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Volumn 24, Issue 4, 2000, Pages 531-548

Themes and variations in prokaryotic cell division

Author keywords

Bacterium; Binary fission; Cell division; Septation

Indexed keywords

TUBULIN;

EID: 0033823009     PISSN: 01686445     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-6445(00)00038-3     Document Type: Review
Times cited : (271)

References (176)
  • 1
    • 0013895663 scopus 로고
    • The cell wall and cell division of Gram-negative bacteria
    • Steed P., Murray R.G. The cell wall and cell division of Gram-negative bacteria. Can. J. Microbiol. 12:1966;263-270.
    • (1966) Can. J. Microbiol. , vol.12 , pp. 263-270
    • Steed, P.1    Murray, R.G.2
  • 2
    • 0019480394 scopus 로고
    • Constriction and septation during cell division in caulobacters
    • Poindexter J.S., Hagenzieker J.G. Constriction and septation during cell division in caulobacters. Can. J. Microbiol. 27:1981;704-719.
    • (1981) Can. J. Microbiol. , vol.27 , pp. 704-719
    • Poindexter, J.S.1    Hagenzieker, J.G.2
  • 3
    • 0031912354 scopus 로고    scopus 로고
    • Morphogenesis of Escherichia coli
    • Nanninga N. Morphogenesis of Escherichia coli. Microbiol. Mol. Biol. Rev. 62:1998;110-129.
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 110-129
    • Nanninga, N.1
  • 5
    • 0032103029 scopus 로고    scopus 로고
    • A green light for the bacterial cytoskeleton
    • Margolin W. A green light for the bacterial cytoskeleton. Trends Microbiol. 6:1998;233-238.
    • (1998) Trends Microbiol. , vol.6 , pp. 233-238
    • Margolin, W.1
  • 7
    • 0030829601 scopus 로고    scopus 로고
    • FtsZ, a tubulin homologue in prokaryote division
    • Erickson H.P. FtsZ, a tubulin homologue in prokaryote division. Trends Cell Biol. 7:1997;362-367.
    • (1997) Trends Cell Biol. , vol.7 , pp. 362-367
    • Erickson, H.P.1
  • 8
    • 0027184918 scopus 로고
    • FtsZ ring in bacterial cytokinesis
    • Lutkenhaus J. FtsZ ring in bacterial cytokinesis. Mol. Microbiol. 9:1993;403-410.
    • (1993) Mol. Microbiol. , vol.9 , pp. 403-410
    • Lutkenhaus, J.1
  • 10
    • 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. Proc. Natl. Acad. Sci. USA. 81:1984;4490-4494.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 4490-4494
    • Huisman, O.1    D'Ari, R.2    Gottesman, S.3
  • 11
    • 0027513320 scopus 로고
    • Cell division inhibitors SulA and MinCD prevent formation of the FtsZ ring
    • Bi E., Lutkenhaus J. Cell division inhibitors SulA and MinCD prevent formation of the FtsZ ring. J. Bacteriol. 175:1993;1118-1125.
    • (1993) J. Bacteriol. , vol.175 , pp. 1118-1125
    • Bi, E.1    Lutkenhaus, J.2
  • 12
    • 0032539813 scopus 로고    scopus 로고
    • Inhibition of FtsZ polymerization by SulA, an inhibitor of septation in Escherichia coli
    • Mukherjee A., Cao C., Lutkenhaus J. Inhibition of FtsZ polymerization by SulA, an inhibitor of septation in Escherichia coli. Proc. Natl. Acad. Sci. USA. 95:1998;2885-2890.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 2885-2890
    • Mukherjee, A.1    Cao, C.2    Lutkenhaus, J.3
  • 13
    • 0031859259 scopus 로고    scopus 로고
    • Bacterial SOS checkpoint protein SulA inhibits polymerization of purified FtsZ cell division protein
    • Trusca D., Scott S., Thompson C., Bramhill D. Bacterial SOS checkpoint protein SulA inhibits polymerization of purified FtsZ cell division protein. J. Bacteriol. 180:1998;3946-3953.
    • (1998) J. Bacteriol. , vol.180 , pp. 3946-3953
    • Trusca, D.1    Scott, S.2    Thompson, C.3    Bramhill, D.4
  • 14
    • 0031968795 scopus 로고    scopus 로고
    • FtsZ from Escherichia coli, Azotobacter vinelandii, and Thermotoga maritima - quantitation, GTP hydrolysis, and assembly
    • Lu C., Stricker J., Erickson H.P. FtsZ from Escherichia coli, Azotobacter vinelandii, and Thermotoga maritima - quantitation, GTP hydrolysis, and assembly. Cell Motil. Cytoskeleton. 40:1998;71-86.
    • (1998) Cell Motil. Cytoskeleton , vol.40 , pp. 71-86
    • Lu, C.1    Stricker, J.2    Erickson, H.P.3
  • 15
    • 0026059127 scopus 로고
    • FtsZ ring structure associated with division in Escherichia coli
    • Bi E., Lutkenhaus J. FtsZ ring structure associated with division in Escherichia coli. Nature. 354:1991;161-164.
    • (1991) Nature , vol.354 , pp. 161-164
    • Bi, E.1    Lutkenhaus, J.2
  • 16
    • 0029918758 scopus 로고    scopus 로고
    • Transcription factor Spo0A switches the localization of the cell division protein FtsZ from a medial to a bipolar pattern in Bacillus subtilis
    • Levin P.A., Losick R. Transcription factor Spo0A switches the localization of the cell division protein FtsZ from a medial to a bipolar pattern in Bacillus subtilis. Genes Dev. 10:1996;478-488.
    • (1996) Genes Dev. , vol.10 , pp. 478-488
    • Levin, P.A.1    Losick, R.2
  • 17
    • 0029851154 scopus 로고    scopus 로고
    • Colocalization of cell division proteins FtsZ and FtsA to cytoskeletal structures in living Escherichia coli cells by using green fluorescent protein
    • Ma X., Ehrhardt D.W., Margolin W. Colocalization of cell division proteins FtsZ and FtsA to cytoskeletal structures in living Escherichia coli cells by using green fluorescent protein. Proc. Natl. Acad. Sci. USA. 93:1996;12998-13003.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12998-13003
    • Ma, X.1    Ehrhardt, D.W.2    Margolin, W.3
  • 19
    • 0031018531 scopus 로고    scopus 로고
    • Inactivation of FtsIh inhibits constriction of the FtsZ cytokinetic ring and delays the assembly of FtsZ rings at potential division sites
    • Pogliano J., Pogliano K., Weiss D.S., Losick R., Beckwith J. Inactivation of FtsIh inhibits constriction of the FtsZ cytokinetic ring and delays the assembly of FtsZ rings at potential division sites. Proc. Natl. Acad. Sci. USA. 94:1997;559-564.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 559-564
    • Pogliano, J.1    Pogliano, K.2    Weiss, D.S.3    Losick, R.4    Beckwith, J.5
  • 20
    • 0029743706 scopus 로고    scopus 로고
    • FtsZ ring: The eubacterial division apparatus conserved in archaebacteria
    • Wang X., Lutkenhaus J. FtsZ ring: the eubacterial division apparatus conserved in archaebacteria. Mol. Microbiol. 21:1996;313-320.
    • (1996) Mol. Microbiol. , vol.21 , pp. 313-320
    • Wang, X.1    Lutkenhaus, J.2
  • 21
    • 0031924531 scopus 로고    scopus 로고
    • FtsZ dynamics during the cell division cycle of live Escherichia coli
    • Sun Q., Margolin W. FtsZ dynamics during the cell division cycle of live Escherichia coli. J. Bacteriol. 180:1998;2050-2056.
    • (1998) J. Bacteriol. , vol.180 , pp. 2050-2056
    • Sun, Q.1    Margolin, W.2
  • 22
    • 0026705484 scopus 로고
    • The essential bacterial cell-division protein FtsZ is a GTPase
    • de Boer P., Crossley R., Rothfield L. The essential bacterial cell-division protein FtsZ is a GTPase. Nature. 359:1992;254-256.
    • (1992) Nature , vol.359 , pp. 254-256
    • De Boer, P.1    Crossley, R.2    Rothfield, L.3
  • 23
    • 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. 176:1994;2754-2758.
    • (1994) J. Bacteriol. , vol.176 , pp. 2754-2758
    • Mukherjee, A.1    Lutkenhaus, J.2
  • 24
    • 0027500054 scopus 로고
    • Escherichia coli cell division protein FtsZ is a guanine nucleotide binding protein
    • Mukherjee A., Dai K., Lutkenhaus J. Escherichia coli cell division protein FtsZ is a guanine nucleotide binding protein. Proc. Natl. Acad. Sci. USA. 90:1993;1053-1057.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 1053-1057
    • Mukherjee, A.1    Dai, K.2    Lutkenhaus, J.3
  • 25
    • 0026778964 scopus 로고
    • Escherichia coli cell-division gene ftsZ encodes a novel GTP-binding protein
    • Raychaudhuri D., Park J.T. Escherichia coli cell-division gene ftsZ encodes a novel GTP-binding protein. Nature. 359:1992;251-254.
    • (1992) Nature , vol.359 , pp. 251-254
    • Raychaudhuri, D.1    Park, J.T.2
  • 26
    • 2642593025 scopus 로고    scopus 로고
    • Crystal structure of the bacterial cell-division protein FtsZ
    • Löwe J., Amos L.A. Crystal structure of the bacterial cell-division protein FtsZ. Nature. 391:1998;203-206.
