borne, R.2    Dupaigne, P.3
  • 29
    • 84921468436 scopus 로고    scopus 로고
    • MapZ marks the division sites and positions FtsZ rings in Streptococcus pneumoniae
    • Fleurie A, Lesterlin C, Manuse S, et al. MapZ marks the division sites and positions FtsZ rings in Streptococcus pneumoniae. Nature 2014;516:259-62.
    • (2014) Nature , vol.516 , pp. 259-262
    • Fleurie, A.1    Lesterlin, C.2    Manuse, S.3
  • 30
    • 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, et al. In vivo structure of the E. coli FtsZ-ring revealed by photoactivated localization microscopy (PALM). PLoS One 2010;5:e12682.
    • (2010) PLoS One , vol.5 , pp. e12682
    • Fu, G.1    Huang, T.2    Buss, J.3
  • 31
    • 84855881444 scopus 로고    scopus 로고
    • FtsZ-ZapA-ZapB interactome of Escherichia coli
    • Galli E, Gerdes K. FtsZ-ZapA-ZapB interactome of Escherichia coli. J Bacteriol 2012;194:292-302.
    • (2012) J Bacteriol , vol.194 , pp. 292-302
    • Galli, E.1    Gerdes, K.2
  • 32
    • 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, Margolin W. A gain-of-function mutation in ftsA bypasses the requirement for the essential cell division gene zipA in Escherichia coli. P Natl Acad Sci USA 2003;100:4197-202.
    • (2003) P Natl Acad Sci USA , vol.100 , pp. 4197-4202
    • Geissler, B.1    Elraheb, D.2    Margolin, W.3
  • 33
    • 84921715486 scopus 로고    scopus 로고
    • MinCD cell division proteins form alternating copolymeric cytomotive filaments
    • Ghosal D, Trambaiolo D, Amos LA, et al. MinCD cell division proteins form alternating copolymeric cytomotive filaments. Nat Commun 2014;5:5341.
    • (2014) Nat Commun , vol.5 , pp. 5341
    • Ghosal, D.1    Trambaiolo, D.2    Amos, L.A.3
  • 34
    • 84937976428 scopus 로고    scopus 로고
    • The essential role of SepF in mycobacterial division
    • Gola S, Munder T, Casonato S, et al. The essential role of SepF in mycobacterial division. Mol Microbiol 2015;97:560-76.
    • (2015) Mol Microbiol , vol.97 , pp. 560-576
    • Gola, S.1    Munder, T.2    Casonato, S.3
  • 35
    • 0036791675 scopus 로고    scopus 로고
    • A widely conserved bacterial cell division protein that promotes assembly of the tubulin-like protein FtsZ
    • Gueiros-Filho FJ, Losick R. A widely conserved bacterial cell division protein that promotes assembly of the tubulin-like protein FtsZ. Gene Dev 2002;16:2544-56.
    • (2002) Gene Dev , vol.16 , pp. 2544-2556
    • Gueiros-Filho, F.J.1    Losick, R.2
  • 36
    • 63049127158 scopus 로고    scopus 로고
    • ClpX inhibits FtsZ assembly in a manner that does not require its ATP hydrolysisdependent chaperone activity
    • Haeusser DP, Lee AH, Weart RB, et al. ClpX inhibits FtsZ assembly in a manner that does not require its ATP hydrolysisdependent chaperone activity. J Bacteriol 2009;191:1986-91.
    • (2009) J Bacteriol , vol.191 , pp. 1986-1991
    • Haeusser, D.P.1    Lee, A.H.2    Weart, R.B.3
  • 37
    • 84939795102 scopus 로고    scopus 로고
    • Amutation in Escherichia coli ftsZ bypasses the requirement for the essential division gene zipA and confers resistance to FtsZ assembly inhibitors by stabilizing protofilament bundling
    • Haeusser DP, Rowlett VW, Margolin W. Amutation in Escherichia coli ftsZ bypasses the requirement for the essential division gene zipA and confers resistance to FtsZ assembly inhibitors by stabilizing protofilament bundling. Mol Microbiol 2015;97:988-1005.
    • (2015) Mol Microbiol , vol.97 , pp. 988-1005
    • Haeusser, D.P.1    Rowlett, V.W.2    Margolin, W.3
  • 38
    • 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. coli
    • Hale CA, de Boer PA. 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.
    • (1997) Cell , vol.88 , pp. 175-185
    • Hale, C.A.1    de Boer, P.A.2
  • 39
    • 0032953626 scopus 로고    scopus 로고
    • Recruitment of ZipA to the septal ring of Escherichia coli is dependent on FtsZ and independent of FtsA
    • Hale CA, de Boer PA. Recruitment of ZipA to the septal ring of Escherichia coli is dependent on FtsZ and independent of FtsA. J Bacteriol 1999;181:167-76.
    • (1999) J Bacteriol , vol.181 , pp. 167-176
    • Hale, C.A.1    de Boer, P.A.2
  • 40
    • 0033810918 scopus 로고    scopus 로고
    • ZipA-induced bundling of FtsZ polymers mediated by an interaction between C-terminal domains
    • Hale CA, Rhee AC, de Boer PA. ZipA-induced bundling of FtsZ polymers mediated by an interaction between C-terminal domains. J Bacteriol 2000;182:5153-66.
    • (2000) J Bacteriol , vol.182 , pp. 5153-5166
    • Hale, C.A.1    Rhee, A.C.2    de Boer, P.A.3
  • 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 CA, Shiomi D, Liu B, 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.
