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Volumn 15, Issue 12, 2013, Pages 3169-3182

The Escherichia coli divisome: Born to divide

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 84888864453     PISSN: 14622912     EISSN: 14622920     Source Type: Journal    
DOI: 10.1111/1462-2920.12227     Document Type: Short Survey
Times cited : (28)

References (160)
  • 2
    • 0029806478 scopus 로고    scopus 로고
    • FtsZ-spirals and -arcs determine the shape of the invaginating septa in some mutants of Escherichia coli
    • Addinall, S.G., and Lutkenhaus, J. (1996) FtsZ-spirals and -arcs determine the shape of the invaginating septa in some mutants of Escherichia coli. Mol Microbiol 22: 231-237.
    • (1996) Mol Microbiol , vol.22 , pp. 231-237
    • Addinall, S.G.1    Lutkenhaus, J.2
  • 3
    • 0030856502 scopus 로고    scopus 로고
    • FtsN, a late recruit to the septum in Escherichia coli
    • Addinall, S.G., Cao, C., and Lutkenhaus, J. (1997) FtsN, a late recruit to the septum in Escherichia coli. Mol Microbiol 25: 303-309.
    • (1997) Mol Microbiol , vol.25 , pp. 303-309
    • Addinall, S.G.1    Cao, C.2    Lutkenhaus, J.3
  • 5
    • 0026757024 scopus 로고
    • Cell division in Escherichia coli minB mutants
    • Akerlund, T., Bernander, R., and Nordström, K. (1992) Cell division in Escherichia coli minB mutants. Mol Microbiol 6: 2073-2083.
    • (1992) Mol Microbiol , vol.6 , pp. 2073-2083
    • Akerlund, T.1    Bernander, R.2    Nordström, K.3
  • 6
    • 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., Jr, 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.
    • (2010) Mol Microbiol , vol.77 , pp. 384-398
    • Alexeeva, S.1    Gadella Jr, T.W.2    Verheul, J.3    Verhoeven, G.S.4    den Blaauwen, T.5
  • 7
    • 67549107869 scopus 로고    scopus 로고
    • ATP-binding site lesions in FtsE impair cell division
    • Arends, S.J., Kustusch, R.J., and Weiss, D.S. (2009) ATP-binding site lesions in FtsE impair cell division. J Bacteriol 191: 3772-3784.
    • (2009) J Bacteriol , vol.191 , pp. 3772-3784
    • Arends, S.J.1    Kustusch, R.J.2    Weiss, D.S.3
  • 8
    • 84869467537 scopus 로고    scopus 로고
    • Surface topology engineering of membranes for the mechanical investigation of the tubulin homologue FtsZ
    • Arumugam, S., Chwastek, G., Fischer-Friedrich, E., Ehrig, C., Monch, I., and Schwille, P. (2012) Surface topology engineering of membranes for the mechanical investigation of the tubulin homologue FtsZ. Angew Chem Int Ed Engl 51: 11858-11862.
    • (2012) Angew Chem Int Ed Engl , vol.51 , pp. 11858-11862
    • Arumugam, S.1    Chwastek, G.2    Fischer-Friedrich, E.3    Ehrig, C.4    Monch, I.5    Schwille, P.6
  • 9
    • 0024094022 scopus 로고
    • Cloning and characterization of Bacillus subtilis homologs of Escherichia coli cell division genes ftsZ and ftsA
    • Beall, B., Lowe, M., and Lutkenhaus, J. (1988) Cloning and characterization of Bacillus subtilis homologs of Escherichia coli cell division genes ftsZ and ftsA. J Bacteriol 170: 4855-4864.
    • (1988) J Bacteriol , vol.170 , pp. 4855-4864
    • Beall, B.1    Lowe, M.2    Lutkenhaus, J.3
  • 10
    • 0025608737 scopus 로고
    • The balance between different peptidoglycan precursors determines whether Escherichia coli cells will elongate or divide
    • Begg, K.J., Takasuga, A., Edwards, D.H., Dewar, S.J., Spratt, B.G., Adachi, H., etal. (1990) The balance between different peptidoglycan precursors determines whether Escherichia coli cells will elongate or divide. J Bacteriol 172: 6697-6703.
    • (1990) J Bacteriol , vol.172 , pp. 6697-6703
    • Begg, K.J.1    Takasuga, A.2    Edwards, D.H.3    Dewar, S.J.4    Spratt, B.G.5    Adachi, H.6
  • 11
  • 12
    • 0026059127 scopus 로고
    • FtsZ ring structure associated with division in Escherichia coli
    • Bi, E.F., and Lutkenhaus, J. (1991) FtsZ ring structure associated with division in Escherichia coli. Nature 354: 161-164.