    • (1998) Nature , vol.391 , pp. 203-206
    • Löwe, J.1    Amos, L.A.2
  • 27
    • 0030068218 scopus 로고    scopus 로고
    • Bacterial cell division protein FtsZ assembles into protofilament sheets and minirings, structural homologs of tubulin polymers
    • Erickson H.P., Taylor D.W., Taylor K.A., Bramhill D. Bacterial cell division protein FtsZ assembles into protofilament sheets and minirings, structural homologs of tubulin polymers. Proc. Natl. Acad. Sci. USA. 93:1996;519-523.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 519-523
    • Erickson, H.P.1    Taylor, D.W.2    Taylor, K.A.3    Bramhill, D.4
  • 28
    • 0030266954 scopus 로고    scopus 로고
    • Protofilaments and rings, two conformations of the tubulin family conserved from bacterial FtsZ to α, β, and γ tubulin
    • Erickson H.P., Stoffler D. Protofilaments and rings, two conformations of the tubulin family conserved from bacterial FtsZ to α, β, and γ tubulin. J. Cell Biol. 135:1996;5-8.
    • (1996) J. Cell Biol. , vol.135 , pp. 5-8
    • Erickson, H.P.1    Stoffler, D.2
  • 29
    • 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. 16:1997;5455-5463.
    • (1997) EMBO J. , vol.16 , pp. 5455-5463
    • Yu, X.-C.1    Margolin, W.2
  • 30
    • 0028290692 scopus 로고
    • GTP-dependent polymerization of Escherichia coli FtsZ protein to form tubules
    • Bramhill D., Thompson C.M. GTP-dependent polymerization of Escherichia coli FtsZ protein to form tubules. Proc. Natl. Acad. Sci. USA. 91:1994;5813-5817.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 5813-5817
    • Bramhill, D.1    Thompson, C.M.2
  • 31
    • 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. 17:1998;462-469.
    • (1998) EMBO J. , vol.17 , pp. 462-469
    • Mukherjee, A.1    Lutkenhaus, J.2
  • 32
    • 0032562286 scopus 로고    scopus 로고
    • Inhibition of assembly of bacterial cell division protein FtsZ by the hydrophobic dye bis-8-anilino-1-naphthalenesulfonate
    • Yu X.-C., Margolin W. Inhibition of assembly of bacterial cell division protein FtsZ by the hydrophobic dye bis-8-anilino-1-naphthalenesulfonate. J. Biol. Chem. 273:1998;10216-10222.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10216-10222
    • Yu, X.-C.1    Margolin, W.2
  • 33
    • 0032773065 scopus 로고    scopus 로고
    • Vinblastine induces an interaction between FtsZ and tubulin in mammalian cells
    • Yu X., Margolin W., Gonzalez-Garay M.L., Cabral F. Vinblastine induces an interaction between FtsZ and tubulin in mammalian cells. J. Cell Sci. 112:1999;2301-2311.
    • (1999) J. Cell Sci. , vol.112 , pp. 2301-2311
    • Yu, X.1    Margolin, W.2    Gonzalez-Garay, M.L.3    Cabral, F.4
  • 34
    • 0025733254 scopus 로고
    • FtsZ is an essential cell division gene in Escherichia coli
    • Dai K., Lutkenhaus J. ftsZ is an essential cell division gene in Escherichia coli. J. Bacteriol. 173:1991;3500-3506.
    • (1991) J. Bacteriol. , vol.173 , pp. 3500-3506
    • Dai, K.1    Lutkenhaus, J.2
  • 35
    • 0030837787 scopus 로고    scopus 로고
    • Temperature shift experiments with an ftsZ84(Ts) strain reveal rapid dynamics of FtsZ localization and indicate that the Z ring is required throughout septation and cannot reoccupy division sites once constriction has initiated
    • Addinall S.G., Cao C., Lutkenhaus J. Temperature shift experiments with an ftsZ84(Ts) strain reveal rapid dynamics of FtsZ localization and indicate that the Z ring is required throughout septation and cannot reoccupy division sites once constriction has initiated. J. Bacteriol. 179:1997;4277-4284.
    • (1997) J. Bacteriol. , vol.179 , pp. 4277-4284
    • Addinall, S.G.1    Cao, C.2    Lutkenhaus, J.3
  • 36
    • 0025357084 scopus 로고
    • FtsZ regulates the frequency of cell division in Escherichia coli
    • Bi E., Lutkenhaus J. FtsZ regulates the frequency of cell division in Escherichia coli. J. Bacteriol. 172:1990;2765-2768.
    • (1990) J. Bacteriol. , vol.172 , pp. 2765-2768
    • Bi, E.1    Lutkenhaus, J.2
  • 37
    • 0022137060 scopus 로고
    • Overproduction of FtsZ induces minicells in E. coli
    • Ward J.E., Lutkenhaus J. Overproduction of FtsZ induces minicells in E. coli. Cell. 42:1985;941-949.
    • (1985) Cell , vol.42 , pp. 941-949
    • Ward, J.E.1    Lutkenhaus, J.2
  • 38
    • 0028170164 scopus 로고
    • Relationship between ftsZ gene expression and chromosome replication in Escherichia coli
    • Zhou P., Helmstetter C.E. Relationship between ftsZ gene expression and chromosome replication in Escherichia coli. J. Bacteriol. 176:1994;6100-6106.
    • (1994) J. Bacteriol. , vol.176 , pp. 6100-6106
    • Zhou, P.1    Helmstetter, C.E.2
  • 39
    • 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. 181:1999;823-832.
    • (1999) J. Bacteriol. , vol.181 , pp. 823-832
    • Mukherjee, A.1    Lutkenhaus, J.2
  • 40
    • 0031953140 scopus 로고    scopus 로고
    • Cell cycle arrest in Era GTPase mutants: A potential growth rate regulated checkpoint in Escherichia coli
    • Britton R.A., Powell B.S., Dasgupta S., Sun Q., Margolin W., Lupski J.R., Court D.L. Cell cycle arrest in Era GTPase mutants: a potential growth rate regulated checkpoint in Escherichia coli. Mol. Microbiol. 27:1998;739-750.
    • (1998) Mol. Microbiol. , vol.27 , pp. 739-750
    • Britton, R.A.1    Powell, B.S.2    Dasgupta, S.3    Sun, Q.4    Margolin, W.5    Lupski, J.R.6    Court, D.L.7
  • 41
    • 0018823665 scopus 로고
    • Involvement of the ftsA gene product in late stages of the Escherichia coli cell cycle
    • Tormo A., Martinez-Salas E., Vicente M. Involvement of the ftsA gene product in late stages of the Escherichia coli cell cycle. J. Bacteriol. 141:1980;806-813.
    • (1980) J. Bacteriol. , vol.141 , pp. 806-813
    • Tormo, A.1    Martinez-Salas, E.2    Vicente, M.3
  • 43
    • 0026687729 scopus 로고
    • An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins
    • Bork P., Sander C., Valencia A. An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins. Proc. Natl. Acad. Sci. USA. 89:1992;7290-7294.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 7290-7294
    • Bork, P.1    Sander, C.2    Valencia, A.3
  • 44
    • 0030448723 scopus 로고    scopus 로고
    • FtsA is localized to the septum in an FtsZ-dependent manner
    • Addinall S.G., Lutkenhaus J. FtsA is localized to the septum in an FtsZ-dependent manner. J. Bacteriol. 178:1996;7167-7172.
    • (1996) J. Bacteriol. , vol.178 , pp. 7167-7172
    • Addinall, S.G.1    Lutkenhaus, J.2
  • 45
    • 0030681278 scopus 로고    scopus 로고
    • Interactions between heterologous FtsA and FtsZ proteins at the FtsZ ring
    • Ma X., Sun Q., Wang R., Singh G., Jonietz E.L., Margolin W. Interactions between heterologous FtsA and FtsZ proteins at the FtsZ ring. J. Bacteriol. 179:1997;6788-6797.
    • (1997) J. Bacteriol. , vol.179 , pp. 6788-6797
    • Ma, X.1    Sun, Q.2    Wang, R.3    Singh, G.4    Jonietz, E.L.5    Margolin, W.6
  • 46
    • 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 M.-J., Sandler C., Vicente M. Correlation between the structure and biochemical activities of FtsA, an essential cell division protein of the actin family. EMBO J. 13:1994;4919-4925.
    • (1994) EMBO J. , vol.13 , pp. 4919-4925
    • Sanchez, M.1    Valencia, A.2    Ferrandiz, M.-J.3    Sandler, C.4    Vicente, M.5
  • 47
    • 0032786248 scopus 로고    scopus 로고
    • Genetic and functional analysis of the conserved C-terminal core domain of Escherichia coli FtsZ
    • Ma X., Margolin W. Genetic and functional analysis of the conserved C-terminal core domain of Escherichia coli FtsZ. J. Bacteriol. 181:1999;7531-7544.
    • (1999) J. Bacteriol. , vol.181 , pp. 7531-7544
    • Ma, X.1    Margolin, W.2
  • 48
    • 0031780597 scopus 로고    scopus 로고
    • Dominant C-terminal deletions of FtsZ that affect its ability to localize in Caulobacter and its interaction with FtsA
    • Din N., Quardokus E.M., Sackett M.J., Brun Y.V. Dominant C-terminal deletions of FtsZ that affect its ability to localize in Caulobacter and its interaction with FtsA. Mol. Microbiol. 27:1998;1051-1063.
    • (1998) Mol. Microbiol. , vol.27 , pp. 1051-1063
    • Din, N.1    Quardokus, E.M.2    Sackett, M.J.3    Brun, Y.V.4
  • 49
    • 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. 174:1992;6145-6151.