    • (2011) J Bacteriol , vol.193 , pp. 1393-1404
    • Hale, C.A.1    Shiomi, D.2    Liu, B.3
  • 42
    • 33645055098 scopus 로고    scopus 로고
    • SepF, a novel FtsZinteracting protein required for a late step in cell division
    • Hamoen LW, Meile JC, de Jong W, et al. SepF, a novel FtsZinteracting protein required for a late step in cell division. Mol Microbiol 2006;59:989-99.
    • (2006) Mol Microbiol , vol.59 , pp. 989-999
    • Hamoen, L.W.1    Meile, J.C.2    de Jong, W.3
  • 43
    • 84911970999 scopus 로고    scopus 로고
    • A thermosensitive defect in the ATP binding pocket of FtsA can be suppressed by allosteric changes in the dimer interface
    • Herricks JR, Nguyen D, Margolin W. A thermosensitive defect in the ATP binding pocket of FtsA can be suppressed by allosteric changes in the dimer interface. Mol Microbiol 2014;94:713-27.
    • (2014) Mol Microbiol , vol.94 , pp. 713-727
    • Herricks, J.R.1    Nguyen, D.2    Margolin, W.3
  • 44
    • 84924178704 scopus 로고    scopus 로고
    • LocZ is a new cell division protein involved in proper septum placement in Streptococcus pneumoniae
    • Holeckova N, Doubravova L, Massidda O, et al. LocZ is a new cell division protein involved in proper septum placement in Streptococcus pneumoniae. MBio 2015;6:e01700-14.
    • (2015) MBio , vol.6 , pp. e01700-e01714
    • Holeckova, N.1    Doubravova, L.2    Massidda, O.3
  • 45
    • 0037241005 scopus 로고    scopus 로고
    • A conserved sequence at the C-terminus of MinD is required for binding to the membrane and targeting MinC to the septum
    • Hu Z, Lutkenhaus J. A conserved sequence at the C-terminus of MinD is required for binding to the membrane and targeting MinC to the septum. Mol Microbiol 2003;47:345-55.
    • (2003) Mol Microbiol , vol.47 , pp. 345-355
    • Hu, Z.1    Lutkenhaus, J.2
  • 46
    • 0033592949 scopus 로고    scopus 로고
    • The MinC component of the division site selection system in Escherichia coli interacts with FtsZ to prevent polymerization
    • Hu Z, Mukherjee A, Pichoff S, et al. The MinC component of the division site selection system in Escherichia coli interacts with FtsZ to prevent polymerization. P Natl Acad Sci USA 1999;96:14819-24.
    • (1999) P Natl Acad Sci USA , vol.96 , pp. 14819-14824
    • Hu, Z.1    Mukherjee, A.2    Pichoff, S.3
  • 47
    • 84876189962 scopus 로고    scopus 로고
    • FtsZ ring stability: of bundles, tubules, crosslinks, and curves
    • Huang KH, Durand-Heredia J, Janakiraman A. FtsZ ring stability: of bundles, tubules, crosslinks, and curves. J Bacteriol 2013;195:1859-68.
    • (2013) J Bacteriol , vol.195 , pp. 1859-1868
    • Huang, K.H.1    Durand-Heredia, J.2    Janakiraman, A.3
  • 48
    • 0344321693 scopus 로고
    • Cell-division control in Escherichia coli: specific induction of the SOS function SfiA protein is sufficient to block septation
    • Huisman O, D'Ari R, Gottesman S. Cell-division control in Escherichia coli: specific induction of the SOS function SfiA protein is sufficient to block septation. P Natl Acad Sci USA 1984;81:4490-4.
    • (1984) P Natl Acad Sci USA , vol.81 , pp. 4490-4494
    • Huisman, O.1    D'Ari, R.2    Gottesman, S.3
  • 49
    • 84903220304 scopus 로고    scopus 로고
    • Cell wall precursors are required to organize the chlamydial division septum
    • Jacquier N, Frandi A, Pillonel T, et al. Cell wall precursors are required to organize the chlamydial division septum. Nat Commun 2014;5:3578.
    • (2014) Nat Commun , vol.5 , pp. 3578
    • Jacquier, N.1    Frandi, A.2    Pillonel, T.3
  • 50
    • 0025314797 scopus 로고
    • Rule governing the division pattern in Escherichia coli minB and wild-type filaments
    • Jaffe A, Boye E, D'Ari R. Rule governing the division pattern in Escherichia coli minB and wild-type filaments. J Bacteriol 1990;172:3500-2.
    • (1990) J Bacteriol , vol.172 , pp. 3500-3502
    • Jaffe, A.1    Boye, E.2    D'Ari, R.3
  • 51
    • 1242275409 scopus 로고    scopus 로고
    • R174 of Escherichia coli FtsZ is involved in membrane interaction and protofilament bundling, and is essential for cell division
    • Koppelman CM, Aarsman ME, Postmus J, 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.
    • (2004) Mol Microbiol , vol.51 , pp. 645-657
    • Koppelman, C.M.1    Aarsman, M.E.2    Postmus, J.3
  • 52
    • 84865058426 scopus 로고    scopus 로고
    • Bacillus subtilis SepF binds to the C-terminus of FtsZ
    • Krol E, van Kessel SP, van Bezouwen LS, et al. Bacillus subtilis SepF binds to the C-terminus of FtsZ. PLoS One 2012;7:e43293.