    • (1991) Nature , vol.354 , pp. 161-164
    • Bi, E.F.1    Lutkenhaus, J.2
  • 13
    • 8544255518 scopus 로고    scopus 로고
    • FtsK activities in Xer recombination, DNA mobilization and cell division involve overlapping and separate domains of the protein
    • Bigot, S., Corre, J., Louarn, J.M., Cornet, F., and Barre, F.X. (2004) FtsK activities in Xer recombination, DNA mobilization and cell division involve overlapping and separate domains of the protein. Mol Microbiol 54: 876-886.
    • (2004) Mol Microbiol , vol.54 , pp. 876-886
    • Bigot, S.1    Corre, J.2    Louarn, J.M.3    Cornet, F.4    Barre, F.X.5
  • 14
    • 27744459076 scopus 로고    scopus 로고
    • KOPS: DNA motifs that control E. coli chromosome segregation by orienting the FtsK translocase
    • Bigot, S., Saleh, O.A., Lesterlin, C., Pages, C., El Karoui, M., Dennis, C., etal. (2005) KOPS: DNA motifs that control E. coli chromosome segregation by orienting the FtsK translocase. EMBO J 24: 3770-3780.
    • (2005) EMBO J , vol.24 , pp. 3770-3780
    • Bigot, S.1    Saleh, O.A.2    Lesterlin, C.3    Pages, C.4    El Karoui, M.5    Dennis, C.6
  • 15
    • 70449576026 scopus 로고    scopus 로고
    • The Bacillus subtilis SftA (YtpS) and SpoIIIE DNA translocases play distinct roles in growing cells to ensure faithful chromosome partitioning
    • Biller, S.J., and Burkholder, W.F. (2009) The Bacillus subtilis SftA (YtpS) and SpoIIIE DNA translocases play distinct roles in growing cells to ensure faithful chromosome partitioning. Mol Microbiol 74: 790-809.
    • (2009) Mol Microbiol , vol.74 , pp. 790-809
    • Biller, S.J.1    Burkholder, W.F.2
  • 18
    • 79960562614 scopus 로고    scopus 로고
    • Identification of a novel function for the FtsL cell division protein from Escherichia coli K12
    • Blencowe, D.K., Al Jubori, S., and Morby, A.P. (2011) Identification of a novel function for the FtsL cell division protein from Escherichia coli K12. Biochem Biophys Res Commun 411: 44-49.
    • (2011) Biochem Biophys Res Commun , vol.411 , pp. 44-49
    • Blencowe, D.K.1    Al Jubori, S.2    Morby, A.P.3
  • 19
    • 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.
    • (1989) Cell , vol.56 , pp. 641-649
    • de Boer, P.A.1    Crossley, R.E.2    Rothfield, L.I.3
  • 20
    • 37349090734 scopus 로고    scopus 로고
    • The ATPase SpoIIIE transports DNA across fused septal membranes during sporulation in Bacillus subtilis
    • Burton, B.M., Marquis, K.A., Sullivan, N.L., Rapoport, T.A., and Rudner, D.Z. (2007) The ATPase SpoIIIE transports DNA across fused septal membranes during sporulation in Bacillus subtilis. Cell 131: 1301-1312.
    • (2007) Cell , vol.131 , pp. 1301-1312
    • Burton, B.M.1    Marquis, K.A.2    Sullivan, N.L.3    Rapoport, T.A.4    Rudner, D.Z.5
  • 21
    • 84861204197 scopus 로고    scopus 로고
    • The early divisome protein FtsA interacts directly through its 1c subdomain with the cytoplasmic domain of the late divisome protein FtsN
    • Busiek, K.K., Eraso, J.M., Wang, Y., and Margolin, W. (2012) The early divisome protein FtsA interacts directly through its 1c subdomain with the cytoplasmic domain of the late divisome protein FtsN. J Bacteriol 194: 1989-2000.
    • (2012) J Bacteriol , vol.194 , pp. 1989-2000
    • Busiek, K.K.1    Eraso, J.M.2    Wang, Y.3    Margolin, W.4
  • 22
    • 84859484529 scopus 로고    scopus 로고
    • Extreme C terminus of bacterial cytoskeletal protein FtsZ plays fundamental role in assembly independent of modulatory proteins
    • Buske, P.J., and Levin, P.A. (2012) Extreme C terminus of bacterial cytoskeletal protein FtsZ plays fundamental role in assembly independent of modulatory proteins. J Biol Chem 287: 10945-10957.