    • (1992) J. Bacteriol. , vol.174 , pp. 6145-6151
    • Dai, K.1    Lutkenhaus, J.2
  • 50
    • 0026738085 scopus 로고
    • Inhibition of cell division initiation by an imbalance in the ratio of FtsA to FtsZ
    • Dewar S.J., Begg K.J., Donachie W.D. Inhibition of cell division initiation by an imbalance in the ratio of FtsA to FtsZ. J. Bacteriol. 174:1992;6314-6316.
    • (1992) J. Bacteriol. , vol.174 , pp. 6314-6316
    • Dewar, S.J.1    Begg, K.J.2    Donachie, W.D.3
  • 51
    • 0030931117 scopus 로고    scopus 로고
    • Analysis of the interaction of FtsZ with itself, GTP, and FtsA
    • Wang X., Huang J., Mukherjee A., Cao C., Lutkenhaus J. Analysis of the interaction of FtsZ with itself, GTP, and FtsA. J. Bacteriol. 179:1997;5551-5559.
    • (1997) J. Bacteriol. , vol.179 , pp. 5551-5559
    • Wang, X.1    Huang, J.2    Mukherjee, A.3    Cao, C.4    Lutkenhaus, J.5
  • 52
    • 0026669489 scopus 로고
    • C-shaped cells caused by expression of an ftsA mutation in Escherichia coli
    • Gayda R.C., Henk M.C., Leong D. C-shaped cells caused by expression of an ftsA mutation in Escherichia coli. J. Bacteriol. 174:1992;5362-5370.
    • (1992) J. Bacteriol. , vol.174 , pp. 5362-5370
    • Gayda, R.C.1    Henk, M.C.2    Leong, D.3
  • 53
    • 0343370794 scopus 로고    scopus 로고
    • unpublished data
    • Margolin, W., unpublished data.
    • Margolin, W.1
  • 54
    • 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 C.A., de Boer P.A. Direct binding of FtsZ to ZipA, an essential component of the septal ring structure that mediates cell division in E. coli. Cell. 88:1997;175-185.
    • (1997) Cell , vol.88 , pp. 175-185
    • Hale, C.A.1    De Boer, P.A.2
  • 55
    • 0032953626 scopus 로고    scopus 로고
    • Recruitment of ZipA to the septal ring of Escherichia coli is dependent on FtsZ and independent of FtsA
    • Hale C.A., de Boer P.A. Recruitment of ZipA to the septal ring of Escherichia coli is dependent on FtsZ and independent of FtsA. J. Bacteriol. 181:1999;167-176.
    • (1999) J. Bacteriol. , vol.181 , pp. 167-176
    • Hale, C.A.1    De Boer, P.A.2
  • 56
    • 0033522467 scopus 로고    scopus 로고
    • ZipA is a MAP-Tau homolog and is essential for structural integrity of the cytokinetic FtsZ ring during bacterial cell division
    • Raychaudhuri D. ZipA is a MAP-Tau homolog and is essential for structural integrity of the cytokinetic FtsZ ring during bacterial cell division. EMBO J. 18:1999;2372-2383.
    • (1999) EMBO J. , vol.18 , pp. 2372-2383
    • Raychaudhuri, D.1
  • 57
    • 0033028421 scopus 로고    scopus 로고
    • Recruitment of ZipA to the division site by interaction with FtsZ
    • Liu Z., Mukherjee A., Lutkenhaus J. Recruitment of ZipA to the division site by interaction with FtsZ. Mol. Microbiol. 31:1999;1853-1861.
    • (1999) Mol. Microbiol. , vol.31 , pp. 1853-1861
    • Liu, Z.1    Mukherjee, A.2    Lutkenhaus, J.3
  • 58
    • 0028034240 scopus 로고
    • Identification of FtsW and characterization of a new ftsW division mutant of Escherichia coli
    • Khattar M.M., Begg K.J., Donachie W.D. Identification of FtsW and characterization of a new ftsW division mutant of Escherichia coli. J. Bacteriol. 176:1994;7140-7147.
    • (1994) J. Bacteriol. , vol.176 , pp. 7140-7147
    • Khattar, M.M.1    Begg, K.J.2    Donachie, W.D.3
  • 59
    • 0028839886 scopus 로고
    • A new Escherichia coli cell division gene, ftsK
    • Begg K.J., Dewar S.J., Donachie W.D. A new Escherichia coli cell division gene, ftsK. J. Bacteriol. 177:1995;6211-6222.
    • (1995) J. Bacteriol. , vol.177 , pp. 6211-6222
    • Begg, K.J.1    Dewar, S.J.2    Donachie, W.D.3
  • 61
    • 0031933996 scopus 로고    scopus 로고
    • Localization of cell division protein FtsK to the Escherichia coli septum and identification of a potential N-terminal targeting domain
    • Yu X.-C., Tran A.H., Sun Q., Margolin W. Localization of cell division protein FtsK to the Escherichia coli septum and identification of a potential N-terminal targeting domain. J. Bacteriol. 180:1998;1296-1304.
    • (1998) J. Bacteriol. , vol.180 , pp. 1296-1304
    • Yu, X.-C.1    Tran, A.H.2    Sun, Q.3    Margolin, W.4
  • 62
    • 0031949032 scopus 로고    scopus 로고
    • FtsK is an essential cell division protein that is localized to the septum and induced as part of the SOS response
    • Wang L., Lutkenhaus J. FtsK is an essential cell division protein that is localized to the septum and induced as part of the SOS response. Mol. Microbiol. 29:1998;731-740.
    • (1998) Mol. Microbiol. , vol.29 , pp. 731-740
    • Wang, L.1    Lutkenhaus, J.2
  • 63
    • 0032453738 scopus 로고    scopus 로고
    • FtsI and FtsW are localized to the septum in Escherichia coli
    • Wang L., Khattar M.K., Donachie W.D., Lutkenhaus J. FtsI and FtsW are localized to the septum in Escherichia coli. J. Bacteriol. 180:1998;2810-2816.
    • (1998) J. Bacteriol. , vol.180 , pp. 2810-2816
    • Wang, L.1    Khattar, M.K.2    Donachie, W.D.3    Lutkenhaus, J.4
  • 66
    • 0031786575 scopus 로고    scopus 로고
    • Role of the C-terminus of FtsK in Escherichia coli chromosome segregation
    • Yu X.C., Weihe E.K., Margolin W. Role of the C-terminus of FtsK in Escherichia coli chromosome segregation. J. Bacteriol. 180:1998;6424-6428.
    • (1998) J. Bacteriol. , vol.180 , pp. 6424-6428
    • Yu, X.C.1    Weihe, E.K.2    Margolin, W.3
  • 67
    • 0031902183 scopus 로고    scopus 로고
    • FtsK is a bifunctional protein involved in cell division and chromosome localization in Escherichia coli
    • Liu G., Draper G.C., Donachie W.D. FtsK is a bifunctional protein involved in cell division and chromosome localization in Escherichia coli. Mol. Microbiol. 29:1998;893-903.
    • (1998) Mol. Microbiol. , vol.29 , pp. 893-903
    • Liu, G.1    Draper, G.C.2    Donachie, W.D.3
  • 68
    • 0029025882 scopus 로고
    • Postseptational chromosome partitioning in bacteria
    • Sharpe M.E., Errington J. Postseptational chromosome partitioning in bacteria. Proc. Natl. Acad. Sci. USA. 92:1995;8630-8634.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8630-8634
    • Sharpe, M.E.1    Errington, J.2
  • 69
    • 0032927732 scopus 로고    scopus 로고
    • The cytoplasmic domain of FtsK protein is required for resolution of chromosome dimers
    • Steiner W., Liu G., Donachie W.D., Kuempel P. The cytoplasmic domain of FtsK protein is required for resolution of chromosome dimers. Mol. Microbiol. 31:1999;579-583.
    • (1999) Mol. Microbiol. , vol.31 , pp. 579-583
    • Steiner, W.1    Liu, G.2    Donachie, W.D.3    Kuempel, P.4
  • 70
    • 0030923499 scopus 로고    scopus 로고
    • A mutation in the ftsK gene of Escherichia coli affects cell-cell separation, stationary-phase survival, stress adaptation, and expression of the gene encoding the stress protein UspA
    • Diez A.A., Farewell A., Nannmark U., Nyström T. A mutation in the ftsK gene of Escherichia coli affects cell-cell separation, stationary-phase survival, stress adaptation, and expression of the gene encoding the stress protein UspA. J. Bacteriol. 179:1997;5878-5883.
    • (1997) J. Bacteriol. , vol.179 , pp. 5878-5883
    • Diez, A.A.1    Farewell, A.2    Nannmark, U.3    Nyström, T.4
  • 71
    • 0032862324 scopus 로고    scopus 로고
    • Synthetic lethal phenotypes caused by mutations affecting chromosome partitioning in Bacillus subtilis
    • Britton R.A., Grossman A.D. Synthetic lethal phenotypes caused by mutations affecting chromosome partitioning in Bacillus subtilis. J. Bacteriol. 181:1999;5860-5864.
    • (1999) J. Bacteriol. , vol.181 , pp. 5860-5864
    • Britton, R.A.1    Grossman, A.D.2
  • 72
    • 0030756250 scopus 로고    scopus 로고
    • Domain-swapping analysis of FtsI, FtsL, and FtsQ, bitopic membrane proteins essential for cell division in Escherichia coli
    • Guzman L.M., Weiss D.S., Beckwith J. Domain-swapping analysis of FtsI, FtsL, and FtsQ, bitopic membrane proteins essential for cell division in Escherichia coli. J. Bacteriol. 179:1997;5094-5103.
