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Volumn 6, Issue JUN, 2015, Pages

Cell age dependent concentration of Escherichia coli divisome proteins analyzed with ImageJ and ObjectJ

Author keywords

Divisome; FtsN; FtsZ; Image analysis; Immunolocalization; LpoA; Non destructive marking; PBP1B

Indexed keywords

BACTERIAL PROTEIN; DIVISOME PROTEIN; GLUCOSE; UNCLASSIFIED DRUG;

EID: 84936993818     PISSN: None     EISSN: 1664302X     Source Type: Journal    
DOI: 10.3389/fmicb.2015.00586     Document Type: Article
Times cited : (87)

References (117)
  • 2
    • 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., Frère, J. M., et al. (1997). 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, 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    Frère, J.M.6
  • 3
    • 0025173687 scopus 로고
    • Division genes in Escherichia coli are expressed coordinately to cell septum requirements by gearbox promoters
    • Aldea, M., Garrido, T., Pla, J., and Vicente, M. (1990). Division genes in Escherichia coli are expressed coordinately to cell septum requirements by gearbox promoters. EMBO J. 9, 3787-3794.
    • (1990) EMBO J , vol.9 , pp. 3787-3794
    • Aldea, M.1    Garrido, T.2    Pla, J.3    Vicente, M.4
  • 4
    • 77954376358 scopus 로고    scopus 로고
    • Direct interactions of early and late assembling division proteins in Escherichia coli cells resolved by FRET
    • Alexeeva, S., Gadella, T. W. J., Verheul, J., Verhoeven, G. S., and den Blaauwen, T. (2010). Direct interactions of early and late assembling division proteins in Escherichia coli cells resolved by FRET. Mol. Microbiol. 77, 384-398. doi: 10.1111/j.1365-2958.2010.07211.x
    • (2010) Mol. Microbiol , vol.77 , pp. 384-398
    • Alexeeva, S.1    Gadella, T.W.J.2    Verheul, J.3    Verhoeven, G.S.4    den Blaauwen, T.5
  • 5
    • 4344652693 scopus 로고    scopus 로고
    • Assembly dynamics of FtsZ rings in Bacillus subtilis and Escherichia coli and effects of FtsZ-regulating proteins
    • Anderson, D. E., Gueiros-Filho, F. J., and Erickson, H. P. (2004). Assembly dynamics of FtsZ rings in Bacillus subtilis and Escherichia coli and effects of FtsZ-regulating proteins. J. Bacteriol. 186, 5775-5781. doi: 10.1128/JB.186.17.5775-5781.2004
    • (2004) J. Bacteriol , vol.186 , pp. 5775-5781
    • Anderson, D.E.1    Gueiros-Filho, F.J.2    Erickson, H.P.3
  • 6
    • 84897531987 scopus 로고    scopus 로고
    • MinCDE exploits the dynamic nature of FtsZ filaments for its spatial regulation
    • Arumugam, S., Petrašek, Z., and Schwille, P. (2014). MinCDE exploits the dynamic nature of FtsZ filaments for its spatial regulation. Proc. Natl. Acad. Sci. U.S.A. 111, E1192-E1200. doi: 10.1073/pnas.1317764111
    • (2014) Proc. Natl. Acad. Sci. U.S.A , vol.111 , pp. E1192-E1200
    • Arumugam, S.1    Petrašek, Z.2    Schwille, P.3
  • 7
    • 31544450286 scopus 로고    scopus 로고
    • Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection
    • Baba, T., Ara, T., Hasegawa, M., Takai, Y., Okumura, Y., Baba, M., et al. (2006). Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection. Mol. Syst. Biol. 2, 2006.0008. doi: 10.1038/msb4100050
    • (2006) Mol. Syst. Biol , vol.2 , Issue.2006 , pp. 8
    • Baba, T.1    Ara, T.2    Hasegawa, M.3    Takai, Y.4    Okumura, Y.5    Baba, M.6
  • 8
    • 0031784284 scopus 로고    scopus 로고
    • The ftsQ1p gearbox promoter of Escherichia coli is a major sigma S-dependent promoter in the ddlB-ftsA region
    • Ballesteros, M., Kusano, S., Ishihama, A., and Vicente, M. (1998). The ftsQ1p gearbox promoter of Escherichia coli is a major sigma S-dependent promoter in the ddlB-ftsA region. Mol. Microbiol. 30, 419-430. doi: 10.1046/j.1365-2958.1998.01077.x
    • (1998) Mol. Microbiol , vol.30 , pp. 419-430
    • Ballesteros, M.1    Kusano, S.2    Ishihama, A.3    Vicente, M.4
  • 10
    • 84906569009 scopus 로고    scopus 로고
    • Site-directed fluorescence labeling reveals a revised N-terminal membrane topology and functional periplasmic residues in the Escherichia coli cell division protein FtsK
    • Berezuk, A. M., Goodyear, M., and Khursigara, C. M. (2014). Site-directed fluorescence labeling reveals a revised N-terminal membrane topology and functional periplasmic residues in the Escherichia coli cell division protein FtsK. J. Biol. Chem. 289, 23287-23301. doi: 10.1074/jbc.M114.569624
    • (2014) J. Biol. Chem , vol.289 , pp. 23287-23301
    • Berezuk, A.M.1    Goodyear, M.2    Khursigara, C.M.3
  • 11
    • 27844575191 scopus 로고    scopus 로고
    • In vitro murein peptidoglycan synthesis by dimers of the bifunctional transglycosylase-transpeptidase PBP1B from Escherichia coli
    • Bertsche, U., Breukink, E., Kast, T., and Vollmer, W. (2005). In vitro murein peptidoglycan synthesis by dimers of the bifunctional transglycosylase-transpeptidase PBP1B from Escherichia coli. J. Biol. Chem. 280, 38096-38101. doi: 10.1074/jbc.M508646200
    • (2005) J. Biol. Chem , vol.280 , pp. 38096-38101
    • Bertsche, U.1    Breukink, E.2    Kast, T.3    Vollmer, W.4
  • 12
    • 33748333182 scopus 로고    scopus 로고
    • Interaction between two murein (peptidoglycan) synthases, PBP3 and PBP1B, in Escherichia coli
    • Bertsche, U., Kast, T., Wolf, B., Fraipont, C., Aarsman, M. E. G., Kannenberg, K., et al. (2006). Interaction between two murein (peptidoglycan) synthases, PBP3 and PBP1B, in Escherichia coli. Mol. Microbiol. 61, 675-690. doi: 10.1111/j.1365-2958.2006.05280.x
    • (2006) Mol. Microbiol , vol.61 , pp. 675-690
    • Bertsche, U.1    Kast, T.2    Wolf, B.3    Fraipont, C.4    Aarsman, M.E.G.5    Kannenberg, K.6
  • 13
    • 84891598518 scopus 로고    scopus 로고
    • MinC, MinD, and MinE drive counter-oscillation of early-cell-division proteins prior to Escherichia coli septum formation.
    • Bisicchia, P., Arumugam, S., Schwille, P., and Sherratt, D. (2013a). MinC, MinD, and MinE drive counter-oscillation of early-cell-division proteins prior to Escherichia coli septum formation. mBio 4:e00856-13. doi: 10.1128/mBio.00856-13
    • (2013) mBio , vol.4
    • Bisicchia, P.1    Arumugam, S.2    Schwille, P.3    Sherratt, D.4
  • 14
    • 84891587996 scopus 로고    scopus 로고
    • The N-terminal membrane-spanning domain of the Escherichia coli DNA translocase FtsK hexamerizes at midcell.
    • Bisicchia, P., Steel, B., Mariam Debela, M. H., Löwe, J., and Sherratt, D. (2013b). The N-terminal membrane-spanning domain of the Escherichia coli DNA translocase FtsK hexamerizes at midcell. mBio 4:e00800-13. doi: 10.1128/mBio.00800-13
    • (2013) mBio , vol.4
    • Bisicchia, P.1    Steel, B.2    Mariam Debela, M.H.3    Löwe, J.4    Sherratt, D.5
  • 15
    • 84859055009 scopus 로고    scopus 로고
    • Three-dimensional super-resolution imaging of the midplane protein FtsZ in live Caulobacter crescentus cells using astigmatism.