    • (2012) PLoS One , vol.7 , pp. e43293
    • Krol, E.1    van Kessel, S.P.2    van Bezouwen, L.S.3
  • 53
    • 84920896637 scopus 로고    scopus 로고
    • Role of the FtsA C terminus as a switch for polymerization and membrane association
    • Krupka M, Cabre EJ, Jimenez M, et al. Role of the FtsA C terminus as a switch for polymerization and membrane association. MBio 2014;5:e02221.
    • (2014) MBio , vol.5 , pp. e02221
    • Krupka, M.1    Cabre, E.J.2    Jimenez, M.3
  • 54
    • 84857738215 scopus 로고    scopus 로고
    • Key role of two terminal domains in the bidirectional polymerization of FtsA protein
    • Krupka M, Rivas G, Rico AI, et al. Key role of two terminal domains in the bidirectional polymerization of FtsA protein. J Biol Chem 2012;287:7756-65.
    • (2012) J Biol Chem , vol.287 , pp. 7756-7765
    • Krupka, M.1    Rivas, G.2    Rico, A.I.3
  • 55
    • 13444282405 scopus 로고    scopus 로고
    • Cell division in cocci: localization and properties of the Streptococcus pneumoniae FtsA protein
    • Lara B, Rico AI, Petruzzelli S, et al. Cell division in cocci: localization and properties of the Streptococcus pneumoniae FtsA protein. Mol Microbiol 2005;55:699-711.
    • (2005) Mol Microbiol , vol.55 , pp. 699-711
    • Lara, B.1    Rico, A.I.2    Petruzzelli, S.3
  • 56
    • 36248938686 scopus 로고    scopus 로고
    • The structure of FtsZ filaments in vivo suggests a force-generating role in cell division
    • Li Z, Trimble MJ, Brun YV, et al. The structure of FtsZ filaments in vivo suggests a force-generating role in cell division. EMBO J 2007;26:4694-708.
    • (2007) EMBO J , vol.26 , pp. 4694-4708
    • Li, Z.1    Trimble, M.J.2    Brun, Y.V.3
  • 57
    • 44049091101 scopus 로고    scopus 로고
    • Spatial regulators for bacterial cell division self-organize into surface waves in vitro
    • Loose M, Fischer-Friedrich E, Ries J, et al. Spatial regulators for bacterial cell division self-organize into surface waves in vitro. Science 2008;320:789-92.
    • (2008) Science , vol.320 , pp. 789-792
    • Loose, M.1    Fischer-Friedrich, E.2    Ries, J.3
  • 58
    • 84891344282 scopus 로고    scopus 로고
    • The bacterial cell division proteins FtsA and FtsZ self-organize into dynamic cytoskeletal patterns
    • Loose M, Mitchison TJ. The bacterial cell division proteins FtsA and FtsZ self-organize into dynamic cytoskeletal patterns. Nat Cell Biol 2014;16:38-46.
    • (2014) Nat Cell Biol , vol.16 , pp. 38-46
    • Loose, M.1    Mitchison, T.J.2
  • 59
    • 84880526897 scopus 로고    scopus 로고
    • Intrinsic disorder of the bacterial cell division protein ZipA: coil-tobrush conformational transition
    • López-Montero I, López-Navajas P, Mingorance J, et al. Intrinsic disorder of the bacterial cell division protein ZipA: coil-tobrush conformational transition. FASEB J 2013;27:3363-75.
    • (2013) FASEB J , vol.27 , pp. 3363-3375
    • López-Montero, I.1    López-Navajas, P.2    Mingorance, J.3
  • 60
    • 4344620117 scopus 로고    scopus 로고
    • The crystal structure of ZapA and its modulation of FtsZ polymerisation
    • Low HH, Moncrieffe MC, Löwe J. The crystal structure of ZapA and its modulation of FtsZ polymerisation. J Mol Biol 2004;341:839-52.
    • (2004) J Mol Biol , vol.341 , pp. 839-852
    • Low, H.H.1    Moncrieffe, M.C.2    Löwe, J.3
  • 61
    • 2642593025 scopus 로고    scopus 로고
    • Crystal structure of the bacterial cell-division protein FtsZ
    • Löwe J, Amos LA. Crystal structure of the bacterial cell-division protein FtsZ. Nature 1998;391:203-6.
    • (1998) Nature , vol.391 , pp. 203-206
    • Löwe, J.1    Amos, L.A.2
  • 62
    • 84867995401 scopus 로고    scopus 로고
    • Bacterial cytokinesis: from Z ring to divisome
    • Lutkenhaus J, Pichoff S, Du S. Bacterial cytokinesis: from Z ring to divisome. Cytoskeleton 2012;69:778-90.
    • (2012) Cytoskeleton , vol.69 , pp. 778-790
    • Lutkenhaus, J.1    Pichoff, S.2    Du, S.3
  • 63
    • 31944450440 scopus 로고    scopus 로고
    • Building the invisible wall: updating the chlamydial peptidoglycan anomaly
    • McCoy AJ, Maurelli AT. Building the invisible wall: updating the chlamydial peptidoglycan anomaly. Trends Microbiol 2006;14:70-7.
    • (2006) Trends Microbiol , vol.14 , pp. 70-77
    • McCoy, A.J.1    Maurelli, A.T.2
  • 64
    • 0032213104 scopus 로고    scopus 로고
    • Polar localization of the MinD protein of Bacillus subtilis and its role in selection of the mid-cell division site
    • Marston AL, Thomaides HB, Edwards DH, et al. Polar localization of the MinD protein of Bacillus subtilis and its role in selection of the mid-cell division site. Gene Dev 1998;12:3419-30.