    • (1997) J. Bacteriol. , vol.179 , pp. 5094-5103
    • Guzman, L.M.1    Weiss, D.S.2    Beckwith, J.3
  • 73
    • 0029863071 scopus 로고    scopus 로고
    • Topological characterization of the essential Escherichia coli cell division protein FtsN
    • Dai K., Xu Y., Lutkenhaus J. Topological characterization of the essential Escherichia coli cell division protein FtsN. J. Bacteriol. 178:1996;1328-1334.
    • (1996) J. Bacteriol. , vol.178 , pp. 1328-1334
    • Dai, K.1    Xu, Y.2    Lutkenhaus, J.3
  • 74
    • 0027062784 scopus 로고
    • FtsL, an essential cytoplasmic membrane protein involved in cell division in Escherichia coli
    • Guzman L.-M., Barondess J.J., Beckwith J. FtsL, an essential cytoplasmic membrane protein involved in cell division in Escherichia coli. J. Bacteriol. 174:1992;7716-7728.
    • (1992) J. Bacteriol. , vol.174 , pp. 7716-7728
    • Guzman, L.-M.1    Barondess, J.J.2    Beckwith, J.3
  • 75
    • 0030921172 scopus 로고    scopus 로고
    • The bimodular G57-V577 polypeptide chain of the class B penicillin-binding protein 3 of Escherichia coli catalyzes peptide bond formation from thiolesters and does not catalyze glycan chain polymerization from the lipid II intermediate
    • Adam M., Fraipont C., Rhazi N., Nguyen-Disteche M., Lakaye B., Frere J.M., Devreese B., Van Beeumen J., van Heijenoort Y., van Heijenoort J., Ghuysen J.M. The bimodular G57-V577 polypeptide chain of the class B penicillin-binding protein 3 of Escherichia coli catalyzes peptide bond formation from thiolesters and does not catalyze glycan chain polymerization from the lipid II intermediate. J. Bacteriol. 179:1997;6005-6009.
    • (1997) J. Bacteriol. , vol.179 , pp. 6005-6009
    • Adam, M.1    Fraipont, C.2    Rhazi, N.3    Nguyen-Disteche, M.4    Lakaye, B.5    Frere, J.M.6    Devreese, B.7    Van Beeumen, J.8    Van Heijenoort, Y.9    Van Heijenoort, J.10    Ghuysen, J.M.11
  • 76
    • 0032953197 scopus 로고    scopus 로고
    • Septal localization of FtsQ, an essential cell division protein in Escherichia coli
    • Chen J.C., Weiss D.S., Ghigo J.M., Beckwith J. Septal localization of FtsQ, an essential cell division protein in Escherichia coli. J. Bacteriol. 181:1999;521-530.
    • (1999) J. Bacteriol. , vol.181 , pp. 521-530
    • Chen, J.C.1    Weiss, D.S.2    Ghigo, J.M.3    Beckwith, J.4
  • 77
    • 0032932435 scopus 로고    scopus 로고
    • Localization of FtsI (PBP3) to the septal ring requires its membrane anchor, the Z ring, FtsA, FtsQ, and FtsL
    • Weiss D.S., Chen J.C., Ghigo J.M., Boyd D., Beckwith J. Localization of FtsI (PBP3) to the septal ring requires its membrane anchor, the Z ring, FtsA, FtsQ, and FtsL. J. Bacteriol. 181:1999;508-520.
    • (1999) J. Bacteriol. , vol.181 , pp. 508-520
    • Weiss, D.S.1    Chen, J.C.2    Ghigo, J.M.3    Boyd, D.4    Beckwith, J.5
  • 79
    • 0030856502 scopus 로고    scopus 로고
    • FtsN, A late recruit to the septum in Escherichia coli
    • Addinall S.G., Cao C., Lutkenhaus J. FtsN, A late recruit to the septum in Escherichia coli. Mol. Microbiol. 25:1997;303-309.
    • (1997) Mol. Microbiol. , vol.25 , pp. 303-309
    • Addinall, S.G.1    Cao, C.2    Lutkenhaus, J.3
  • 80
    • 0033986953 scopus 로고    scopus 로고
    • Cell division in Escherichia coli: Role of FtsL domains in septal localization, function, and oligomerization
    • Ghigo J.M., Beckwith J. Cell division in Escherichia coli: Role of FtsL domains in septal localization, function, and oligomerization. J. Bacteriol. 182:2000;116-129.
    • (2000) J. Bacteriol. , vol.182 , pp. 116-129
    • Ghigo, J.M.1    Beckwith, J.2
  • 81
    • 0027167446 scopus 로고
    • Cloning and characterization of ftsN, an essential cell division gene in Escherichia coli isolated as a multicopy suppressor of ftsa12(ts)
    • Dai K., Xu Y., Lutkenhaus J. Cloning and characterization of ftsN, an essential cell division gene in Escherichia coli isolated as a multicopy suppressor of ftsa12(ts). J. Bacteriol. 175:1993;3790-3797.
    • (1993) J. Bacteriol. , vol.175 , pp. 3790-3797
    • Dai, K.1    Xu, Y.2    Lutkenhaus, J.3
  • 82
    • 0031595241 scopus 로고    scopus 로고
    • Contribution of the Pmra promoter to expression of genes in the Escherichia coli mra cluster of cell envelope biosynthesis and cell division genes
    • Mengin-Lecreulx D., Ayala J., Bouhss A., van Heijenoort J., Parquet C., Hara H. Contribution of the Pmra promoter to expression of genes in the Escherichia coli mra cluster of cell envelope biosynthesis and cell division genes. J. Bacteriol. 180:1998;4406-4412.
    • (1998) J. Bacteriol. , vol.180 , pp. 4406-4412
    • Mengin-Lecreulx, D.1    Ayala, J.2    Bouhss, A.3    Van Heijenoort, J.4    Parquet, C.5    Hara, H.6
  • 83
    • 0029586501 scopus 로고
    • The envA permeability/cell division gene of Escherichia coli encodes the second enzyme of lipid A biosynthesis. UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase
    • Young K., Silver L.L., Bramhill D., Cameron P., Eveland S.S., Raetz C.R., Hyland S.A., Anderson M.S. The envA permeability/cell division gene of Escherichia coli encodes the second enzyme of lipid A biosynthesis. UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase. J. Biol. Chem. 270:1995;30384-30391.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30384-30391
    • Young, K.1    Silver, L.L.2    Bramhill, D.3    Cameron, P.4    Eveland, S.S.5    Raetz, C.R.6    Hyland, S.A.7    Anderson, M.S.8
  • 84
    • 0031724116 scopus 로고    scopus 로고
    • Cell division genes ftsQAZ in Escherichia coli require distant cis- acting signals upstream of ddlB for full expression
    • Flardh K., Palacios P., Vicente M. Cell division genes ftsQAZ in Escherichia coli require distant cis- acting signals upstream of ddlB for full expression. Mol. Microbiol. 30:1998;305-315.
    • (1998) Mol. Microbiol. , vol.30 , pp. 305-315
    • Flardh, K.1    Palacios, P.2    Vicente, M.3
  • 85
    • 0032924410 scopus 로고    scopus 로고
    • Metabolic alarms and cell division in Escherichia coli
    • Joseleau-Petit D., Vinella D., D'Ari R. Metabolic alarms and cell division in Escherichia coli. J. Bacteriol. 181:1999;9-14.
    • (1999) J. Bacteriol. , vol.181 , pp. 9-14
    • Joseleau-Petit, D.1    Vinella, D.2    D'Ari, R.3
  • 86
    • 0031895073 scopus 로고    scopus 로고
    • Regulation of transcription of cell division genes in the Escherichia coli dcw cluster
    • Vicente M., Gomez M.J., Ayala J.A. Regulation of transcription of cell division genes in the Escherichia coli dcw cluster. Cell Mol. Life Sci. 54:1998;317-324.
    • (1998) Cell Mol. Life Sci. , vol.54 , pp. 317-324
    • Vicente, M.1    Gomez, M.J.2    Ayala, J.A.3
  • 87
    • 0031768070 scopus 로고    scopus 로고
    • Unconventional organization of the division and cell wall gene cluster of Streptococcus pneumoniae
    • Massidda O., Anderluzzi D., Friedli L., Feger G. Unconventional organization of the division and cell wall gene cluster of Streptococcus pneumoniae. Microbiology. 144:1998;3069-3078.
    • (1998) Microbiology , vol.144 , pp. 3069-3078
    • Massidda, O.1    Anderluzzi, D.2    Friedli, L.3    Feger, G.4
  • 88
    • 0032752483 scopus 로고    scopus 로고
    • A new essential gene of the 'minimal genome' affecting cell division
    • Dassain M., Leroy A., Colosetti L., Carol S., Bouché J.P. A new essential gene of the 'minimal genome' affecting cell division. Biochimie. 81:1999;889-895.
    • (1999) Biochimie , vol.81 , pp. 889-895
    • Dassain, M.1    Leroy, A.2    Colosetti, L.3    Carol, S.4    Bouché, J.P.5
  • 89
    • 0024672180 scopus 로고
    • Cellular defects caused by deletion of the Escherichia coli dnaK gene indicate roles for heat shock protein in normal metabolism
    • Bukau B., Walker G.C. Cellular defects caused by deletion of the Escherichia coli dnaK gene indicate roles for heat shock protein in normal metabolism. J. Bacteriol. 171:1989;2337-2346.