    • Biteen, J. S., Goley, E. D., Shapiro, L., and Moerner, W. E. (2012). Three-dimensional super-resolution imaging of the midplane protein FtsZ in live Caulobacter crescentus cells using astigmatism. Chemphyschem 13, 1007-1012. doi: 10.1002/cphc.201100686
    • (2012) Chemphyschem , vol.13 , pp. 1007-1012
    • Biteen, J.S.1    Goley, E.D.2    Shapiro, L.3    Moerner, W.E.4
  • 16
    • 85017732734 scopus 로고    scopus 로고
    • Immunolabeling of Proteins in Situ in Escherichia coli K12 Strains.
    • Buddelmeijer, N., Aarsman, M. E. G., and den Blaauwen, T. (2013). Immunolabeling of Proteins in Situ in Escherichia coli K12 Strains. Bio-Protocoll, 1-4. Available at: http://www.bio-protocol.org/wenzhang.aspx?id=852
    • (2013) Bio-Protocoll , pp. 1-4
    • Buddelmeijer, N.1    Aarsman, M.E.G.2    den Blaauwen, T.3
  • 17
    • 2942570076 scopus 로고    scopus 로고
    • A complex of the Escherichia coli cell division proteins FtsL, FtsB and FtsQ forms independently of its localization to the septal region
    • Buddelmeijer, N., and Beckwith, J. (2004). A complex of the Escherichia coli cell division proteins FtsL, FtsB and FtsQ forms independently of its localization to the septal region. Mol. Microbiol. 52, 1315-1327. doi: 10.1111/j.1365-2958.2004.04044.x
    • (2004) Mol. Microbiol , vol.52 , pp. 1315-1327
    • Buddelmeijer, N.1    Beckwith, J.2
  • 18
    • 84902001403 scopus 로고    scopus 로고
    • A role for FtsA in SPOR-independent localization of the essential Escherichia coli cell division protein FtsN
    • Busiek, K. K., and Margolin, W. (2014). A role for FtsA in SPOR-independent localization of the essential Escherichia coli cell division protein FtsN. Mol. Microbiol. 92, 1212-1226. doi: 10.1111/mmi.12623
    • (2014) Mol. Microbiol , vol.92 , pp. 1212-1226
    • Busiek, K.K.1    Margolin, W.2
  • 19
    • 84884282214 scopus 로고    scopus 로고
    • In vivo organization of the FtsZ-ring by ZapA and ZapB revealed by quantitative super-resolution microscopy
    • Buss, J., Coltharp, C., Huang, T., Pohlmeyer, C., Wang, S.-C., Hatem, C., et al. (2013). In vivo organization of the FtsZ-ring by ZapA and ZapB revealed by quantitative super-resolution microscopy. Mol. Microbiol. 89, 1099-1120. doi: 10.1111/mmi.12331
    • (2013) Mol. Microbiol , vol.89 , pp. 1099-1120
    • Buss, J.1    Coltharp, C.2    Huang, T.3    Pohlmeyer, C.4    Wang, S.-C.5    Hatem, C.6
  • 20
    • 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., Yang, X., Hess, H., and Xiao, J. (2015). A multi-layered protein network stabilizes the Escherichia coli FtsZ-ring and modulates constriction dynamics. PLoS Genet. 11:e1005128. doi: 10.1371/journal.pgen.1005128
    • (2015) PLoS Genet. , vol.11
    • Buss, J.1    Coltharp, C.2    Shtengel, G.3    Yang, X.4    Hess, H.5    Xiao, J.6
  • 21
    • 67649811066 scopus 로고    scopus 로고
    • ClpXP protease degrades the cytoskeletal protein, FtsZ, and modulates FtsZ polymer dynamics
    • Camberg, J. L., Hoskins, J. R., and Wickner, S. (2009). ClpXP protease degrades the cytoskeletal protein, FtsZ, and modulates FtsZ polymer dynamics. Proc. Natl. Acad. Sci. U.S.A. 106, 10614-10619. doi: 10.1073/pnas.0904886106
    • (2009) Proc. Natl. Acad. Sci. U.S.A , vol.106 , pp. 10614-10619
    • Camberg, J.L.1    Hoskins, J.R.2    Wickner, S.3
  • 22
    • 79955460424 scopus 로고    scopus 로고
    • The interplay of ClpXP with the cell division machinery in Escherichia coli
    • Camberg, J. L., Hoskins, J. R., and Wickner, S. (2011). The interplay of ClpXP with the cell division machinery in Escherichia coli. J. Bacteriol. 193, 1911-1918. doi: 10.1128/JB.01317-10
    • (2011) J. Bacteriol , vol.193 , pp. 1911-1918
    • Camberg, J.L.1    Hoskins, J.R.2    Wickner, S.3
  • 23
    • 84899503736 scopus 로고    scopus 로고
    • Location of dual sites in E. coli FtsZ important for degradation by ClpXP; one at the C-terminus and one in the disordered linker.
    • Camberg, J. L., Viola, M. G., Rea, L., Hoskins, J. R., and Wickner, S. (2014). Location of dual sites in E. coli FtsZ important for degradation by ClpXP; one at the C-terminus and one in the disordered linker. PLoS ONE 9:e94964. doi: 10.1371/journal.pone.0094964
    • (2014) PLoS ONE , vol.9
    • Camberg, J.L.1    Viola, M.G.2    Rea, L.3    Hoskins, J.R.4    Wickner, S.5
  • 24
    • 20444457941 scopus 로고    scopus 로고
    • Rapid in vitro assembly dynamics and subunit turnover of FtsZ demonstrated by fluorescence resonance energy transfer
    • Chen, Y., and Erickson, H. P. (2005). Rapid in vitro assembly dynamics and subunit turnover of FtsZ demonstrated by fluorescence resonance energy transfer. J. Biol. Chem. 280, 22549-22554. doi: 10.1074/jbc.M500895200
    • (2005) J. Biol. Chem , vol.280 , pp. 22549-22554
    • Chen, Y.1    Erickson, H.P.2
  • 25
    • 33846299252 scopus 로고    scopus 로고
    • Three functional subdomains of the Escherichia coli FtsQ protein are involved in its interaction with the other division proteins.
    • D'Ulisse, V., Fagioli, M., Ghelardini, P., and Paolozzi, L. (2007). Three functional subdomains of the Escherichia coli FtsQ protein are involved in its interaction with the other division proteins. Microbiology 153, 124-138. doi: 10.1099/mic.0.2006/000265-0
    • (2007) Microbiology , vol.153 , pp. 124-138
    • D'Ulisse, V.1    Fagioli, M.2    Ghelardini, P.3    Paolozzi, L.4
  • 26
    • 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, P. A., Crossley, R. E., and Rothfield, L. I. (1989). 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 56, 641-649. doi: 10.1016/0092-8674(89)90586-2
    • (1989) Cell , vol.56 , pp. 641-649
    • de Boer, P.A.1    Crossley, R.E.2    Rothfield, L.I.3
  • 27
    • 0026039677 scopus 로고
    • The MinD protein is a membrane ATPase required for the correct placement of the Escherichia coli division site
    • de Boer, P. A., Crossley, R. E., Hand, A. R., and Rothfield, L. I. (1991). The MinD protein is a membrane ATPase required for the correct placement of the Escherichia coli division site. EMBO J. 10, 4371-4380.
    • (1991) EMBO J , vol.10 , pp. 4371-4380
    • de Boer, P.A.1    Crossley, R.E.2    Hand, A.R.3    Rothfield, L.I.4
  • 29
    • 0016221639 scopus 로고
    • Macromolecular composition during steady-state growth of Escherichia coli B-r
    • Dennis, P. P., and Bremer, H. (1974). Macromolecular composition during steady-state growth of Escherichia coli B-r. J. Bacteriol. 119, 270-281.
    • (1974) J. Bacteriol , vol.119 , pp. 270-281
    • Dennis, P.P.1    Bremer, H.2
  • 30
    • 0346252349 scopus 로고    scopus 로고
    • Use of a two-hybrid assay to study the assembly of a complex multicomponent protein machinery: bacterial septosome differentiation.
    • Di Lallo, G., Fagioli, M., Barionovi, D., Ghelardini, P., and Paolozzi, L. (2003). Use of a two-hybrid assay to study the assembly of a complex multicomponent protein machinery: bacterial septosome differentiation. Microbiology 149, 3353-3359. doi: 10.1099/mic.0.26580-0
    • (2003) Microbiology , vol.149 , pp. 3353-3359
    • Di Lallo, G.1    Fagioli, M.2    Barionovi, D.3    Ghelardini, P.4    Paolozzi, L.5
  • 31
    • 0029956443 scopus 로고    scopus 로고
    • Direct quantitation of the number of individual penicillin-binding proteins per cell in Escherichia coli
    • Dougherty, T. J., Kennedy, K., Kessler, R. E., and Pucci, M. J. (1996). Direct quantitation of the number of individual penicillin-binding proteins per cell in Escherichia coli. J. Bacteriol. 178, 6110-6115.