    • (1998) Gene Dev , vol.12 , pp. 3419-3430
    • Marston, A.L.1    Thomaides, H.B.2    Edwards, D.H.3
  • 65
    • 84899738160 scopus 로고    scopus 로고
    • ZapE is a novel cell division protein interacting with FtsZ and modulating the Zring dynamics
    • Marteyn BS, Karimova G, Fenton AK, et al. ZapE is a novel cell division protein interacting with FtsZ and modulating the Zring dynamics. mBio 2014;5:e00022-14.
    • (2014) mBio , vol.5 , pp. e00022-e00114
    • Marteyn, B.S.1    Karimova, G.2    Fenton, A.K.3
  • 66
    • 84888857354 scopus 로고    scopus 로고
    • From models to pathogens: how much have we learned about Streptococcus pneumoniae cell division?
    • Massidda O, Novakova L, Vollmer W. From models to pathogens: how much have we learned about Streptococcus pneumoniae cell division? Environ Microbiol 2013;15:3133-57.
    • (2013) Environ Microbiol , vol.15 , pp. 3133-3157
    • Massidda, O.1    Novakova, L.2    Vollmer, W.3
  • 67
    • 84855775716 scopus 로고    scopus 로고
    • FtsZ polymers bound to lipid bilayers through ZipA form dynamic two dimensional networks
    • Mateos-Gil P, Marquez I, Lopez-Navajas P, et al. FtsZ polymers bound to lipid bilayers through ZipA form dynamic two dimensional networks. Biochim Biophys Acta 2012;1818:806-13.
    • (2012) Biochim Biophys Acta , vol.1818 , pp. 806-813
    • Mateos-Gil, P.1    Marquez, I.2    Lopez-Navajas, P.3
  • 68
    • 67349175712 scopus 로고    scopus 로고
    • Structural and functional model for ionic (K(+)/Na(+)) and pH dependence of GTPase activity and polymerization of FtsZ, the prokaryotic ortholog of tubulin
    • Mendieta J, Rico AI, Lopez-Vinas E, et al. 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.
    • (2009) J Mol Biol , vol.390 , pp. 17-25
    • Mendieta, J.1    Rico, A.I.2    Lopez-Vinas, E.3
  • 69
    • 77955271619 scopus 로고    scopus 로고
    • Strong FtsZ is with the force: mechanisms to constrict bacteria
    • Mingorance J, Rivas G, Vélez M, et al. Strong FtsZ is with the force: mechanisms to constrict bacteria. Trends Microbiol 2010;18:348-56.
    • (2010) Trends Microbiol , vol.18 , pp. 348-356
    • Mingorance, J.1    Rivas, G.2    Vélez, M.3
  • 70
    • 0034932711 scopus 로고    scopus 로고
    • Escherichia coli FtsZ polymers contain mostly GTP and have a high nucleotide turnover
    • Mingorance J, Rueda S, Gomez-Puertas P, 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    Rueda, S.2    Gomez-Puertas, P.3
  • 71
  • 72
    • 0020651799 scopus 로고
    • Protein degradation in Escherichia coli: the lon gene controls the stability of sulA protein
    • Mizusawa S, Gottesman S. Protein degradation in Escherichia coli: the lon gene controls the stability of sulA protein. P Natl Acad Sci USA 1983;80:358-62.
    • (1983) P Natl Acad Sci USA , vol.80 , pp. 358-362
    • Mizusawa, S.1    Gottesman, S.2
  • 73
    • 72749125802 scopus 로고    scopus 로고
    • The GTPase activity of Escherichia coli FtsZ determines the magnitude of the FtsZ polymer bundling by ZapA in vitro
    • Mohammadi T, Ploeger GE, Verheul J, 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.
    • (2009) Biochemistry , vol.48 , pp. 11056-11066
    • Mohammadi, T.1    Ploeger, G.E.2    Verheul, J.3
  • 74
    • 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, 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.
    • (2000) EMBO J , vol.19 , pp. 3179-3191
    • Mosyak, L.1    Zhang, Y.2    Glasfeld, E.3
  • 75
    • 0034622589 scopus 로고    scopus 로고
    • Solution structure of ZipA, a crucial component of Escherichia coli cell division
    • Moy FJ, Glasfeld E, Mosyak L, et al. Solution structure of ZipA, a crucial component of Escherichia coli cell division. Biochemistry 2000;39:9146-56.
    • (2000) Biochemistry , vol.39 , pp. 9146-9156
    • Moy, F.J.1    Glasfeld, E.2    Mosyak, L.3
  • 76
    • 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;176:2754-8.
    • (1994) J Bacteriol , vol.176 , pp. 2754-2758
    • Mukherjee, A.1    Lutkenhaus, J.2
  • 77
    • 84888864453 scopus 로고    scopus 로고
    • The Escherichia coli divisome: born to divide
    • Natale P, Pazos M, Vicente M. The Escherichia coli divisome: born to divide. Environ Microbiol 2013;15:3169-82.
    • (2013) Environ Microbiol , vol.15 , pp. 3169-3182
    • Natale, P.1    Pazos, M.2    Vicente, M.3
  • 78
    • 0036063886 scopus 로고    scopus 로고
    • Structural evidence that the P/Q domain of ZipA is an unstructured, flexible tether between the membrane and the C-terminal FtsZ-binding domain
    • Ohashi T, Hale CA, de Boer PA, et al. Structural evidence that the P/Q domain of ZipA is an unstructured, flexible tether between the membrane and the C-terminal FtsZ-binding domain. J Bacteriol 2002;184:4313-5.