    • (1989) J. Bacteriol. , vol.171 , pp. 2337-2346
    • Bukau, B.1    Walker, G.C.2
  • 90
    • 0025003789 scopus 로고
    • Trigger factor depletion or overproduction causes defective cell division but does not block protein export
    • Guthrie B., Wickner W. Trigger factor depletion or overproduction causes defective cell division but does not block protein export. J. Bacteriol. 172:1990;5555-5562.
    • (1990) J. Bacteriol. , vol.172 , pp. 5555-5562
    • Guthrie, B.1    Wickner, W.2
  • 91
    • 0030960946 scopus 로고    scopus 로고
    • Mutational analysis of slyD, an Escherichia coli gene encoding a protein of the FKBP immunophilin family
    • Roof W.D., Fang H.Q., Young K.D., Sun J., Young R. Mutational analysis of slyD, an Escherichia coli gene encoding a protein of the FKBP immunophilin family. Mol. Microbiol. 25:1997;1031-1046.
    • (1997) Mol. Microbiol. , vol.25 , pp. 1031-1046
    • Roof, W.D.1    Fang, H.Q.2    Young, K.D.3    Sun, J.4    Young, R.5
  • 93
    • 0031856847 scopus 로고    scopus 로고
    • Localization and function of cell division proteins in filamentous Escherichia coli cells lacking phosphatidylethanolamine
    • Mileykovskaya E., Sun Q., Margolin W., Dowhan W. Localization and function of cell division proteins in filamentous Escherichia coli cells lacking phosphatidylethanolamine. J. Bacteriol. 180:1998;4252-4257.
    • (1998) J. Bacteriol. , vol.180 , pp. 4252-4257
    • Mileykovskaya, E.1    Sun, Q.2    Margolin, W.3    Dowhan, W.4
  • 95
    • 0030052830 scopus 로고    scopus 로고
    • Determination of cell fate in Bacillus subtilis
    • Errington J. Determination of cell fate in Bacillus subtilis. Trends Genet. 12:1996;31-34.
    • (1996) Trends Genet. , vol.12 , pp. 31-34
    • Errington, J.1
  • 96
    • 0030955552 scopus 로고    scopus 로고
    • Protein localization and cell fate in bacteria
    • Shapiro L., Losick R. Protein localization and cell fate in bacteria. Science. 276:1997;712-718.
    • (1997) Science , vol.276 , pp. 712-718
    • Shapiro, L.1    Losick, R.2
  • 97
    • 0030985487 scopus 로고    scopus 로고
    • The division during bacterial sporulation is symmetrically located in Sporosarcina ureae
    • Zhang L., Higgins M.L., Piggot P.J. The division during bacterial sporulation is symmetrically located in Sporosarcina ureae. Mol. Microbiol. 25:1997;1091-1098.
    • (1997) Mol. Microbiol. , vol.25 , pp. 1091-1098
    • Zhang, L.1    Higgins, M.L.2    Piggot, P.J.3
  • 98
    • 0027257145 scopus 로고
    • The FtsZ protein of Bacillus subtilis is localized at the division site and has GTPase activity that is dependent upon FtsZ concentration
    • Wang X., Lutkenhaus J. The FtsZ protein of Bacillus subtilis is localized at the division site and has GTPase activity that is dependent upon FtsZ concentration. Mol. Microbiol. 9:1993;435-442.
    • (1993) Mol. Microbiol. , vol.9 , pp. 435-442
    • Wang, X.1    Lutkenhaus, J.2
  • 99
    • 0031824694 scopus 로고    scopus 로고
    • Characterization of the essential cell division gene ftsL(yIID) of Bacillus subtilis and its role in the assembly of the division apparatus
    • Daniel R.A., Harry E.J., Katis V.L., Wake R.G., Errington J. Characterization of the essential cell division gene ftsL(yIID) of Bacillus subtilis and its role in the assembly of the division apparatus. Mol. Microbiol. 29:1998;593-604.
    • (1998) Mol. Microbiol. , vol.29 , pp. 593-604
    • Daniel, R.A.1    Harry, E.J.2    Katis, V.L.3    Wake, R.G.4    Errington, J.5
  • 100
    • 0026544880 scopus 로고
    • Impaired cell division and sporulation of a Bacillus subtilis strain with the ftsA gene deleted
    • Beall B., Lutkenhaus J. Impaired cell division and sporulation of a Bacillus subtilis strain with the ftsA gene deleted. J. Bacteriol. 174:1992;2398-2403.
    • (1992) J. Bacteriol. , vol.174 , pp. 2398-2403
    • Beall, B.1    Lutkenhaus, J.2
  • 101
    • 0026035515 scopus 로고
    • FtsZ in Bacillus subtilis is required for vegetative septation and for asymmetric septation during sporulation
    • Beall B., Lutkenhaus J. FtsZ in Bacillus subtilis is required for vegetative septation and for asymmetric septation during sporulation. Genes Dev. 5:1991;447-455.
    • (1991) Genes Dev. , vol.5 , pp. 447-455
    • Beall, B.1    Lutkenhaus, J.2
  • 102
    • 0028142862 scopus 로고
    • Conservation of the 168 divIB gene in Bacillus subtilis W23 and B. licheniformis, and evidence for homology to ftsQ of Escherichia coli
    • Harry E.J., Partridge S.R., Weiss A.S., Wake R.G. Conservation of the 168 divIB gene in Bacillus subtilis W23 and B. licheniformis, and evidence for homology to ftsQ of Escherichia coli. Gene. 147:1994;85-89.
    • (1994) Gene , vol.147 , pp. 85-89
    • Harry, E.J.1    Partridge, S.R.2    Weiss, A.S.3    Wake, R.G.4
  • 103
    • 0030818705 scopus 로고    scopus 로고
    • The membrane-bound cell division protein DivIB is localized to the division site in Bacillus subtilis
    • Harry E.J., Wake R.G. The membrane-bound cell division protein DivIB is localized to the division site in Bacillus subtilis. Mol. Microbiol. 25:1997;275-283.
    • (1997) Mol. Microbiol. , vol.25 , pp. 275-283
    • Harry, E.J.1    Wake, R.G.2
  • 104
    • 0033458802 scopus 로고    scopus 로고
    • An in vivo membrane fusion assay implicates SpoIIIE in the final stages of engulfment during Bacillus subtilis sporulation
    • Sharp M.D., Pogliano K. An in vivo membrane fusion assay implicates SpoIIIE in the final stages of engulfment during Bacillus subtilis sporulation. Proc. Natl. Acad. Sci. USA. 96:1999;14553-14558.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14553-14558
    • Sharp, M.D.1    Pogliano, K.2
  • 105
    • 0030891431 scopus 로고    scopus 로고
    • Septal localization of the SpoIIIE chromosome partitioning protein in Bacillus subtilis
    • Wu L.J., Errington J. Septal localization of the SpoIIIE chromosome partitioning protein in Bacillus subtilis. EMBO J. 16:1997;2161-2169.
    • (1997) EMBO J. , vol.16 , pp. 2161-2169
    • Wu, L.J.1    Errington, J.2
  • 106
    • 0028294868 scopus 로고
    • Characterization of a cell division gene from Bacillus subtilis that is required for vegetative and sporulation septum formation
    • Levin P.A., Losick R. Characterization of a cell division gene from Bacillus subtilis that is required for vegetative and sporulation septum formation. J. Bacteriol. 176:1994;1451-1459.
    • (1994) J. Bacteriol. , vol.176 , pp. 1451-1459
    • Levin, P.A.1    Losick, R.2
  • 107
    • 0030662451 scopus 로고    scopus 로고
    • The Bacillus subtilis division protein DivIC is a highly abundant membrane-bound protein that localizes to the division site
    • Katis V.L., Harry E.J., Wake R.G. The Bacillus subtilis division protein DivIC is a highly abundant membrane-bound protein that localizes to the division site. Mol. Microbiol. 26:1997;1047-1055.
    • (1997) Mol. Microbiol. , vol.26 , pp. 1047-1055
    • Katis, V.L.1    Harry, E.J.2    Wake, R.G.3
  • 108
    • 0032953633 scopus 로고    scopus 로고
    • Membrane-bound division proteins DivIB and DivIC of Bacillus subtilis function solely through their external domains in both vegetative and sporulation division
    • Katis V.L., Wake R.G. Membrane-bound division proteins DivIB and DivIC of Bacillus subtilis function solely through their external domains in both vegetative and sporulation division. J. Bacteriol. 181:1999;2710-2718.
    • (1999) J. Bacteriol. , vol.181 , pp. 2710-2718
    • Katis, V.L.1    Wake, R.G.2
  • 110
    • 0030011228 scopus 로고    scopus 로고
    • Cell cycle regulation and cell type-specific localization of the FtsZ division initiation protein in Caulobacter
    • Quardokus E., Din N., Brun Y.V. Cell cycle regulation and cell type-specific localization of the FtsZ division initiation protein in Caulobacter. Proc. Natl. Acad. Sci. USA. 93:1996;6314-6319.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6314-6319
    • Quardokus, E.1    Din, N.2    Brun, Y.V.3
  • 111
    • 0032521234 scopus 로고    scopus 로고
    • Cell cycle dependent transcriptional and proteolytic regulation of FtsZ in Caulobacter
    • Kelly A.J., Sackett M., Din N., Quardokus E., Brun Y.V. Cell cycle dependent transcriptional and proteolytic regulation of FtsZ in Caulobacter. Genes Dev. 12:1998;880-893.