    • (1996) J. Bacteriol , vol.178 , pp. 6110-6115
    • Dougherty, T.J.1    Kennedy, K.2    Kessler, R.E.3    Pucci, M.J.4
  • 32
    • 84887539571 scopus 로고    scopus 로고
    • Identification of SPOR domain amino acids important for septal localization, peptidoglycan binding, and a disulfide bond in the cell division protein FtsN
    • Duncan, T. R., Yahashiri, A., Arends, S. J. R., Popham, D. L., and Weiss, D. S. (2013). Identification of SPOR domain amino acids important for septal localization, peptidoglycan binding, and a disulfide bond in the cell division protein FtsN. J. Bacteriol. 195, 5308-5315. doi: 10.1128/JB.00911-13
    • (2013) J. Bacteriol , vol.195 , pp. 5308-5315
    • Duncan, T.R.1    Yahashiri, A.2    Arends, S.J.R.3    Popham, D.L.4    Weiss, D.S.5
  • 33
    • 0037701641 scopus 로고    scopus 로고
    • Probing the catalytic activity of a cell division-specific transpeptidase in vivo with beta-lactams
    • Eberhardt, C., Kuerschner, L., and Weiss, D. S. (2003). Probing the catalytic activity of a cell division-specific transpeptidase in vivo with beta-lactams. J. Bacteriol. 185, 3726-3734. doi: 10.1128/JB.185.13.3726-3734.2003
    • (2003) J. Bacteriol , vol.185 , pp. 3726-3734
    • Eberhardt, C.1    Kuerschner, L.2    Weiss, D.S.3
  • 34
    • 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., Löwe, J., and Gerdes, K. (2008). Novel coiled-coil cell division factor ZapB stimulates Z ring assembly and cell division. Mol. Microbiol. 68, 720-735. doi: 10.1111/j.1365-2958.2008.06190.x
    • (2008) Mol. Microbiol , vol.68 , pp. 720-735
    • Ebersbach, G.1    Galli, E.2    Møller-Jensen, J.3    Löwe, J.4    Gerdes, K.5
  • 35
    • 84872856522 scopus 로고    scopus 로고
    • The physiology of bacterial cell division
    • Egan, A. J. F., and Vollmer, W. (2013). The physiology of bacterial cell division. Ann. N. Y. Acad. Sci. 1277, 8-28. doi: 10.1111/j.1749-6632.2012.06818.x
    • (2013) Ann. N. Y. Acad. Sci , vol.1277 , pp. 8-28
    • Egan, A.J.F.1    Vollmer, W.2
  • 36
    • 84864147092 scopus 로고    scopus 로고
    • A MatP-divisome interaction coordinates chromosome segregation with cell division in E
    • Espeli, O., Borne, R., Dupaigne, P., Thiel, A., Gigant, E., Mercier, R., et al. (2012). A MatP-divisome interaction coordinates chromosome segregation with cell division in E. coli. EMBO J. 31, 3198-3211. doi: 10.1038/emboj.2012.128
    • (2012) coli. EMBO J , vol.31 , pp. 3198-3211
    • Espeli, O.1    Borne, R.2    Dupaigne, P.3    Thiel, A.4    Gigant, E.5    Mercier, R.6
  • 37
    • 84880238403 scopus 로고    scopus 로고
    • Direct interaction of FtsZ and MreB is required for septum synthesis and cell division in Escherichia coli
    • Fenton, A. K., and Gerdes, K. (2013). Direct interaction of FtsZ and MreB is required for septum synthesis and cell division in Escherichia coli. EMBO J. 32, 1953-1965. doi: 10.1038/emboj.2013.129
    • (2013) EMBO J , vol.32 , pp. 1953-1965
    • Fenton, A.K.1    Gerdes, K.2
  • 38
    • 78650738448 scopus 로고    scopus 로고
    • The integral membrane FtsW protein and peptidoglycan synthase PBP3 form a subcomplex in Escherichia coli.
    • Fraipont, C., Alexeeva, S., Wolf, B., van der Ploeg, R., Schloesser, M., den Blaauwen, T., et al. (2011). The integral membrane FtsW protein and peptidoglycan synthase PBP3 form a subcomplex in Escherichia coli. Microbiology 157, 251-259. doi: 10.1099/mic.0.040071-0
    • (2011) Microbiology , vol.157 , pp. 251-259
    • Fraipont, C.1    Alexeeva, S.2    Wolf, B.3    van der Ploeg, R.4    Schloesser, M.5    den Blaauwen, T.6
  • 39
    • 77958525927 scopus 로고    scopus 로고
    • In vivo structure of the E. coli FtsZ-ring revealed by photoactivated localization Microscopy (PALM).
    • Fu, G., Huang, T., Buss, J., Coltharp, C., Hensel, Z., and Xiao, J. (2010). In vivo structure of the E. coli FtsZ-ring revealed by photoactivated localization Microscopy (PALM). PLoS ONE 5:e12682. doi: 10.1371/journal.pone.0012680
    • (2010) PLoS ONE , vol.5
    • Fu, G.1    Huang, T.2    Buss, J.3    Coltharp, C.4    Hensel, Z.5    Xiao, J.6
  • 40
    • 77953494296 scopus 로고    scopus 로고
    • Spatial resolution of two bacterial cell division proteins: ZapA recruits ZapB to the inner face of the Z-ring
    • Galli, E., and Gerdes, K. (2010). Spatial resolution of two bacterial cell division proteins: ZapA recruits ZapB to the inner face of the Z-ring. Mol. Microbiol. 76, 1514-1526. doi: 10.1111/j.1365-2958.2010.07183.x
    • (2010) Mol. Microbiol , vol.76 , pp. 1514-1526
    • Galli, E.1    Gerdes, K.2
  • 41
    • 0027176669 scopus 로고
    • Transcription of ftsZ oscillates during the cell cycle of Escherichia coli
    • Garrido, T., Sánchez, M., Palacios, P., Aldea, M., and Vicente, M. (1993). Transcription of ftsZ oscillates during the cell cycle of Escherichia coli. EMBO J. 12, 3957-3965.
    • (1993) EMBO J , vol.12 , pp. 3957-3965
    • Garrido, T.1    Sánchez, M.2    Palacios, P.3    Aldea, M.4    Vicente, M.5
  • 42
    • 72449160318 scopus 로고    scopus 로고
    • Self-enhanced accumulation of FtsN at division sites and roles for other proteins with a SPOR domain (DamX, DedD, and RlpA) in Escherichia coli cell constriction
    • Gerding, M. A., Liu, B., Bendezú, F. O., Hale, C. A., Bernhardt, T. G., and De Boer, P. A. J. (2009). Self-enhanced accumulation of FtsN at division sites and roles for other proteins with a SPOR domain (DamX, DedD, and RlpA) in Escherichia coli cell constriction. J. Bacteriol. 191, 7383-7401. doi: 10.1128/JB.00811-09
    • (2009) J. Bacteriol , vol.191 , pp. 7383-7401
    • Gerding, M.A.1    Liu, B.2    Bendezú, F.O.3    Hale, C.A.4    Bernhardt, T.G.5    De Boer, P.A.J.6
  • 43
    • 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., and de Boer, P. A. (1999). Recruitment of ZipA to the septal ring of Escherichia coli is dependent on FtsZ and independent of FtsA. J. Bacteriol. 181, 167-176.
    • (1999) J. Bacteriol , vol.181 , pp. 167-176
    • Hale, C.A.1    de Boer, P.A.2
  • 44
    • 0036229552 scopus 로고    scopus 로고
    • ZipA is required for recruitment of FtsK, FtsQ, FtsL, and FtsN to the septal ring in Escherichia coli
    • Hale, C. A., and de Boer, P. A. J. (2002). ZipA is required for recruitment of FtsK, FtsQ, FtsL, and FtsN to the septal ring in Escherichia coli. J. Bacteriol. 184, 2552-2556. doi: 10.1128/JB.184.9.2552-2556.2002
    • (2002) J. Bacteriol , vol.184 , pp. 2552-2556
    • Hale, C.A.1    de Boer, P.A.J.2
  • 45
    • 0035853803 scopus 로고    scopus 로고
    • Genetic analysis of the Escherichia coli FtsZ.ZipA interaction in the yeast two-hybrid system. Characterization of FtsZ residues essential for the interactions with ZipA and with FtsA.