    • (2012) J Biol Chem , vol.287 , pp. 10945-10957
    • Buske, P.J.1    Levin, P.A.2
  • 23
    • 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 USA 106: 10614-10619.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 10614-10619
    • Camberg, J.L.1    Hoskins, J.R.2    Wickner, S.3
  • 24
    • 84856666861 scopus 로고    scopus 로고
    • Oriented imaging of 3D subcellular structures in bacterial cells using optical tweezers
    • Carmon, G., Fishov, I., and Feingold, M. (2012) Oriented imaging of 3D subcellular structures in bacterial cells using optical tweezers. Opt Lett 37: 440-442.
    • (2012) Opt Lett , vol.37 , pp. 440-442
    • Carmon, G.1    Fishov, I.2    Feingold, M.3
  • 25
    • 0034740520 scopus 로고    scopus 로고
    • FtsQ, FtsL and FtsI require FtsK, but not FtsN, for co-localization with FtsZ during Escherichia coli cell division
    • Chen, J.C., and Beckwith, J. (2001) FtsQ, FtsL and FtsI require FtsK, but not FtsN, for co-localization with FtsZ during Escherichia coli cell division. Mol Microbiol 42: 395-413.
    • (2001) Mol Microbiol , vol.42 , pp. 395-413
    • Chen, J.C.1    Beckwith, J.2
  • 26
    • 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., and Beckwith, J. (1999) Septal localization of FtsQ, an essential cell division protein in Escherichia coli. J Bacteriol 181: 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
  • 27
    • 84874784097 scopus 로고    scopus 로고
    • Identification of the SlmA active site responsible for blocking bacterial cytokinetic ring assembly over the chromosome
    • Cho, H., and Bernhardt, T.G. (2013) Identification of the SlmA active site responsible for blocking bacterial cytokinetic ring assembly over the chromosome. PLoS Genet 9: e1003304.
    • (2013) PLoS Genet , vol.9
    • Cho, H.1    Bernhardt, T.G.2
  • 28
    • 79952741894 scopus 로고    scopus 로고
    • Nucleoid occlusion factor SlmA is a DNA-activated FtsZ polymerization antagonist
    • Cho, H., McManus, H.R., Dove, S.L., and Bernhardt, T.G. (2011) Nucleoid occlusion factor SlmA is a DNA-activated FtsZ polymerization antagonist. Proc Natl Acad Sci USA 108: 3773-3778.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 3773-3778
    • Cho, H.1    McManus, H.R.2    Dove, S.L.3    Bernhardt, T.G.4
  • 29
    • 84869868586 scopus 로고    scopus 로고
    • Superresolution microscopy for microbiology
    • Coltharp, C., and Xiao, J. (2012) Superresolution microscopy for microbiology. Cell Microbiol 14: 1808-1818.
    • (2012) Cell Microbiol , vol.14 , pp. 1808-1818
    • Coltharp, C.1    Xiao, J.2
  • 30
    • 7744230898 scopus 로고    scopus 로고
    • Z-ring-independent interaction between a subdomain of FtsA and late septation proteins as revealed by a polar recruitment assay
    • Corbin, B.D., Geissler, B., Sadasivam, M., and Margolin, W. (2004) Z-ring-independent interaction between a subdomain of FtsA and late septation proteins as revealed by a polar recruitment assay. J Bacteriol 186: 7736.
    • (2004) J Bacteriol , vol.186 , pp. 7736
    • Corbin, B.D.1    Geissler, B.2    Sadasivam, M.3    Margolin, W.4
  • 31
    • 34247859209 scopus 로고    scopus 로고
    • Interaction between cell division proteins FtsE and FtsZ
    • Corbin, B.D., Wang, Y., Beuria, T.K., and Margolin, W. (2007) Interaction between cell division proteins FtsE and FtsZ. J Bacteriol 189: 3026-3035.
    • (2007) J Bacteriol , vol.189 , pp. 3026-3035
    • Corbin, B.D.1    Wang, Y.2    Beuria, T.K.3    Margolin, W.4
  • 33
    • 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., and Lutkenhaus, J. (1993) Cloning and characterization of ftsN, an essential cell division gene in Escherichia coli isolated as a multicopy suppressor of ftsA12(Ts). J Bacteriol 175: 3790-3797.
    • (1993) J Bacteriol , vol.175 , pp. 3790-3797
    • Dai, K.1    Xu, Y.2    Lutkenhaus, J.3
  • 34
  • 36
    • 39749105962 scopus 로고    scopus 로고
    • The monofunctional glycosyltransferase of Escherichia coli localizes to the cell division site and interacts with penicillin-binding protein 3, FtsW, and FtsN
    • Derouaux, A., Wolf, B., Fraipont, C., Breukink, E., Nguyen-Distèche, M., and Terrak, M. (2008) The monofunctional glycosyltransferase of Escherichia coli localizes to the cell division site and interacts with penicillin-binding protein 3, FtsW, and FtsN. J Bacteriol 190: 1831-1834.