    • (1998) Genes Dev. , vol.12 , pp. 880-893
    • Kelly, A.J.1    Sackett, M.2    Din, N.3    Quardokus, E.4    Brun, Y.V.5
  • 112
    • 0031959650 scopus 로고    scopus 로고
    • Ordered expression of ftsQA and ftsZ during the Caulobacter crescentus cell cycle
    • Sackett M.J., Kelly A.J., Brun Y.V. Ordered expression of ftsQA and ftsZ during the Caulobacter crescentus cell cycle. Mol. Microbiol. 28:1998;421-434.
    • (1998) Mol. Microbiol. , vol.28 , pp. 421-434
    • Sackett, M.J.1    Kelly, A.J.2    Brun, Y.V.3
  • 113
    • 0015061858 scopus 로고
    • Procaryotic cell division with respect to wall and membranes
    • Higgins M.L., Shockman G.D. Procaryotic cell division with respect to wall and membranes. CRC Crit. Rev. Microbiol. 1:1971;29-72.
    • (1971) CRC Crit. Rev. Microbiol. , vol.1 , pp. 29-72
    • Higgins, M.L.1    Shockman, G.D.2
  • 114
    • 0025810776 scopus 로고
    • Salt-mediated multicell formation in Deinococcus radiodurans
    • Chou F.I., Tan S.T. Salt-mediated multicell formation in Deinococcus radiodurans. J. Bacteriol. 173:1991;3184-3190.
    • (1991) J. Bacteriol. , vol.173 , pp. 3184-3190
    • Chou, F.I.1    Tan, S.T.2
  • 115
    • 0021061626 scopus 로고
    • Cell division in Deinococcus radiodurans and a method for displaying septa
    • Murray R.G., Hall M., Thompson B.G. Cell division in Deinococcus radiodurans and a method for displaying septa. Can. J. Microbiol. 29:1983;1412-1423.
    • (1983) Can. J. Microbiol. , vol.29 , pp. 1412-1423
    • Murray, R.G.1    Hall, M.2    Thompson, B.G.3
  • 117
    • 0030995309 scopus 로고    scopus 로고
    • Isolation and characterization of autolysin-defective mutants of Staphylococcus aureus that form cell packets
    • Kaneda S. Isolation and characterization of autolysin-defective mutants of Staphylococcus aureus that form cell packets. Curr. Microbiol. 34:1997;354-359.
    • (1997) Curr. Microbiol. , vol.34 , pp. 354-359
    • Kaneda, S.1
  • 118
    • 0031977950 scopus 로고    scopus 로고
    • Division planes alternate in spherical cells of Escherichia coli
    • Begg K.J., Donachie W.D. Division planes alternate in spherical cells of Escherichia coli. J. Bacteriol. 180:1998;2564-2567.
    • (1998) J. Bacteriol. , vol.180 , pp. 2564-2567
    • Begg, K.J.1    Donachie, W.D.2
  • 119
    • 0007097379 scopus 로고    scopus 로고
    • The chlamydial developmental cycle
    • (Brun, Y. and Shimkets, L., Eds.), American Society for Microbiology, Washington, DC
    • Rockey, D.D. and Matsmoto, A. (2000) The chlamydial developmental cycle, In: Prokaryotic Development (Brun, Y. and Shimkets, L., Eds.), pp. 403-426. American Society for Microbiology, Washington, DC.
    • (2000) In: Prokaryotic Development , pp. 403-426
    • Rockey, D.D.1    Matsmoto, A.2
  • 120
    • 0032977966 scopus 로고    scopus 로고
    • Chlamydia infection of epithelial cells expressing dynamin and Eps15 mutants: Clathrin-independent entry into cells and dynamin-dependent productive growth
    • Boleti H., Benmerah A., Ojcius D.M., Cerf-Bensussan N., Dautry-Varsat A. Chlamydia infection of epithelial cells expressing dynamin and Eps15 mutants: clathrin-independent entry into cells and dynamin-dependent productive growth. J. Cell Sci. 112:1999;1487-1496.
    • (1999) J. Cell Sci. , vol.112 , pp. 1487-1496
    • Boleti, H.1    Benmerah, A.2    Ojcius, D.M.3    Cerf-Bensussan, N.4    Dautry-Varsat, A.5
  • 121
    • 0033959142 scopus 로고    scopus 로고
    • Identification of an antigen localized to an apparent septum within dividing chlamydiae
    • Brown W.J., Rockey D.D. Identification of an antigen localized to an apparent septum within dividing chlamydiae. Infect. Immun. 68:2000;708-715.
    • (2000) Infect. Immun. , vol.68 , pp. 708-715
    • Brown, W.J.1    Rockey, D.D.2
  • 122
    • 0033057626 scopus 로고    scopus 로고
    • Mycoplasma pneumoniae protein P30 is required for cytadherence and associated with proper cell development
    • Romero-Arroyo C.E., Jordan J., Peacock S.J., Willby M.J., Farmer M.A., Krause D.C. Mycoplasma pneumoniae protein P30 is required for cytadherence and associated with proper cell development. J. Bacteriol. 181:1999;1079-1087.
    • (1999) J. Bacteriol. , vol.181 , pp. 1079-1087
    • Romero-Arroyo, C.E.1    Jordan, J.2    Peacock, S.J.3    Willby, M.J.4    Farmer, M.A.5    Krause, D.C.6
  • 123
    • 0032749689 scopus 로고    scopus 로고
    • Cell reproduction cycle of mycoplasma
    • Miyata M., Seto S. Cell reproduction cycle of mycoplasma. Biochimie. 81:1999;873-878.
    • (1999) Biochimie , vol.81 , pp. 873-878
    • Miyata, M.1    Seto, S.2
  • 124
    • 0023102281 scopus 로고
    • Morphology, growth and reversion in a stable L-form of Escherichia coli K12
    • Onoda T., Oshima A., Nakano S., Matsuno A. Morphology, growth and reversion in a stable L-form of Escherichia coli K12. J. Gen. Microbiol. 133:1987;527-534.
    • (1987) J. Gen. Microbiol. , vol.133 , pp. 527-534
    • Onoda, T.1    Oshima, A.2    Nakano, S.3    Matsuno, A.4
  • 125
    • 0032510454 scopus 로고    scopus 로고
    • Archaeal genomics: Do archaea have a mixed heritage?
    • Doolittle W.F., Logsdon J.M. Jr. Archaeal genomics: do archaea have a mixed heritage? Curr. Biol. 8:1998;209-211.
    • (1998) Curr. Biol. , vol.8 , pp. 209-211
    • Doolittle, W.F.1    Logsdon J.M., Jr.2
  • 126
    • 0029864056 scopus 로고    scopus 로고
    • Isolation of an ftsZ homolog from the archaebacterium Halobacterium salinarium: Implications for the evolution of FtsZ and tubulin
    • Margolin W., Wang R., Kumar M. Isolation of an ftsZ homolog from the archaebacterium Halobacterium salinarium: implications for the evolution of FtsZ and tubulin. J. Bacteriol. 178:1996;1320-1327.
    • (1996) J. Bacteriol. , vol.178 , pp. 1320-1327
    • Margolin, W.1    Wang, R.2    Kumar, M.3
  • 127
    • 0030006337 scopus 로고    scopus 로고
    • An archaebacterial homologue of the essential eubacterial cell division protein FtsZ
    • Baumann P., Jackson S.P. An archaebacterial homologue of the essential eubacterial cell division protein FtsZ. Proc. Natl. Acad. Sci. USA. 93:1996;6726-6730.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6726-6730
    • Baumann, P.1    Jackson, S.P.2
  • 128
    • 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. 8:1998;338-341.
    • (1998) Curr. Biol. , vol.8 , pp. 338-341
    • Faguy, D.M.1    Doolittle, W.F.2
  • 129
    • 0028209091 scopus 로고
    • Rhizobium meliloti contains a novel second copy of the cell division gene ftsZ
    • Margolin W., Long S.R. Rhizobium meliloti contains a novel second copy of the cell division gene ftsZ. J. Bacteriol. 176:1994;2033-2043.
    • (1994) J. Bacteriol. , vol.176 , pp. 2033-2043
    • Margolin, W.1    Long, S.R.2
  • 130
    • 0033517997 scopus 로고    scopus 로고
    • Lessons from the Aeropyrum pernix genome
    • Faguy D., Doolittle W.F. Lessons from the Aeropyrum pernix genome. Curr. Biol. 9:1999;883-886.
    • (1999) Curr. Biol. , vol.9 , pp. 883-886
    • Faguy, D.1    Doolittle, W.F.2
  • 131
    • 0031844818 scopus 로고    scopus 로고
    • Archaea and the cell cycle
    • Bernander R. Archaea and the cell cycle. Mol. Microbiol. 29:1998;955-961.
    • (1998) Mol. Microbiol. , vol.29 , pp. 955-961
    • Bernander, R.1
  • 132
    • 0033367329 scopus 로고    scopus 로고
    • Mitochondrial genome evolution and the origin of eukaryotes
    • Lang B.F., Gray M.W., Burger G. Mitochondrial genome evolution and the origin of eukaryotes. Annu Rev. Genet. 33:1999;351-397.
    • (1999) Annu Rev. Genet. , vol.33 , pp. 351-397
    • Lang, B.F.1    Gray, M.W.2    Burger, G.3
  • 133
    • 0032572804 scopus 로고    scopus 로고
    • Organelle division: From coli to chloroplasts
    • Lutkenhaus J. Organelle division: from coli to chloroplasts. Curr. Biol. 8:1998;619-621.