    • Haney, S. A., Glasfeld, E., Hale, C., Keeney, D., He, Z., and de Boer, P. (2001). Genetic analysis of the Escherichia coli FtsZ.ZipA interaction in the yeast two-hybrid system. Characterization of FtsZ residues essential for the interactions with ZipA and with FtsA. J. Biol. Chem. 276, 11980-11987. doi: 10.1074/jbc.M009810200
    • (2001) J. Biol. Chem , vol.276 , pp. 11980-11987
    • Haney, S.A.1    Glasfeld, E.2    Hale, C.3    Keeney, D.4    He, Z.5    de Boer, P.6
  • 46
    • 84864010982 scopus 로고    scopus 로고
    • Osmolality-dependent relocation of penicillin-binding protein PBP2 to the division site in caulobacter crescentus
    • Hocking, J., Priyadarshini, R., Takacs, C. N., Costa, T., Dye, N. A., Shapiro, L., et al. (2012). Osmolality-dependent relocation of penicillin-binding protein PBP2 to the division site in caulobacter crescentus. J. Bacteriol. 194, 3116-3127. doi: 10.1128/JB.00260-12
    • (2012) J. Bacteriol , vol.194 , pp. 3116-3127
    • Hocking, J.1    Priyadarshini, R.2    Takacs, C.N.3    Costa, T.4    Dye, N.A.5    Shapiro, L.6
  • 47
    • 0037858060 scopus 로고    scopus 로고
    • Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli
    • Höltje, J. V. (1998). Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli. Microbiol. Mol. Biol. Rev. 62, 181-203.
    • (1998) Microbiol. Mol. Biol. Rev , vol.62 , pp. 181-203
    • Höltje, J.V.1
  • 48
    • 79952041482 scopus 로고    scopus 로고
    • Super-resolution imaging of the bacterial cytokinetic protein FtsZ.
    • Jennings, P. C., Cox, G. C., Monahan, L. G., and Harry, E. J. (2011). Super-resolution imaging of the bacterial cytokinetic protein FtsZ. Micron 42, 336-341. doi: 10.1016/j.micron.2010.09.003
    • (2011) Micron , vol.42 , pp. 336-341
    • Jennings, P.C.1    Cox, G.C.2    Monahan, L.G.3    Harry, E.J.4
  • 49
    • 77955932270 scopus 로고    scopus 로고
    • Changes in the Min oscillation pattern before and after cell birth
    • Juarez, J. R., and Margolin, W. (2010). Changes in the Min oscillation pattern before and after cell birth. J. Bacteriol. 192, 4134-4142. doi: 10.1128/JB.00364-10
    • (2010) J. Bacteriol , vol.192 , pp. 4134-4142
    • Juarez, J.R.1    Margolin, W.2
  • 50
    • 34250627500 scopus 로고    scopus 로고
    • DNA and origin region segregation are not affected by the transition from rod to sphere after inhibition of Escherichia coli MreB by A22
    • Karczmarek, A., Martínez-Arteaga, R., Baselga, R. M.-A., Alexeeva, S., Hansen, F. G., Vicente, M., et al. (2007). DNA and origin region segregation are not affected by the transition from rod to sphere after inhibition of Escherichia coli MreB by A22. Mol. Microbiol. 65, 51-63. doi: 10.1111/j.1365-2958.2007.05777.x
    • (2007) Mol. Microbiol , vol.65 , pp. 51-63
    • Karczmarek, A.1    Martínez-Arteaga, R.2    Baselga, R.M.-A.3    Alexeeva, S.4    Hansen, F.G.5    Vicente, M.6
  • 51
    • 15244361175 scopus 로고    scopus 로고
    • Interaction network among Escherichia coli membrane proteins involved in cell division as revealed by bacterial two-hybrid analysis
    • Karimova, G., Dautin, N., and Ladant, D. (2005). Interaction network among Escherichia coli membrane proteins involved in cell division as revealed by bacterial two-hybrid analysis. J. Bacteriol. 187, 2233-2243. doi: 10.1128/JB.187.7.2233-2243.2005
    • (2005) J. Bacteriol , vol.187 , pp. 2233-2243
    • Karimova, G.1    Dautin, N.2    Ladant, D.3
  • 52
    • 58149492417 scopus 로고    scopus 로고
    • Characterization of YmgF, a 72-residue inner membrane protein that associates with the Escherichia coli cell division machinery
    • Karimova, G., Robichon, C., and Ladant, D. (2009). Characterization of YmgF, a 72-residue inner membrane protein that associates with the Escherichia coli cell division machinery. J. Bacteriol. 191, 333-346. doi: 10.1128/JB.00331-08
    • (2009) J. Bacteriol , vol.191 , pp. 333-346
    • Karimova, G.1    Robichon, C.2    Ladant, D.3
  • 53
    • 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, C.-M., Aarsman, M. E. G., Postmus, J., Pas, E., Muijsers, A. O., Scheffers, D.-J., et al. (2004). R174 of Escherichia coli FtsZ is involved in membrane interaction and protofilament bundling, and is essential for cell division. Mol. Microbiol. 51, 645-657. doi: 10.1046/j.1365-2958.2003.03876.x
    • (2004) Mol. Microbiol , vol.51 , pp. 645-657
    • Koppelman, C.-M.1    Aarsman, M.E.G.2    Postmus, J.3    Pas, E.4    Muijsers, A.O.5    Scheffers, D.-J.6
  • 54
    • 82555203013 scopus 로고    scopus 로고
    • ZipA binds to FtsZ with high affinity and enhances the stability of FtsZ protofilaments.
    • Kuchibhatla, A., Bhattacharya, A., and Panda, D. (2011). ZipA binds to FtsZ with high affinity and enhances the stability of FtsZ protofilaments. PLoS ONE 6:e28262. doi: 10.1371/journal.pone.0028262.g007
    • (2011) PLoS ONE , vol.6
    • Kuchibhatla, A.1    Bhattacharya, A.2    Panda, D.3
  • 55
    • 84899550455 scopus 로고    scopus 로고
    • Quantifying absolute protein synthesis rates reveals principles underlying allocation of cellular resources.
    • Li, G.-W., Burkhardt, D., Gross, C., and Weissman, J. S. (2014). Quantifying absolute protein synthesis rates reveals principles underlying allocation of cellular resources. Cell 157, 624-635. doi: 10.1016/j.cell.2014.02.033
    • (2014) Cell , vol.157 , pp. 624-635
    • Li, G.-W.1    Burkhardt, D.2    Gross, C.3    Weissman, J.S.4
  • 56
    • 84924595732 scopus 로고    scopus 로고
    • Roles for both FtsA and the FtsBLQ subcomplex in FtsN-stimulated cell constriction in Escherichia coli
    • Liu, B., Persons, L., Lee, L., and De Boer, P. A. J. (2015). Roles for both FtsA and the FtsBLQ subcomplex in FtsN-stimulated cell constriction in Escherichia coli. Mol Microbiol. 95, 945-970. doi: 10.1111/mmi.12906
    • (2015) Mol Microbiol , vol.95 , pp. 945-970
    • Liu, B.1    Persons, L.2    Lee, L.3    De Boer, P.A.J.4
  • 57
    • 79955571598 scopus 로고    scopus 로고
    • Min protein patterns emerge from rapid rebinding and membrane interaction of MinE
    • Loose, M., Fischer-Friedrich, E., Herold, C., Kruse, K., and Schwille, P. (2011). Min protein patterns emerge from rapid rebinding and membrane interaction of MinE. Nat. Struct. Mol. Biol. 18, 577-583. doi: 10.1038/nsmb.2037
    • (2011) Nat. Struct. Mol. Biol , vol.18 , pp. 577-583
    • Loose, M.1    Fischer-Friedrich, E.2    Herold, C.3    Kruse, K.4    Schwille, P.5
  • 58
    • 84891344282 scopus 로고    scopus 로고
    • The bacterial cell division proteins FtsA and FtsZ self-organize into dynamic cytoskeletal patterns
    • Loose, M., and Mitchison, T. J. (2014). The bacterial cell division proteins FtsA and FtsZ self-organize into dynamic cytoskeletal patterns. Nat. Cell Biol. 16, 38-46. doi: 10.1038/ncb2885
    • (2014) Nat. Cell Biol , vol.16 , pp. 38-46
    • Loose, M.1    Mitchison, T.J.2
  • 59
    • 4344620117 scopus 로고    scopus 로고
    • The crystal structure of ZapA and its modulation of FtsZ polymerisation
    • Low, H. H., Moncrieffe, M. C., and Löwe, J. (2004). The crystal structure of ZapA and its modulation of FtsZ polymerisation. J. Mol. Biol. 341, 839-852. doi: 10.1016/j.jmb.2004.05.031
    • (2004) J. Mol. Biol , vol.341 , pp. 839-852
    • Low, H.H.1    Moncrieffe, M.C.2    Löwe, J.3
  • 60
    • 49349104892 scopus 로고    scopus 로고
    • Molecular mechanism of sequence-directed DNA loading and translocation by FtsK
    • Löwe, J., Ellonen, A., Allen, M. D., Atkinson, C., Sherratt, D. J., and Grainge, I. (2008). Molecular mechanism of sequence-directed DNA loading and translocation by FtsK. Mol. Cell. 31, 498-509. doi: 10.1016/j.molcel.2008.05.027
    • (2008) Mol. Cell , vol.31 , pp. 498-509
    • Löwe, J.1    Ellonen, A.2    Allen, M.D.3    Atkinson, C.4    Sherratt, D.J.5    Grainge, I.6
  • 61
    • 84867995401 scopus 로고    scopus 로고
    • Bacterial cytokinesis: From Z ring to divisome.