    • (2002) J Bacteriol , vol.184 , pp. 4313-4315
    • Ohashi, T.1    Hale, C.A.2    de Boer, P.A.3
  • 79
    • 84983120974 scopus 로고    scopus 로고
    • MinC/MinD copolymers are not required for Min function
    • Park KT, Du S, Lutkenhaus J. MinC/MinD copolymers are not required for Min function. Mol Microbiol 2015, doi: 10.1111/mmi.13164.
    • (2015) Mol Microbiol
    • Park, K.T.1    Du, S.2    Lutkenhaus, J.3
  • 80
    • 79961135028 scopus 로고    scopus 로고
    • The Min oscillator uses MinDdependent conformational changes in MinE to spatially regulate cytokinesis
    • Park KT, Wu W, Battaile KP, et al. The Min oscillator uses MinDdependent conformational changes in MinE to spatially regulate cytokinesis. Cell 2011;146:396-407.
    • (2011) Cell , vol.146 , pp. 396-407
    • Park, K.T.1    Wu, W.2    Battaile, K.P.3
  • 81
    • 84898657563 scopus 로고    scopus 로고
    • FtsZ placement in nucleoid-free bacteria
    • Pazos M, Casanova M, Palacios P, et al. FtsZ placement in nucleoid-free bacteria. PLoS One 2014;9:e91984.
    • (2014) PLoS One , vol.9 , pp. e91984
    • Pazos, M.1    Casanova, M.2    Palacios, P.3
  • 82
    • 84888872850 scopus 로고    scopus 로고
    • Interactions among the early Escherichia coli divisome proteins revealed by bimolecular fluorescence complementation
    • Pazos M, Natale P, Margolin W, et al. Interactions among the early Escherichia coli divisome proteins revealed by bimolecular fluorescence complementation. Environ Microbiol 2013;15:3282-91.
    • (2013) Environ Microbiol , vol.15 , pp. 3282-3291
    • Pazos, M.1    Natale, P.2    Margolin, W.3
  • 83
    • 84873286335 scopus 로고    scopus 로고
    • A specific role for the ZipA protein in cell division: stabilization of the FtsZ protein
    • Pazos M, Natale P, Vicente M. A specific role for the ZipA protein in cell division: stabilization of the FtsZ protein. J Biol Chem 2013;288:3219-26.
    • (2013) J Biol Chem , vol.288 , pp. 3219-3226
    • Pazos, M.1    Natale, P.2    Vicente, M.3
  • 84
    • 15744385269 scopus 로고    scopus 로고
    • Tethering the Z ring to the membrane through a conserved membrane targeting sequence in FtsA
    • Pichoff S, Lutkenhaus J. Tethering the Z ring to the membrane through a conserved membrane targeting sequence in FtsA. Mol Microbiol 2005;55:1722-34.
    • (2005) Mol Microbiol , vol.55 , pp. 1722-1734
    • Pichoff, S.1    Lutkenhaus, J.2
  • 85
    • 84890205605 scopus 로고    scopus 로고
    • Discovery of chlamydial peptidoglycan reveals bacteria withmurein sacculi but without FtsZ
    • Pilhofer M, Aistleitner K, Biboy J, et al. Discovery of chlamydial peptidoglycan reveals bacteria withmurein sacculi but without FtsZ. Nat Commun 2013;4:2856.
    • (2013) Nat Commun , vol.4 , pp. 2856
    • Pilhofer, M.1    Aistleitner, K.2    Biboy, J.3
  • 86
    • 0025769943 scopus 로고
    • Preferential cytoplasmic location of FtsZ, a protein essential for Escherichia coli septation
    • Pla J, Sanchez M, Palacios P, et al. Preferential cytoplasmic location of FtsZ, a protein essential for Escherichia coli septation. Mol Microbiol 1991;5:1681-6.
    • (1991) Mol Microbiol , vol.5 , pp. 1681-1686
    • Pla, J.1    Sanchez, M.2    Palacios, P.3
  • 87
    • 67249144043 scopus 로고    scopus 로고
    • FtsZ condensates: an in vitro electron microscopy study
    • Popp D, Iwasa M, Narita A, et al. FtsZ condensates: an in vitro electron microscopy study. Biopolymers 2009;91:340-50.
    • (2009) Biopolymers , vol.91 , pp. 340-350
    • Popp, D.1    Iwasa, M.2    Narita, A.3
  • 88
    • 84868326175 scopus 로고    scopus 로고
    • ZipA is required for FtsZdependent preseptal peptidoglycan synthesis prior to invagination during cell division
    • Potluri LP, Kannan S, Young KD. ZipA is required for FtsZdependent preseptal peptidoglycan synthesis prior to invagination during cell division. J Bacteriol 2012;194: 5334-42.
    • (2012) J Bacteriol , vol.194 , pp. 5334-5342
    • Potluri, L.P.1    Kannan, S.2    Young, K.D.3
  • 89
    • 0033609139 scopus 로고    scopus 로고
    • Rapid pole-to-pole oscillation of a protein required for directing division to the middle of Escherichia coli
    • Raskin DM, de Boer PA. Rapid pole-to-pole oscillation of a protein required for directing division to the middle of Escherichia coli. P Natl Acad Sci USA 1999;96:4971-6.