    • (1998) Curr. Biol. , vol.8 , pp. 619-621
    • Lutkenhaus, J.1
  • 134
    • 0032287069 scopus 로고    scopus 로고
    • Chloroplast division in higher plants requires members of two functionally divergent gene families with homology to bacterial FtsZ
    • Osteryoung K.W., Stokes K.D., Rutherford S.M., Percival A.L., Lee W.Y. Chloroplast division in higher plants requires members of two functionally divergent gene families with homology to bacterial FtsZ. Plant Cell. 10:1998;1991-2004.
    • (1998) Plant Cell , vol.10 , pp. 1991-2004
    • Osteryoung, K.W.1    Stokes, K.D.2    Rutherford, S.M.3    Percival, A.L.4    Lee, W.Y.5
  • 135
    • 0032516067 scopus 로고    scopus 로고
    • Plant nuclear gene knockout reveals a role in plastid division for the homolog of the bacterial cell division protein FtsZ, an ancestral tubulin
    • Strepp R., Scholz S., Kruse S., Speth V., Reski R. Plant nuclear gene knockout reveals a role in plastid division for the homolog of the bacterial cell division protein FtsZ, an ancestral tubulin. Proc. Natl. Acad. Sci. USA. 95:1998;4368-4373.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 4368-4373
    • Strepp, R.1    Scholz, S.2    Kruse, S.3    Speth, V.4    Reski, R.5
  • 139
    • 0032895234 scopus 로고    scopus 로고
    • FtsZ ring clusters in min and partition mutants: Role of both the Min system and the nucleoid in regulating FtsZ ring localization
    • Yu X.-C., Margolin W. FtsZ ring clusters in min and partition mutants: Role of both the Min system and the nucleoid in regulating FtsZ ring localization. Mol. Microbiol. 32:1999;315-326.
    • (1999) Mol. Microbiol. , vol.32 , pp. 315-326
    • Yu, X.-C.1    Margolin, W.2
  • 140
    • 0023876706 scopus 로고
    • Isolation and properties of minB, a complex genetic locus involved in correct placement of the division site in Escherichia coli
    • de Boer P.A., Crossley R.E., Rothfield L.I. Isolation and properties of minB, a complex genetic locus involved in correct placement of the division site in Escherichia coli. J. Bacteriol. 170:1988;2106-2112.
    • (1988) J. Bacteriol. , vol.170 , pp. 2106-2112
    • De Boer, P.A.1    Crossley, R.E.2    Rothfield, L.I.3
  • 141
    • 0024977391 scopus 로고
    • A division inhibitor and a topological specificity factor coded for by the minicell locus determine the proper placement of the division site in Escherichia coli
    • de Boer P.A.J., Crossley R.E., Rothfield L.I. A division inhibitor and a topological specificity factor coded for by the minicell locus determine the proper placement of the division site in Escherichia coli. Cell. 56:1989;641-649.
    • (1989) Cell , vol.56 , pp. 641-649
    • De Boer, P.A.J.1    Crossley, R.E.2    Rothfield, L.I.3
  • 142
    • 0033060058 scopus 로고    scopus 로고
    • Bacterial cell division: A moveable feast
    • Jacobs C., Shapiro L. Bacterial cell division: a moveable feast. Proc. Natl. Acad. Sci. USA. 96:1999;5891-5893.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 5891-5893
    • Jacobs, C.1    Shapiro, L.2
  • 143
    • 0030780085 scopus 로고    scopus 로고
    • The MinE ring: An FtsZ-independent cell structure required for selection of the correct division site in E. coli
    • Raskin D.M., deBoer P.A.J. The MinE ring: an FtsZ-independent cell structure required for selection of the correct division site in E. coli. Cell. 91:1997;685-694.
    • (1997) Cell , vol.91 , pp. 685-694
    • Raskin, D.M.1    Deboer, P.A.J.2
  • 144
    • 0020054652 scopus 로고
    • On the precision and accuracy achieved by Escherichia coli cells at fission about their middle
    • Trueba F.J. On the precision and accuracy achieved by Escherichia coli cells at fission about their middle. Arch. Microbiol. 131:1982;55-59.
    • (1982) Arch. Microbiol. , vol.131 , pp. 55-59
    • Trueba, F.J.1
  • 145
    • 0033609139 scopus 로고    scopus 로고
    • Rapid pole-to-pole oscillation of a protein required for directing division to the middle of Escherichia coli
    • Raskin D.M., de Boer P.A. Rapid pole-to-pole oscillation of a protein required for directing division to the middle of Escherichia coli. Proc. Natl. Acad. Sci. USA. 96:1999;4971-4976.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4971-4976
    • Raskin, D.M.1    De Boer, P.A.2
  • 146
    • 0032743092 scopus 로고    scopus 로고
    • MinDE-dependent pole-to-pole oscillation of division inhibitor MinC in Escherichia coli
    • Raskin D.M., de Boer P.A. MinDE-dependent pole-to-pole oscillation of division inhibitor MinC in Escherichia coli. J. Bacteriol. 181:1999;6419-6424.
    • (1999) J. Bacteriol. , vol.181 , pp. 6419-6424
    • Raskin, D.M.1    De Boer, P.A.2
  • 147
    • 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., Lutkenhaus J. The MinC component of the division site selection system in Escherichia coli interacts with FtsZ to prevent polymerization. Proc. Natl. Acad. Sci. USA. 96:1999;14819-14824.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14819-14824
    • Hu, Z.1    Mukherjee, A.2    Pichoff, S.3    Lutkenhaus, J.4
  • 148
    • 0024044911 scopus 로고
    • Minicell-forming mutants of Escherichia coli: Production of minicells and anucleate rods
    • Jaffé A., D'Ari R., Hiraga S. Minicell-forming mutants of Escherichia coli: production of minicells and anucleate rods. J. Bacteriol. 170:1988;3094-3101.
    • (1988) J. Bacteriol. , vol.170 , pp. 3094-3101
    • Jaffé, A.1    D'Ari, R.2    Hiraga, S.3
  • 150
    • 0033231557 scopus 로고    scopus 로고
    • Control of development by altered localization of a transcription factor in B. subtilis
    • Quisel J.D., Lin D.C.-H., Grossman A.D. Control of development by altered localization of a transcription factor in B. subtilis. Mol. Cell. 4:1999;665-672.
    • (1999) Mol. Cell , vol.4 , pp. 665-672
    • Quisel, J.D.1    Lin, D.C.-H.2    Grossman, A.D.3
  • 151
    • 0033231585 scopus 로고    scopus 로고
    • Dynamic movement of the ParA-like Soj protein of B. subtilis and its dual role in nucleoid organization and developmental regulation
    • Marston A.L., Errington J. Dynamic movement of the ParA-like Soj protein of B. subtilis and its dual role in nucleoid organization and developmental regulation. Mol. Cell. 4:1999;673-682.
    • (1999) Mol. Cell , vol.4 , pp. 673-682
    • Marston, A.L.1    Errington, J.2
  • 152
    • 0026768828 scopus 로고
    • Identification of Bacillus subtilis genes for septum placement and shape determination
    • Levin P.A., Margolis P.S., Setlow P., Losick R., Sun D. Identification of Bacillus subtilis genes for septum placement and shape determination. J. Bacteriol. 174:1992;6717.
    • (1992) J. Bacteriol. , vol.174 , pp. 6717
    • Levin, P.A.1    Margolis, P.S.2    Setlow, P.3    Losick, R.4    Sun, D.5
  • 153
    • 0032973292 scopus 로고    scopus 로고
    • Selection of the midcell division site in Bacillus subtilis through MinD-dependent polar localization and activation of MinC
    • Marston A.L., Errington J. Selection of the midcell division site in Bacillus subtilis through MinD-dependent polar localization and activation of MinC. Mol. Microbiol. 33:1999;84-96.
    • (1999) Mol. Microbiol. , vol.33 , pp. 84-96
    • Marston, A.L.1    Errington, J.2
  • 154
    • 0030876575 scopus 로고    scopus 로고
    • The Bacillus subtilis DivIVA protein targets to the division septum and controls the site specificity of cell division
    • Edwards D.H., Errington J. The Bacillus subtilis DivIVA protein targets to the division septum and controls the site specificity of cell division. Mol. Microbiol. 24:1997;905-915.
    • (1997) Mol. Microbiol. , vol.24 , pp. 905-915
    • Edwards, D.H.1    Errington, J.2
  • 155
    • 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 A.L., Thomaides H.B., Edwards D.H., Sharpe M.E., Errington J. Polar localization of the MinD protein of Bacillus subtilis and its role in selection of the mid-cell division site. Genes Dev. 12:1998;3419-3430.
    • (1998) Genes Dev. , vol.12 , pp. 3419-3430
    • Marston, A.L.1    Thomaides, H.B.2    Edwards, D.H.3    Sharpe, M.E.4    Errington, J.5
  • 156
    • 0031765193 scopus 로고    scopus 로고
    • Effect of minCD on FtsZ ring position and polar septation in Bacillus subtilis
    • Levin P.A., Shim J.J., Grossman A.D. Effect of minCD on FtsZ ring position and polar septation in Bacillus subtilis. J. Bacteriol. 180:1998;6048-6051.