    • Lutkenhaus, J., Pichoff, S., and Du, S. (2012). Bacterial cytokinesis: From Z ring to divisome. Cytoskeleton (Hoboken) 69, 778-790. doi: 10.1002/cm.21054
    • (2012) Cytoskeleton (Hoboken) , vol.69 , pp. 778-790
    • Lutkenhaus, J.1    Pichoff, S.2    Du, S.3
  • 62
    • 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., and Margolin, W. (1996). Colocalization of cell division proteins FtsZ and FtsA to cytoskeletal structures in living Escherichia coli cells by using green fluorescent protein. Proc. Natl. Acad. Sci. U.S.A. 93, 12998-13003. doi: 10.1073/pnas.93.23.12998
    • (1996) Proc. Natl. Acad. Sci. U.S.A , vol.93 , pp. 12998-13003
    • Ma, X.1    Ehrhardt, D.W.2    Margolin, W.3
  • 63
    • 33746987484 scopus 로고    scopus 로고
    • Double-stranded DNA translocation: structure and mechanism of hexameric FtsK
    • Massey, T. H., Mercogliano, C. P., Yates, J., Sherratt, D. J., and Löwe, J. (2006). Double-stranded DNA translocation: structure and mechanism of hexameric FtsK. Mol. Cell. 23, 457-469. doi: 10.1016/j.molcel.2006.06.019
    • (2006) Mol. Cell , vol.23 , pp. 457-469
    • Massey, T.H.1    Mercogliano, C.P.2    Yates, J.3    Sherratt, D.J.4    Löwe, J.5
  • 64
    • 54949146519 scopus 로고    scopus 로고
    • The MatP/matS site-specific system organizes the terminus region of the E. coli chromosome into a macrodomain.
    • Mercier, R., Petit, M.-A., Schbath, S., Robin, S., El Karoui, M., Boccard, F., et al. (2008). The MatP/matS site-specific system organizes the terminus region of the E. coli chromosome into a macrodomain. Cell 135, 475-485. doi: 10.1016/j.cell.2008.08.031
    • (2008) Cell , vol.135 , pp. 475-485
    • Mercier, R.1    Petit, M.-A.2    Schbath, S.3    Robin, S.4    El Karoui, M.5    Boccard, F.6
  • 65
    • 34547651288 scopus 로고    scopus 로고
    • The essential peptidoglycan glycosyltransferase MurG forms a complex with proteins involved in lateral envelope growth as well as with proteins involved in cell division in Escherichia coli
    • Mohammadi, T., Karczmarek, A., Crouvoisier, M., Bouhss, A., Mengin-Lecreulx, D., and den Blaauwen, T. (2007). The essential peptidoglycan glycosyltransferase MurG forms a complex with proteins involved in lateral envelope growth as well as with proteins involved in cell division in Escherichia coli. Mol. Microbiol. 65, 1106-1121. doi: 10.1111/j.1365-2958.2007.05851.x
    • (2007) Mol. Microbiol , vol.65 , pp. 1106-1121
    • Mohammadi, T.1    Karczmarek, A.2    Crouvoisier, M.3    Bouhss, A.4    Mengin-Lecreulx, D.5    den Blaauwen, T.6
  • 66
    • 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, G. E. J., Verheul, J., Comvalius, A. D., Martos, A., Alfonso, C., et al. (2009). The GTPase activity of Escherichia coli FtsZ determines the magnitude of the FtsZ polymer bundling by ZapA in vitro. Biochemistry 48, 11056-11066. doi: 10.1021/bi901461p
    • (2009) Biochemistry , vol.48 , pp. 11056-11066
    • Mohammadi, T.1    Ploeger, G.E.J.2    Verheul, J.3    Comvalius, A.D.4    Martos, A.5    Alfonso, C.6
  • 67
    • 84901389207 scopus 로고    scopus 로고
    • Specificity of the transport of Lipid II by FtsW in Escherichia coli
    • Mohammadi, T., Sijbrandi, R., Lutters, M., Verheul, J., Martin, N., den Blaauwen, T., et al. (2014). Specificity of the transport of Lipid II by FtsW in Escherichia coli. J. Biol. Chem. 289, 17707-17718. doi: 10.1074/jbc.M114.557371
    • (2014) J. Biol. Chem , vol.289 , pp. 17707-17718
    • Mohammadi, T.1    Sijbrandi, R.2    Lutters, M.3    Verheul, J.4    Martin, N.5    den Blaauwen, T.6
  • 68
    • 79955007775 scopus 로고    scopus 로고
    • Identification of FtsW as a transporter of lipid-linked cell wall precursors across the membrane
    • Mohammadi, T., van Dam, V., Sijbrandi, R., Vernet, T., Zapun, A. E., Bouhss, A., et al. (2011). Identification of FtsW as a transporter of lipid-linked cell wall precursors across the membrane. EMBO J. 30, 1425-1432. doi: 10.1038/emboj.2011.61
    • (2011) EMBO J , vol.30 , pp. 1425-1432
    • Mohammadi, T.1    van Dam, V.2    Sijbrandi, R.3    Vernet, T.4    Zapun, A.E.5    Bouhss, A.6
  • 69
    • 0034600952 scopus 로고    scopus 로고
    • The bacterial cell-division protein ZipA and its interaction with an FtsZ fragment revealed by X-ray crystallography
    • Mosyak, L., Zhang, Y., Glasfeld, E., Haney, S., Stahl, M., Seehra, J., et al. (2000). The bacterial cell-division protein ZipA and its interaction with an FtsZ fragment revealed by X-ray crystallography. EMBO J. 19, 3179-3191. doi: 10.1093/emboj/19.13.3179
    • (2000) EMBO J , vol.19 , pp. 3179-3191
    • Mosyak, L.1    Zhang, Y.2    Glasfeld, E.3    Haney, S.4    Stahl, M.5    Seehra, J.6
  • 70
    • 0025100516 scopus 로고
    • Differential translation of cell division proteins
    • Mukherjee, A., and Donachie, W. D. (1990). Differential translation of cell division proteins. J. Bacteriol. 172, 6106-6111.
    • (1990) J. Bacteriol , vol.172 , pp. 6106-6111
    • Mukherjee, A.1    Donachie, W.D.2
  • 71
    • 37548998632 scopus 로고    scopus 로고
    • The essential cell division protein FtsN interacts with the murein (peptidoglycan) synthase PBP1B in Escherichia coli
    • Müller, P., Ewers, C., Bertsche, U., Anstett, M., Kallis, T., Breukink, E., et al. (2007). The essential cell division protein FtsN interacts with the murein (peptidoglycan) synthase PBP1B in Escherichia coli. J. Biol. Chem. 282, 36394-36402. doi: 10.1074/jbc.M706390200
    • (2007) J. Biol. Chem , vol.282 , pp. 36394-36402
    • Müller, P.1    Ewers, C.2    Bertsche, U.3    Anstett, M.4    Kallis, T.5    Breukink, E.6
  • 74
    • 78650497005 scopus 로고    scopus 로고
    • Lipoprotein cofactors located in the outer membrane activate bacterial cell wall polymerases.