    • (1999) P Natl Acad Sci USA , vol.96 , pp. 4971-4976
    • Raskin, D.M.1    de Boer, P.A.2
  • 90
    • 0033522467 scopus 로고    scopus 로고
    • ZipA is aMAP-Tau homolog and is essential for structural integrity of the cytokinetic FtsZ ring during bacterial cell division
    • RayChaudhuri D. ZipA is aMAP-Tau homolog and is essential for structural integrity of the cytokinetic FtsZ ring during bacterial cell division. EMBO J 1999;18:2372-83.
    • (1999) EMBO J , vol.18 , pp. 2372-2383
    • RayChaudhuri, D.1
  • 91
    • 0028142491 scopus 로고
    • A point mutation converts Escherichia coli FtsZ septation GTPase to an ATPase
    • RayChaudhuri D, Park JT. A point mutation converts Escherichia coli FtsZ septation GTPase to an ATPase. J Biol Chem 1994;269:22941-4.
    • (1994) J Biol Chem , vol.269 , pp. 22941-22944
    • RayChaudhuri, D.1    Park, J.T.2
  • 92
    • 4444300864 scopus 로고    scopus 로고
    • Role of two essential domains of Escherichia coli FtsA in localization and progression of the division ring
    • Rico AI, Garcia-Ovalle M, Mingorance J, et al. Role of two essential domains of Escherichia coli FtsA in localization and progression of the division ring. Mol Microbiol 2004;53:1359-71.
    • (2004) Mol Microbiol , vol.53 , pp. 1359-1371
    • Rico, A.I.1    Garcia-Ovalle, M.2    Mingorance, J.3
  • 93
    • 84880563030 scopus 로고    scopus 로고
    • In the beginning Escherichia coli assembled a proto-ring: the initial phases of bacterial division
    • Rico AI, Krupka M, Vicente M. In the beginning Escherichia coli assembled a proto-ring: the initial phases of bacterial division. J Biol Chem 2013;288:20830-6.
    • (2013) J Biol Chem , vol.288 , pp. 20830-20836
    • Rico, A.I.1    Krupka, M.2    Vicente, M.3
  • 95
    • 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, 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.
    • (2003) J Bacteriol , vol.185 , pp. 3344-3351
    • Rueda, S.1    Vicente, M.2    Mingorance, J.3
  • 96
    • 0027961077 scopus 로고
    • Correlation between the structure and biochemical activities of FtsA, an essential cell division protein of the actin family
    • Sanchez M, Valencia A, Ferrandiz MJ, et al. Correlation between the structure and biochemical activities of FtsA, an essential cell division protein of the actin family. EMBO J 1994;13: 4919-25.
    • (1994) EMBO J , vol.13 , pp. 4919-4925
    • Sanchez, M.1    Valencia, A.2    Ferrandiz, M.J.3
  • 97
    • 5344269437 scopus 로고    scopus 로고
    • Sculpting the proteome with AAA(+) proteases and disassembly machines
    • Sauer RT, Bolon DN, Burton BM, et al. Sculpting the proteome with AAA(+) proteases and disassembly machines. Cell 2004;119:9-18.
    • (2004) Cell , vol.119 , pp. 9-18
    • Sauer, R.T.1    Bolon, D.N.2    Burton, B.M.3
  • 98
    • 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 DJ, de Wit JG, den Blaauwen T, et al. GTP hydrolysis of cell division protein FtsZ: evidence that the active site is formed by the association of monomers. Biochemistry 2002;41:521-9.
    • (2002) Biochemistry , vol.41 , pp. 521-529
    • Scheffers, D.J.1    de Wit, J.G.2    den Blaauwen, T.3
  • 99
    • 0036268368 scopus 로고    scopus 로고
    • Immediate GTP hydrolysis upon FtsZ polymerization
    • Scheffers DJ, Driessen AJ. Immediate GTP hydrolysis upon FtsZ polymerization. Mol Microbiol 2002;43:1517-21.
    • (2002) Mol Microbiol , vol.43 , pp. 1517-1521
    • Scheffers, D.J.1    Driessen, A.J.2
  • 100
    • 34648819672 scopus 로고    scopus 로고
    • A membrane protein, EzrA, regulates assembly dynamics of FtsZ by interacting with the C-terminal tail of FtsZ
    • Singh JK, Makde RD, Kumar V, et al. A membrane protein, EzrA, regulates assembly dynamics of FtsZ by interacting with the C-terminal tail of FtsZ. Biochemistry 2007;46:11013-22.
    • (2007) Biochemistry , vol.46 , pp. 11013-11022
    • Singh, J.K.1    Makde, R.D.2    Kumar, V.3
  • 101
    • 57649165574 scopus 로고    scopus 로고
    • SepF increases the assembly and bundling of FtsZ polymers and stabilizes FtsZ protofilaments by binding along its length
    • Singh JK, Makde RD, Kumar V, et al. SepF increases the assembly and bundling of FtsZ polymers and stabilizes FtsZ protofilaments by binding along its length. J Biol Chem 2008;283: 31116-24.
    • (2008) J Biol Chem , vol.283 , pp. 31116-31124
    • Singh, J.K.1    Makde, R.D.2    Kumar, V.3
  • 102
    • 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, 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.
    • (2007) J Mol Biol , vol.369 , pp. 210-221
    • Small, E.1    Marrington, R.2    Rodger, A.3
  • 103
    • 84897109056 scopus 로고    scopus 로고
    • Disassembly of the divisome in Escherichia coli: evidence that FtsZ dissociates before compartmentalization
    • Soderstrom B, Skoog K, Blom H, et al. Disassembly of the divisome in Escherichia coli: evidence that FtsZ dissociates before compartmentalization. Mol Microbiol 2014;92:1-9.