    • (1998) J. Bacteriol. , vol.180 , pp. 6048-6051
    • Levin, P.A.1    Shim, J.J.2    Grossman, A.D.3
  • 157
    • 0033578438 scopus 로고    scopus 로고
    • Identification and characterization of a negative regulator of FtsZ ring formation in Bacillus subtilis
    • Levin P.A., Kurtser I.G., Grossman A.D. Identification and characterization of a negative regulator of FtsZ ring formation in Bacillus subtilis. Proc. Natl. Acad. Sci. USA. 96:1999;9642-9647.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 9642-9647
    • Levin, P.A.1    Kurtser, I.G.2    Grossman, A.D.3
  • 158
    • 0344653593 scopus 로고    scopus 로고
    • Isolation of a minD-like gene in the hyperthermophilic archaeon Pyrococcus AL585, and phylogenetic characterization of related proteins in the three domains of life
    • Gérard E., Labedan B., Forterre P. Isolation of a minD-like gene in the hyperthermophilic archaeon Pyrococcus AL585, and phylogenetic characterization of related proteins in the three domains of life. Gene. 222:1998;99-106.
    • (1998) Gene , vol.222 , pp. 99-106
    • Gérard, E.1    Labedan, B.2    Forterre, P.3
  • 159
    • 0033056682 scopus 로고    scopus 로고
    • Nucleoid-independent identification of cell division sites in Escherichia coli
    • Cook W.R., Rothfield L.I. Nucleoid-independent identification of cell division sites in Escherichia coli. J. Bacteriol. 181:1999;1900-1905.
    • (1999) J. Bacteriol. , vol.181 , pp. 1900-1905
    • Cook, W.R.1    Rothfield, L.I.2
  • 160
    • 0026069582 scopus 로고
    • The new gene mukB codes for a 177-kDa protein with coiled-coil domains involved in chromosome partitioning of Escherichia coli
    • Niki H., Jaffé A., Imamura R., Ogura T., Hiraga S. The new gene mukB codes for a 177-kDa protein with coiled-coil domains involved in chromosome partitioning of Escherichia coli. EMBO J. 10:1991;183-194.
    • (1991) EMBO J. , vol.10 , pp. 183-194
    • Niki, H.1    Jaffé, A.2    Imamura, R.3    Ogura, T.4    Hiraga, S.5
  • 161
    • 0031850025 scopus 로고    scopus 로고
    • Assembly of the FtsZ ring at the central division site in the absence of the chromosome
    • Sun Q., Yu X.-C., Margolin W. Assembly of the FtsZ ring at the central division site in the absence of the chromosome. Mol. Microbiol. 29:1998;491-504.
    • (1998) Mol. Microbiol. , vol.29 , pp. 491-504
    • Sun, Q.1    Yu, X.-C.2    Margolin, W.3
  • 162
    • 0025813235 scopus 로고
    • Toporegulation of bacterial division according to the nucleoid occlusion model
    • Woldringh C.L., Mulder E., Huls P.G., Vischer N. Toporegulation of bacterial division according to the nucleoid occlusion model. Res. Microbiol. 142:1991;309-320.
    • (1991) Res. Microbiol. , vol.142 , pp. 309-320
    • Woldringh, C.L.1    Mulder, E.2    Huls, P.G.3    Vischer, N.4
  • 164
    • 0031991771 scopus 로고    scopus 로고
    • Cell cycle-dependent duplication and bidirectional migration of SeqA-associated DNA-protein complexes in E. coli
    • Hiraga S., Ichinose C., Niki H., Yamazoe M. Cell cycle-dependent duplication and bidirectional migration of SeqA-associated DNA-protein complexes in E. coli. Mol. Cell. 1:1998;381-387.
    • (1998) Mol. Cell , vol.1 , pp. 381-387
    • Hiraga, S.1    Ichinose, C.2    Niki, H.3    Yamazoe, M.4
  • 165
    • 0032553470 scopus 로고    scopus 로고
    • Localization of bacterial DNA polymerase: Evidence for a factory model of replication
    • Lemon K.P., Grossman A.D. Localization of bacterial DNA polymerase: evidence for a factory model of replication. Science. 282:1998;1516-1519.
    • (1998) Science , vol.282 , pp. 1516-1519
    • Lemon, K.P.1    Grossman, A.D.2
  • 166
    • 0033011423 scopus 로고    scopus 로고
    • Co-ordinating DNA replication with cell division in bacteria: A link between the early stages of a round of replication and mid-cell Z ring assembly
    • Harry E.J., Rodwell J., Wake R.G. Co-ordinating DNA replication with cell division in bacteria: a link between the early stages of a round of replication and mid-cell Z ring assembly. Mol. Microbiol. 33:1999;33-40.
    • (1999) Mol. Microbiol. , vol.33 , pp. 33-40
    • Harry, E.J.1    Rodwell, J.2    Wake, R.G.3
  • 167
    • 0027406492 scopus 로고
    • Axial filament formation in Bacillus subtilis: Induction of nucleoids of increasing length after addition of chloramphenicol to exponential-phase cultures approaching stationary phase
    • Bylund J.E., Haines M.A., Piggot P.J., Higgins M.L. Axial filament formation in Bacillus subtilis: induction of nucleoids of increasing length after addition of chloramphenicol to exponential-phase cultures approaching stationary phase. J. Bacteriol. 175:1993;1886-1890.
    • (1993) J. Bacteriol. , vol.175 , pp. 1886-1890
    • Bylund, J.E.1    Haines, M.A.2    Piggot, P.J.3    Higgins, M.L.4
  • 168
    • 0030664213 scopus 로고    scopus 로고
    • Requirement of topoisomerase IV parC and parE genes for cell cycle progression and developmental regulation in Caulobacter crescentus
    • Ward D., Newton A. Requirement of topoisomerase IV parC and parE genes for cell cycle progression and developmental regulation in Caulobacter crescentus. Mol. Microbiol. 26:1997;897-910.
    • (1997) Mol. Microbiol. , vol.26 , pp. 897-910
    • Ward, D.1    Newton, A.2
  • 169
    • 0032733107 scopus 로고    scopus 로고
    • Chromosome segregation during the prokaryotic division cycle
    • Jensen R.B., Shapiro L. Chromosome segregation during the prokaryotic division cycle. Curr. Opin. Cell Biol. 11:1999;726-731.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 726-731
    • Jensen, R.B.1    Shapiro, L.2
  • 170
    • 0030946611 scopus 로고    scopus 로고
    • Generation of buds, swellings, and branches instead of filaments after blocking the cell cycle of Rhizobium meliloti
    • Latch J.N., Margolin W. Generation of buds, swellings, and branches instead of filaments after blocking the cell cycle of Rhizobium meliloti. J. Bacteriol. 179:1997;2373-2381.
    • (1997) J. Bacteriol. , vol.179 , pp. 2373-2381
    • Latch, J.N.1    Margolin, W.2
  • 171
    • 0030931867 scopus 로고    scopus 로고
    • The CcrM DNA methyltransferase is widespread in the alpha subdivision of proteobacteria, and its essential functions are conserved in Rhizobium meliloti and Caulobacter crescentus
    • Wright R., Stephens C., Shapiro L. The CcrM DNA methyltransferase is widespread in the alpha subdivision of proteobacteria, and its essential functions are conserved in Rhizobium meliloti and Caulobacter crescentus. J. Bacteriol. 179:1997;5869-5877.
    • (1997) J. Bacteriol. , vol.179 , pp. 5869-5877
    • Wright, R.1    Stephens, C.2    Shapiro, L.3
  • 172
    • 0032747168 scopus 로고    scopus 로고
    • On the origin of branches in Escherichia coli
    • Gullbrand B., Åkerlund T., Nordström K. On the origin of branches in Escherichia coli. J. Bacteriol. 181:1999;6607-6614.
    • (1999) J. Bacteriol. , vol.181 , pp. 6607-6614
    • Gullbrand, B.1    Åkerlund, T.2    Nordström, K.3
  • 173
    • 0025247055 scopus 로고
    • To shape a cell: An inquiry into the causes of morphogenesis of microorganisms
    • Harold F.M. To shape a cell: an inquiry into the causes of morphogenesis of microorganisms. Microbiol. Rev. 54:1990;381-431.
    • (1990) Microbiol. Rev. , vol.54 , pp. 381-431
    • Harold, F.M.1
  • 174
    • 0029829906 scopus 로고    scopus 로고
    • Cell division gene ftsQ is required for efficient sporulation but not growth and viability in Streptomyces coelicolor A3
    • McCormick J.R., Losick R. Cell division gene ftsQ is required for efficient sporulation but not growth and viability in Streptomyces coelicolor A3. J. Bacteriol. 178:(2):1996;5295-5301.
    • (1996) J. Bacteriol. , vol.178 , Issue.2 , pp. 5295-5301
    • McCormick, J.R.1    Losick, R.2
  • 175
    • 0027996226 scopus 로고
    • Growth and viability of Streptomyces coelicolor mutant for the cell division gene ftsZ
    • McCormick J.R., Su E.P., Driks A., Losick R. Growth and viability of Streptomyces coelicolor mutant for the cell division gene ftsZ. Mol. Microbiol. 14:1994;243-254.
    • (1994) Mol. Microbiol. , vol.14 , pp. 243-254
    • McCormick, J.R.1    Su, E.P.2    Driks, A.3    Losick, R.4
  • 176
    • 0027489263 scopus 로고
    • Cloning and sequencing of the cell division gene pbpB, which encodes penicillin-binding protein 2B in Bacillus subtilis
    • Yanouri A., Daniel R.A., Errington J., Buchanan C.E. Cloning and sequencing of the cell division gene pbpB, which encodes penicillin-binding protein 2B in Bacillus subtilis. J. Bacteriol. 175:1993;7604-7616.
    • (1993) J. Bacteriol. , vol.175 , pp. 7604-7616
    • Yanouri, A.1    Daniel, R.A.2    Errington, J.3    Buchanan, C.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.