    • Paradis-Bleau, C., Markovski, M., Uehara, T., Lupoli, T. J., Walker, S., Kahne, D. E., et al. (2010). Lipoprotein cofactors located in the outer membrane activate bacterial cell wall polymerases. Cell 143, 1110-1120. doi: 10.1016/j.cell.2010.11.037
    • (2010) Cell , vol.143 , pp. 1110-1120
    • Paradis-Bleau, C.1    Markovski, M.2    Uehara, T.3    Lupoli, T.J.4    Walker, S.5    Kahne, D.E.6
  • 75
    • 84873286335 scopus 로고    scopus 로고
    • A specific role for the ZipA protein in cell division: stabilization of the FtsZ protein.
    • Pazos, M., Natale, P., and Vicente, M. (2013a). A specific role for the ZipA protein in cell division: stabilization of the FtsZ protein. J. Biol. Chem. 288, 3219-3226. doi: 10.1074/jbc.M112.434944
    • (2013) J. Biol. Chem. , vol.288 , pp. 3219-3226
    • Pazos, M.1    Natale, P.2    Vicente, M.3
  • 76
    • 84888872850 scopus 로고    scopus 로고
    • Interactions among the early Escherichia coli divisome proteins revealed by bimolecular fluorescence complementation.
    • Pazos, M., Natale, P., Margolin, W., and Vicente, M. (2013b). Interactions among the early Escherichia coli divisome proteins revealed by bimolecular fluorescence complementation. Environ. Microbiol. 15, 3282-3291. doi: 10.1111/1462-2920.12225
    • (2013) Environ. Microbiol. , vol.15 , pp. 3282-3291
    • Pazos, M.1    Natale, P.2    Margolin, W.3    Vicente, M.4
  • 77
    • 84924531244 scopus 로고    scopus 로고
    • The bypass of ZipA by overexpression of FtsN requires a previously unknown conserved FtsN motif essential for FtsA-FtsN interaction supporting a model in which FtsA monomers recruit late cell division proteins to the Z ring
    • Pichoff, S., Du, S., and Lutkenhaus, J. (2014). The bypass of ZipA by overexpression of FtsN requires a previously unknown conserved FtsN motif essential for FtsA-FtsN interaction supporting a model in which FtsA monomers recruit late cell division proteins to the Z ring. Mol. Microbiol. 95, 971-981. doi: 10.1111/mmi.12907
    • (2014) Mol. Microbiol , vol.95 , pp. 971-981
    • Pichoff, S.1    Du, S.2    Lutkenhaus, J.3
  • 78
    • 84155167132 scopus 로고    scopus 로고
    • FtsA mutants impaired for self-interaction bypass ZipA suggesting a model in which FtsA's self-interaction competes with its ability to recruit downstream division proteins
    • Pichoff, S., Shen, B., Sullivan, B., and Lutkenhaus, J. (2012). FtsA mutants impaired for self-interaction bypass ZipA suggesting a model in which FtsA's self-interaction competes with its ability to recruit downstream division proteins. Mol. Microbiol. 83, 151-167. doi: 10.1111/j.1365-2958.2011.07923.x
    • (2012) Mol. Microbiol , vol.83 , pp. 151-167
    • Pichoff, S.1    Shen, B.2    Sullivan, B.3    Lutkenhaus, J.4
  • 79
    • 4444297890 scopus 로고    scopus 로고
    • Structural determinants required to target penicillin-binding protein 3 to the septum of Escherichia coli
    • Piette, A., Fraipont, C., den Blaauwen, T., Aarsman, M. E. G., Pastoret, S., and Nguyen-Distèche, M. (2004). Structural determinants required to target penicillin-binding protein 3 to the septum of Escherichia coli. J. Bacteriol. 186, 6110-6117. doi: 10.1128/JB.186.18.6110-6117.2004
    • (2004) J. Bacteriol , vol.186 , pp. 6110-6117
    • Piette, A.1    Fraipont, C.2    den Blaauwen, T.3    Aarsman, M.E.G.4    Pastoret, S.5    Nguyen-Distèche, M.6
  • 80
    • 0025074816 scopus 로고
    • The native form of FtsA, a septal protein of Escherichia coli, is located in the cytoplasmic membrane
    • Pla, J., Dopazo, A., and Vicente, M. (1990). The native form of FtsA, a septal protein of Escherichia coli, is located in the cytoplasmic membrane. J. Bacteriol. 172, 5097-5102.
    • (1990) J. Bacteriol , vol.172 , pp. 5097-5102
    • Pla, J.1    Dopazo, A.2    Vicente, M.3
  • 81
    • 0031018531 scopus 로고    scopus 로고
    • Inactivation of FtsI 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., and Beckwith, J. (1997). Inactivation of FtsI inhibits constriction of the FtsZ cytokinetic ring and delays the assembly of FtsZ rings at potential division sites. Proc. Natl. Acad. Sci. U.S.A. 94, 559-564. doi: 10.1073/pnas.94.2.559
    • (1997) Proc. Natl. Acad. Sci. U.S.A , vol.94 , pp. 559-564
    • Pogliano, J.1    Pogliano, K.2    Weiss, D.S.3    Losick, R.4    Beckwith, J.5
  • 82
    • 77954375639 scopus 로고    scopus 로고
    • Septal and lateral wall localization of PBP5, the major D, D-carboxypeptidase of Escherichia coli, requires substrate recognition and membrane attachment
    • Potluri, L., Karczmarek, A., Verheul, J., Piette, A., Wilkin, J.-M., Werth, N., et al. (2010). Septal and lateral wall localization of PBP5, the major D, D-carboxypeptidase of Escherichia coli, requires substrate recognition and membrane attachment. Mol. Microbiol. 77, 300-323. doi: 10.1111/j.1365-2958.2010.07205.x
    • (2010) Mol. Microbiol , vol.77 , pp. 300-323
    • Potluri, L.1    Karczmarek, A.2    Verheul, J.3    Piette, A.4    Wilkin, J.-M.5    Werth, N.6
  • 83
    • 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., and de Boer, P. A. (1997). The MinE ring: an FtsZ-independent cell structure required for selection of the correct division site in E. coli. Cell 91, 685-694. doi: 10.1016/S0092-8674(00)80455-9
    • (1997) Cell , vol.91 , pp. 685-694
    • Raskin, D.M.1    de Boer, P.A.2
  • 84
    • 0032743092 scopus 로고    scopus 로고
    • MinDE-dependent pole-to-pole oscillation of division inhibitor MinC in Escherichia coli.
    • Raskin, D. M., and de Boer, P. A. (1999a). MinDE-dependent pole-to-pole oscillation of division inhibitor MinC in Escherichia coli. J. Bacteriol. 181, 6419-6424.
    • (1999) J. Bacteriol. , vol.181 , pp. 6419-6424
    • Raskin, D.M.1    de Boer, P.A.2
  • 85
    • 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., and de Boer, P. A. (1999b). Rapid pole-to-pole oscillation of a protein required for directing division to the middle of Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 96, 4971-4976. doi: 10.1073/pnas.96.9.4971
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 4971-4976
    • Raskin, D.M.1    de Boer, P.A.2
  • 86
    • 84880563030 scopus 로고    scopus 로고
    • In the beginning Escherichia coli assembled the proto-ring: an initial phase of division
    • Rico, A. I., Krupka, M., and Vicente, M. (2013). In the beginning Escherichia coli assembled the proto-ring: an initial phase of division. J. Biol. Chem. 288, 20830-20836. doi: 10.1074/jbc.R113.479519
    • (2013) J. Biol. Chem , vol.288 , pp. 20830-20836
    • Rico, A.I.1    Krupka, M.2    Vicente, M.3
  • 87
    • 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., and Mingorance, J. (2003). Concentration and assembly of the division ring proteins FtsZ, FtsA, and ZipA during the Escherichia coli cell cycle. J. Bacteriol. 185, 3344-3351. doi: 10.1128/JB.185.11.3344-3351.2003
    • (2003) J. Bacteriol , vol.185 , pp. 3344-3351
    • Rueda, S.1    Vicente, M.2    Mingorance, J.3
  • 88
    • 55749095406 scopus 로고    scopus 로고
    • Bioinformatics identification of MurJ (MviN) as the peptidoglycan lipid II flippase in Escherichia coli
    • Ruiz, N. (2008). Bioinformatics identification of MurJ (MviN) as the peptidoglycan lipid II flippase in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 105, 15553-15557. doi: 10.1073/pnas.0808352105
    • (2008) Proc. Natl. Acad. Sci. U.S.A , vol.105 , pp. 15553-15557
    • Ruiz, N.1
  • 89
    • 84902153114 scopus 로고    scopus 로고
    • Crystal structure of penicillin-binding protein 3 (PBP3) from Escherichia coli.