    • (2014) Mol Microbiol , vol.92 , pp. 1-9
    • Soderstrom, B.1    Skoog, K.2    Blom, H.3
  • 104
    • 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 ED, et al. Rapid assembly dynamics of the Escherichia coli FtsZ-ring demonstrated by fluorescence recovery after photobleaching. P Natl Acad Sci USA 2002;99:3171-5.
    • (2002) P Natl Acad Sci USA , vol.99 , pp. 3171-3175
    • Stricker, J.1    Maddox, P.2    Salmon, E.D.3
  • 105
    • 84934901914 scopus 로고    scopus 로고
    • The bacterial tubulin FtsZ requires its intrinsically disordered linker to direct robust cell wall construction
    • Sundararajan K, Miguel A, Desmarais SM, et al. The bacterial tubulin FtsZ requires its intrinsically disordered linker to direct robust cell wall construction. Nat Commun 2015;6:7281.
    • (2015) Nat Commun , vol.6 , pp. 7281
    • Sundararajan, K.1    Miguel, A.2    Desmarais, S.M.3
  • 106
    • 0141925615 scopus 로고    scopus 로고
    • The MinD membrane targeting sequence is a transplantable lipid-binding helix
    • Szeto TH, Rowland SL, Habrukowich CL, et al. The MinD membrane targeting sequence is a transplantable lipid-binding helix. J Biol Chem 2003;278:40050-6.
    • (2003) J Biol Chem , vol.278 , pp. 40050-40056
    • Szeto, T.H.1    Rowland, S.L.2    Habrukowich, C.L.3
  • 107
    • 84990997649 scopus 로고    scopus 로고
    • Architecture of the ring formed by the tubulin homologue FtsZ in bacterial cell division
    • Szwedziak P, Wang Q, Bharat TA, et al. Architecture of the ring formed by the tubulin homologue FtsZ in bacterial cell division. Elife 2014;3:e04601.
    • (2014) Elife , vol.3 , pp. e04601
    • Szwedziak, P.1    Wang, Q.2    Bharat, T.A.3
  • 108
    • 84861151969 scopus 로고    scopus 로고
    • FtsA forms actin-like protofilaments
    • Szwedziak P, Wang Q, Freund SM, et al. FtsA forms actin-like protofilaments. EMBO J 2012;31:2249-60.
    • (2012) EMBO J , vol.31 , pp. 2249-2260
    • Szwedziak, P.1    Wang, Q.2    Freund, S.M.3
  • 109
    • 78650910561 scopus 로고    scopus 로고
    • Molecular mechanism by which the nucleoid occlusion factor, SlmA, keeps cytokinesis in check
    • Tonthat NK, Arold ST, Pickering BF, et al. Molecular mechanism by which the nucleoid occlusion factor, SlmA, keeps cytokinesis in check. EMBO J 2011;30:154-64.
    • (2011) EMBO J , vol.30 , pp. 154-164
    • Tonthat, N.K.1    Arold, S.T.2    Pickering, B.F.3
  • 110
    • 84879531614 scopus 로고    scopus 로고
    • SlmA forms a higherorder structure on DNA that inhibits cytokinetic Z-ring formation over the nucleoid
    • Tonthat NK, Milam SL, Chinnam N, et al. SlmA forms a higherorder structure on DNA that inhibits cytokinetic Z-ring formation over the nucleoid. P Natl Acad Sci USA 2013;110:10586-91.
    • (2013) P Natl Acad Sci USA , vol.110 , pp. 10586-10591
    • Tonthat, N.K.1    Milam, S.L.2    Chinnam, N.3
  • 111
    • 84872394561 scopus 로고    scopus 로고
    • PomZ, a ParAlike protein, regulates Z-ring formation and cell division in Myxococcus xanthus
    • Treuner-Lange A, Aguiluz K, van der Does C, et al. PomZ, a ParAlike protein, regulates Z-ring formation and cell division in Myxococcus xanthus. Mol Microbiol 2013;87:235-53.
    • (2013) Mol Microbiol , vol.87 , pp. 235-253
    • Treuner-Lange, A.1    Aguiluz, K.2    van der Does, C.3
  • 112
    • 0031859259 scopus 로고    scopus 로고
    • Bacterial SOS checkpoint protein SulA inhibits polymerization of purified FtsZ cell division protein
    • Trusca D, Scott S, Thompson C, et al. Bacterial SOS checkpoint protein SulA inhibits polymerization of purified FtsZ cell division protein. J Bacteriol 1998;180:3946-53.
    • (1998) J Bacteriol , vol.180 , pp. 3946-3953
    • Trusca, D.1    Scott, S.2    Thompson, C.3
  • 113
    • 0034675921 scopus 로고    scopus 로고
    • Crystal structure of the cell division protein FtsA from Thermotoga maritima
    • van den Ent F, Löwe J. Crystal structure of the cell division protein FtsA from Thermotoga maritima. EMBO J 2000;19:5300-7.
    • (2000) EMBO J , vol.19 , pp. 5300-5307
    • van den Ent, F.1    Löwe, J.2
  • 114
    • 1642462396 scopus 로고    scopus 로고
    • Molecular evolution of FtsZ protein sequences encoded within the genomes of archaea, bacteria, and eukaryota
    • Vaughan S, Wickstead B, Gull K, et al. Molecular evolution of FtsZ protein sequences encoded within the genomes of archaea, bacteria, and eukaryota. J Mol Evol 2004;58:19-29.