    • Sauvage, E., Derouaux, A., Fraipont, C., Joris, M., Herman, R., Rocaboy, M., et al. (2014). Crystal structure of penicillin-binding protein 3 (PBP3) from Escherichia coli. PLoS ONE 9:e98042. doi: 10.1371/journal.pone.0098042
    • (2014) PLoS ONE , vol.9
    • Sauvage, E.1    Derouaux, A.2    Fraipont, C.3    Joris, M.4    Herman, R.5    Rocaboy, M.6
  • 90
    • 84863205849 scopus 로고    scopus 로고
    • NIH Image to ImageJ: 25 years of image analysis
    • Schneider, C. A., Rasband, W. S., and Eliceiri, K. W. (2012). NIH Image to ImageJ: 25 years of image analysis. Nat. Chem. Biol. 9, 671-675. doi: 10.1038/nmeth.2089
    • (2012) Nat. Chem. Biol , vol.9 , pp. 671-675
    • Schneider, C.A.1    Rasband, W.S.2    Eliceiri, K.W.3
  • 91
    • 84904097466 scopus 로고    scopus 로고
    • Bacterial cell wall. MurJ is the flippase of lipid-linked precursors for peptidoglycan biogenesis.
    • Sham, L.-T., Butler, E. K., Lebar, M. D., Kahne, D., Bernhardt, T. G., and Ruiz, N. (2014). Bacterial cell wall. MurJ is the flippase of lipid-linked precursors for peptidoglycan biogenesis. Science 345, 220-222. doi: 10.1126/science.1254522
    • (2014) Science , vol.345 , pp. 220-222
    • Sham, L.-T.1    Butler, E.K.2    Lebar, M.D.3    Kahne, D.4    Bernhardt, T.G.5    Ruiz, N.6
  • 92
    • 0036646101 scopus 로고    scopus 로고
    • Division site placement in E.coli: mutations that prevent formation of the MinE ring lead to loss of the normal midcell arrest of growth of polar MinD membrane domains
    • Shih, Y.-L., Fu, X., King, G. F., Le, T., and Rothfield, L. (2002). Division site placement in E.coli: mutations that prevent formation of the MinE ring lead to loss of the normal midcell arrest of growth of polar MinD membrane domains. EMBO J. 21, 3347-3357. doi: 10.1093/emboj/cdf323
    • (2002) EMBO J , vol.21 , pp. 3347-3357
    • Shih, Y.-L.1    Fu, X.2    King, G.F.3    Le, T.4    Rothfield, L.5
  • 93
    • 0030064119 scopus 로고    scopus 로고
    • Control of cell division in Escherichia coli: regulation of transcription of ftsQA involves both rpoS and SdiA-mediated autoinduction
    • Sitnikov, D. M., Schineller, J. B., and Baldwin, T. O. (1996). Control of cell division in Escherichia coli: regulation of transcription of ftsQA involves both rpoS and SdiA-mediated autoinduction. Proc. Natl. Acad. Sci. U.S.A. 93, 336-341. doi: 10.1073/pnas.93.1.336
    • (1996) Proc. Natl. Acad. Sci. U.S.A , vol.93 , pp. 336-341
    • Sitnikov, D.M.1    Schineller, J.B.2    Baldwin, T.O.3
  • 94
    • 84857375148 scopus 로고    scopus 로고
    • The Escherichia coli cell division protein ZipA forms homodimers prior to association with FtsZ.
    • Skoog, K., and Daley, D. O. (2012). The Escherichia coli cell division protein ZipA forms homodimers prior to association with FtsZ. Biochemistry 51, 1407-1415. doi: 10.1021/bi2015647
    • (2012) Biochemistry , vol.51 , pp. 1407-1415
    • Skoog, K.1    Daley, D.O.2
  • 95
    • 34247495145 scopus 로고    scopus 로고
    • FtsZ polymer-bundling by the Escherichia coli ZapA orthologue, YgfE, involves a conformational change in bound GTP
    • Small, E., Marrington, R., Rodger, A., Scott, D. J., Sloan, K., Roper, D., et al. (2007). FtsZ polymer-bundling by the Escherichia coli ZapA orthologue, YgfE, involves a conformational change in bound GTP. J. Mol. Biol. 369, 210-221. doi: 10.1016/j.jmb.2007.03.025
    • (2007) J. Mol. Biol , vol.369 , pp. 210-221
    • Small, E.1    Marrington, R.2    Rodger, A.3    Scott, D.J.4    Sloan, K.5    Roper, D.6
  • 96
    • 0037022642 scopus 로고    scopus 로고
    • Rapid assembly dynamics of the Escherichia coli FtsZ-ring demonstrated by fluorescence recovery after photobleaching
    • Stricker, J., Maddox, P., Salmon, E. D., and Erickson, H. P. (2002). Rapid assembly dynamics of the Escherichia coli FtsZ-ring demonstrated by fluorescence recovery after photobleaching. Proc. Natl. Acad. Sci. U.S.A. 99, 3171-3175. doi: 10.1073/pnas.052595099
    • (2002) Proc. Natl. Acad. Sci. U.S.A , vol.99 , pp. 3171-3175
    • Stricker, J.1    Maddox, P.2    Salmon, E.D.3    Erickson, H.P.4
  • 97
    • 0034751570 scopus 로고    scopus 로고
    • The dimerization function of MinC resides in a structurally autonomous C-terminal domain
    • Szeto, T. H., Rowland, S. L., and King, G. F. (2001). The dimerization function of MinC resides in a structurally autonomous C-terminal domain. J. Bacteriol. 183, 6684-6687. doi: 10.1128/JB.183.22.6684-6687.2001
    • (2001) J. Bacteriol , vol.183 , pp. 6684-6687
    • Szeto, T.H.1    Rowland, S.L.2    King, G.F.3
  • 98
    • 84861151969 scopus 로고    scopus 로고
    • FtsA forms actin-like protofilaments
    • Szwedziak, P., Wang, Q., Freund, S. M. V., and Löwe, J. (2012). FtsA forms actin-like protofilaments. EMBO J. 31, 2249-2260. doi: 10.1038/emboj.2012.76
    • (2012) EMBO J , vol.31 , pp. 2249-2260
    • Szwedziak, P.1    Wang, Q.2    Freund, S.M.V.3    Löwe, J.4
  • 100
    • 0023992940 scopus 로고
    • Division behavior and shape changes in isogenic ftsZ, ftsQ, ftsA, pbpB, and ftsE cell division mutants of Escherichia coli during temperature shift experiments
    • Taschner, P. E., Huls, P. G., Pas, E., and Woldringh, C. L. (1988). Division behavior and shape changes in isogenic ftsZ, ftsQ, ftsA, pbpB, and ftsE cell division mutants of Escherichia coli during temperature shift experiments. J. Bacteriol. 170, 1533-1540.
    • (1988) J. Bacteriol , vol.170 , pp. 1533-1540
    • Taschner, P.E.1    Huls, P.G.2    Pas, E.3    Woldringh, C.L.4
  • 101
    • 84924577747 scopus 로고    scopus 로고
    • A role for the FtsQLB complex in cytokinetic ring activation revealed by an ftsL allele that accelerates division
    • Tsang, M.-J., and Bernhardt, T. G. (2015). A role for the FtsQLB complex in cytokinetic ring activation revealed by an ftsL allele that accelerates division. Mol. Microbiol. 95, 925-944. doi: 10.1111/mmi.12905
    • (2015) Mol. Microbiol , vol.95 , pp. 925-944
    • Tsang, M.-J.1    Bernhardt, T.G.2
  • 102
    • 78650431707 scopus 로고    scopus 로고
    • Regulation of peptidoglycan synthesis by outer-membrane proteins.