    • (2004) J Mol Evol , vol.58 , pp. 19-29
    • Vaughan, S.1    Wickstead, B.2    Gull, K.3
  • 115
    • 42549083859 scopus 로고    scopus 로고
    • How similar cell division genes are located and behave in different bacteria
    • USA: Springer
    • Vicente M, Álvarez J, Martínez-Arteaga R. How similar cell division genes are located and behave in different bacteria. In: Molecules in Time and Space. USA: Springer, 2004.
    • (2004) Molecules in Time and Space
    • Vicente, M.1    Álvarez, J.2    Martínez-Arteaga, R.3
  • 116
    • 0031895073 scopus 로고    scopus 로고
    • Regulation of transcription of cell division genes in the Escherichia coli dcw cluster
    • Vicente M, Gomez MJ, Ayala JA. Regulation of transcription of cell division genes in the Escherichia coli dcw cluster. Cell Mol Life Sci 1998;54:317-24.
    • (1998) Cell Mol Life Sci , vol.54 , pp. 317-324
    • Vicente, M.1    Gomez, M.J.2    Ayala, J.A.3
  • 117
    • 33745209434 scopus 로고    scopus 로고
    • The order of the ring: assembly of Escherichia coli cell division components
    • Vicente M, Rico AI. The order of the ring: assembly of Escherichia coli cell division components. Mol Microbiol 2006;61:5-8.
    • (2006) Mol Microbiol , vol.61 , pp. 5-8
    • Vicente, M.1    Rico, A.I.2
  • 118
    • 0028792495 scopus 로고
    • SOS-regulated proteins in translesion DNA synthesis and mutagenesis
    • Walker GC. SOS-regulated proteins in translesion DNA synthesis and mutagenesis. Trends Biochem Sci 1995;20:416-20.
    • (1995) Trends Biochem Sci , vol.20 , pp. 416-420
    • Walker, G.C.1
  • 119
    • 21244497829 scopus 로고    scopus 로고
    • The ClpX chaperone modulates assembly of the tubulin-like protein FtsZ
    • Weart RB, Nakano S, Lane BE, et al. The ClpX chaperone modulates assembly of the tubulin-like protein FtsZ. Mol Microbiol 2005;57:238-49.
    • (2005) Mol Microbiol , vol.57 , pp. 238-249
    • Weart, R.B.1    Nakano, S.2    Lane, B.E.3
  • 120
    • 78650917468 scopus 로고    scopus 로고
    • Positive control of cell division: FtsZ is recruited by SsgB during sporulation of Streptomyces
    • Willemse J, Borst JW, de Waal E, et al. Positive control of cell division: FtsZ is recruited by SsgB during sporulation of Streptomyces. Gene Dev 2011;25:89-99.
    • (2011) Gene Dev , vol.25 , pp. 89-99
    • Willemse, J.1    Borst, J.W.2    de Waal, E.3
  • 121
    • 0025813235 scopus 로고
    • Toporegulation of bacterial division according to the nucleoid occlusion model
    • Woldringh CL, Mulder E, Huls PG, et al. Toporegulation of bacterial division according to the nucleoid occlusion model. Res Microbiol 1991;142:309-20.
    • (1991) Res Microbiol , vol.142 , pp. 309-320
    • Woldringh, C.L.1    Mulder, E.2    Huls, P.G.3
  • 122
    • 2942752105 scopus 로고    scopus 로고
    • Coordination of cell division and chromosome segregation by a nucleoid occlusion protein in Bacillus subtilis
    • Wu LJ, Errington J. Coordination of cell division and chromosome segregation by a nucleoid occlusion protein in Bacillus subtilis. Cell 2004;117:915-25.
    • (2004) Cell , vol.117 , pp. 915-925
    • Wu, L.J.1    Errington, J.2
  • 123
    • 67650435786 scopus 로고    scopus 로고
    • Noc protein binds to specific DNA sequences to coordinate cell divisionwith chromosome segregation
    • Wu LJ, Ishikawa S, Kawai Y, et al. Noc protein binds to specific DNA sequences to coordinate cell divisionwith chromosome segregation. EMBO J 2009;28:1940-52.
    • (2009) EMBO J , vol.28 , pp. 1940-1952
    • Wu, L.J.1    Ishikawa, S.2    Kawai, Y.3
  • 124
    • 0030815131 scopus 로고    scopus 로고
    • Ca2+-mediated GTP-dependent dynamic assembly of bacterial cell division protein FtsZ into asters and polymer networks in vitro
    • Yu XC, Margolin W. Ca2+-mediated GTP-dependent dynamic assembly of bacterial cell division protein FtsZ into asters and polymer networks in vitro. EMBO J 1997;16: 5455-63.
    • (1997) EMBO J , vol.16 , pp. 5455-5463
    • Yu, X.C.1    Margolin, W.2
  • 125
    • 16844368281 scopus 로고    scopus 로고
    • MinC mutants deficient in MinD- and DicB-mediated cell division inhibition due to loss of interaction with MinD, DicB, or a septal component
    • Zhou H, Lutkenhaus J. MinC mutants deficient in MinD- and DicB-mediated cell division inhibition due to loss of interaction with MinD, DicB, or a septal component. J Bacteriol 2005;187:2846-57.
    • (2005) J Bacteriol , vol.187 , pp. 2846-2857
    • Zhou, H.1    Lutkenhaus, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.