    • Typas, A., Banzhaf, M., van den Berg van Saparoea, B., Verheul, J., Biboy, J., Nichols, R. J., et al. (2010). Regulation of peptidoglycan synthesis by outer-membrane proteins. Cell 143, 1097-1109. doi: 10.1016/j.cell.2010.11.038
    • (2010) Cell , vol.143 , pp. 1097-1109
    • Typas, A.1    Banzhaf, M.2    van den Berg van Saparoea, B.3    Verheul, J.4    Biboy, J.5    Nichols, R.J.6
  • 103
    • 4944223117 scopus 로고    scopus 로고
    • Murein (peptidoglycan) binding property of the essential cell division protein FtsN from Escherichia coli
    • Ursinus, A., van den Ent, F., Brechtel, S., de Pedro, M., Höltje, J.-V., Löwe, J., et al. (2004). Murein (peptidoglycan) binding property of the essential cell division protein FtsN from Escherichia coli. J. Bacteriol. 186, 6728-6737. doi: 10.1128/JB.186.20.6728-6737.2004
    • (2004) J. Bacteriol , vol.186 , pp. 6728-6737
    • Ursinus, A.1    van den Ent, F.2    Brechtel, S.3    de Pedro, M.4    Höltje, J.-V.5    Löwe, J.6
  • 104
    • 84883136544 scopus 로고    scopus 로고
    • Fine mapping the contact sites of Escherichia coli cell division proteins FtsB and FtsL on FtsQ protein
    • van den Berg van Saparoea, H. B., Glas, M., Vernooij, I. G. W. H., Bitter, W., den Blaauwen, T., and Luirink, J. (2013). Fine mapping the contact sites of Escherichia coli cell division proteins FtsB and FtsL on FtsQ protein. J. Biol. Chem. 288, 24340-24350. doi: 10.1074/jbc.M113.485888
    • (2013) J. Biol. Chem , vol.288 , pp. 24340-24350
    • van den Berg van Saparoea, H.B.1    Glas, M.2    Vernooij, I.G.W.H.3    Bitter, W.4    den Blaauwen, T.5    Luirink, J.6
  • 105
    • 84874214695 scopus 로고    scopus 로고
    • Colocalization and interaction between elongasome and divisome during a preparative cell division phase in Escherichia coli
    • van der Ploeg, R., Verheul, J., Vischer, N. O. E., Alexeeva, S., Hoogendoorn, E., Postma, M., et al. (2013). Colocalization and interaction between elongasome and divisome during a preparative cell division phase in Escherichia coli. Mol. Microbiol. 87, 1074-1087. doi: 10.1111/mmi.12150
    • (2013) Mol. Microbiol , vol.87 , pp. 1074-1087
    • van der Ploeg, R.1    Verheul, J.2    Vischer, N.O.E.3    Alexeeva, S.4    Hoogendoorn, E.5    Postma, M.6
  • 106
    • 62949149564 scopus 로고    scopus 로고
    • Assembly of the MreB-associated cytoskeletal ring of Escherichia coli
    • Vats, P., Shih, Y.-L., and Rothfield, L. (2009). Assembly of the MreB-associated cytoskeletal ring of Escherichia coli. Mol. Microbiol. 72, 170-182. doi: 10.1111/j.1365-2958.2009.06632.x
    • (2009) Mol. Microbiol , vol.72 , pp. 170-182
    • Vats, P.1    Shih, Y.-L.2    Rothfield, L.3
  • 107
    • 78650972239 scopus 로고    scopus 로고
    • Self-organized partitioning of dynamically localized proteins in bacterial cell division
    • Ventura, B. D., and Sourjik, V. (2011). Self-organized partitioning of dynamically localized proteins in bacterial cell division. Mol. Syst. Biol. 7, 1-13. doi: 10.1038/msb.2010.111
    • (2011) Mol. Syst. Biol , vol.7 , pp. 1-13
    • Ventura, B.D.1    Sourjik, V.2
  • 108
    • 0031895073 scopus 로고    scopus 로고
    • Regulation of transcription of cell division genes in the Escherichia coli dcw cluster.
    • Vicente, M., Gomez, M. J., and Ayala, J. A. (1998). Regulation of transcription of cell division genes in the Escherichia coli dcw cluster. Cell Mol. Life Sci. 54, 317-324 doi: 10.1007/s000180050158
    • (1998) Cell Mol. Life Sci. , vol.54 , pp. 317-324
    • Vicente, M.1    Gomez, M.J.2    Ayala, J.A.3
  • 109
    • 0023638691 scopus 로고
    • Mutant isolation and molecular cloning of mre genes, which determine cell shape, sensitivity to mecillinam, and amount of penicillin-binding proteins in Escherichia coli
    • Wachi, M., Doi, M., Tamaki, S., Park, W., Nakajima-Iijima, S., and Matsuhashi, M. (1987). Mutant isolation and molecular cloning of mre genes, which determine cell shape, sensitivity to mecillinam, and amount of penicillin-binding proteins in Escherichia coli. J. Bacteriol. 169, 4935-4940.
    • (1987) J. Bacteriol , vol.169 , pp. 4935-4940
    • Wachi, M.1    Doi, M.2    Tamaki, S.3    Park, W.4    Nakajima-Iijima, S.5    Matsuhashi, M.6
  • 110
    • 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., and Lutkenhaus, J. (1998). FtsK is an essential cell division protein that is localized to the septum and induced as part of the SOS response. Mol. Microbiol. 29, 731-740. doi: 10.1046/j.1365-2958.1998.00958.x
    • (1998) Mol. Microbiol , vol.29 , pp. 731-740
    • Wang, L.1    Lutkenhaus, J.2
  • 111
    • 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., and Beckwith, J. (1999). Localization of FtsI (PBP3) to the septal ring requires its membrane anchor, the Z ring, FtsA, FtsQ, and FtsL. J. Bacteriol. 181, 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
  • 112
    • 77951608842 scopus 로고    scopus 로고
    • Positioning cell wall synthetic complexes by the bacterial morphogenetic proteins MreB and MreD
    • White, C. L., Kitich, A., and Gober, J. W. (2010). Positioning cell wall synthetic complexes by the bacterial morphogenetic proteins MreB and MreD. Mol. Microbiol. 76, 616-633. doi: 10.1111/j.1365-2958.2010.07108.x
    • (2010) Mol. Microbiol , vol.76 , pp. 616-633
    • White, C.L.1    Kitich, A.2    Gober, J.W.3
  • 113
    • 0024381715 scopus 로고
    • Rate and topography of peptidoglycan synthesis during cell division in Escherichia coli: concept of a leading edge
    • Wientjes, F. B., and Nanninga, N. (1989). Rate and topography of peptidoglycan synthesis during cell division in Escherichia coli: concept of a leading edge. J. Bacteriol. 171, 3412-3419.
    • (1989) J. Bacteriol , vol.171 , pp. 3412-3419
    • Wientjes, F.B.1    Nanninga, N.2
  • 114
    • 73849087355 scopus 로고    scopus 로고
    • Update on the Keio collection of Escherichia coli single-gene deletion mutants
    • Yamamoto, N., Nakahigashi, K., Nakamichi, T., Yoshino, M., Takai, Y., Touda, Y., et al. (2009). Update on the Keio collection of Escherichia coli single-gene deletion mutants. Mol. Syst. Biol. 5, 335. doi: 10.1038/msb.2009.92
    • (2009) Mol. Syst. Biol , vol.5 , pp. 335
    • Yamamoto, N.1    Nakahigashi, K.2    Nakamichi, T.3    Yoshino, M.4    Takai, Y.5    Touda, Y.6
  • 115
    • 0034643273 scopus 로고    scopus 로고
    • A conserved residue at the extreme C-terminus of FtsZ is critical for the FtsA-FtsZ interaction in Staphylococcus aureus
    • Yan, K., Pearce, K. H., and Payne, D. J. (2000). A conserved residue at the extreme C-terminus of FtsZ is critical for the FtsA-FtsZ interaction in Staphylococcus aureus. Biochem. Biophys. Res. Commun. 270, 387-392. doi: 10.1006/bbrc.2000.2439
    • (2000) Biochem. Biophys. Res. Commun , vol.270 , pp. 387-392
    • Yan, K.1    Pearce, K.H.2    Payne, D.J.3
  • 116
    • 2442631494 scopus 로고    scopus 로고
    • Solution structure and domain architecture of the divisome protein FtsN
    • Yang, J.-C., van den Ent, F., Neuhaus, D., Brevier, J., and Löwe, J. (2004). Solution structure and domain architecture of the divisome protein FtsN. Mol. Microbiol. 52, 651-660. doi: 10.1111/j.1365-2958.2004.03991.x
    • (2004) Mol. Microbiol , vol.52 , pp. 651-660
    • Yang, J.-C.1    van den Ent, F.2    Neuhaus, D.3    Brevier, J.4    Löwe, J.5
  • 117
    • 0025990145 scopus 로고
    • Penicillin-binding protein 1B of Escherichia coli exists in dimeric forms
    • Zijderveld, C. A., Aarsman, M. E., den Blaauwen, T., and Nanninga, N. (1991). Penicillin-binding protein 1B of Escherichia coli exists in dimeric forms. J. Bacteriol. 173, 5740-5746.
    • (1991) J. Bacteriol , vol.173 , pp. 5740-5746
    • Zijderveld, C.A.1    Aarsman, M.E.2    den Blaauwen, T.3    Nanninga, N.4


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