    • (2008) J Bacteriol , vol.190 , pp. 1831-1834
    • Derouaux, A.1    Wolf, B.2    Fraipont, C.3    Breukink, E.4    Nguyen-Distèche, M.5    Terrak, M.6
  • 37
    • 0034725994 scopus 로고    scopus 로고
    • Membrane topology of the N-terminus of the Escherichia coli FtsK division protein
    • Dorazi, R., and Dewar, S.J. (2000) Membrane topology of the N-terminus of the Escherichia coli FtsK division protein. FEBS Lett 478: 13-18.
    • (2000) FEBS Lett , vol.478 , pp. 13-18
    • Dorazi, R.1    Dewar, S.J.2
  • 38
  • 39
    • 84870388864 scopus 로고    scopus 로고
    • Molecular basis for a protein-mediated DNA-bridging mechanism that functions in condensation of the E. coli chromosome
    • Dupaigne, P., Tonthat, N.K., Espéli, O., Whitfill, T., Boccard, F., and Schumacher, M.A. (2012) Molecular basis for a protein-mediated DNA-bridging mechanism that functions in condensation of the E. coli chromosome. Mol Cell 48: 560-571.
    • (2012) Mol Cell , vol.48 , pp. 560-571
    • Dupaigne, P.1    Tonthat, N.K.2    Espéli, O.3    Whitfill, T.4    Boccard, F.5    Schumacher, M.A.6
  • 40
    • 84864018985 scopus 로고    scopus 로고
    • Identification of ZapD as a cell division factor that promotes the assembly of FtsZ in Escherichia coli
    • Durand-Heredia, J., Rivkin, E., Fan, G., Morales, J., and Janakiraman, A. (2012) Identification of ZapD as a cell division factor that promotes the assembly of FtsZ in Escherichia coli. J Bacteriol 194: 3189-3198.
    • (2012) J Bacteriol , vol.194 , pp. 3189-3198
    • Durand-Heredia, J.1    Rivkin, E.2    Fan, G.3    Morales, J.4    Janakiraman, A.5
  • 41
    • 79952403634 scopus 로고    scopus 로고
    • Identification and characterization of ZapC, a stabilizer of the FtsZ ring in Escherichia coli
    • Durand-Heredia, J.M., Yu, H.H., De Carlo, S., Lesser, C.F., and Janakiraman, A. (2011) Identification and characterization of ZapC, a stabilizer of the FtsZ ring in Escherichia coli. J Bacteriol 193: 1405-1413.
    • (2011) J Bacteriol , vol.193 , pp. 1405-1413
    • Durand-Heredia, J.M.1    Yu, H.H.2    De Carlo, S.3    Lesser, C.F.4    Janakiraman, A.5
  • 42
    • 84872856522 scopus 로고    scopus 로고
    • The physiology of bacterial cell division
    • Egan, A.J., and Vollmer, W. (2013) The physiology of bacterial cell division. Ann N Y Acad Sci 1277: 8-28.
    • (2013) Ann N Y Acad Sci , vol.1277 , pp. 8-28
    • Egan, A.J.1    Vollmer, W.2
  • 43
    • 84888875374 scopus 로고    scopus 로고
    • Tracking of individual freely diffusing fluorescent protein molecules in the bacterial cytoplasm. In ArXiv:10032110.
    • English, B.P., Sanamrad, A., Tankov, S., Hauryliuk, V., and Elf, J. (2010) Tracking of individual freely diffusing fluorescent protein molecules in the bacterial cytoplasm. In ArXiv:10032110.
    • (2010)
    • English, B.P.1    Sanamrad, A.2    Tankov, S.3    Hauryliuk, V.4    Elf, J.5
  • 45
    • 0034675921 scopus 로고    scopus 로고
    • Crystal structure of the cell division protein FtsA from Thermotoga maritima
    • van den Ent, F., and Löwe, J. (2000) Crystal structure of the cell division protein FtsA from Thermotoga maritima. EMBO J 19: 5300-5307.
    • (2000) EMBO J , vol.19 , pp. 5300-5307
    • van den Ent, F.1    Löwe, J.2
  • 46
    • 0035817819 scopus 로고    scopus 로고
    • Prokaryotic origin of the actin cytoskeleton
    • van den Ent, F., Amos, L.A., and Lowe, J. (2001) Prokaryotic origin of the actin cytoskeleton. Nature 413: 39-44.
    • (2001) Nature , vol.413 , pp. 39-44
    • van den Ent, F.1    Amos, L.A.2    Lowe, J.3
  • 48
    • 67249097621 scopus 로고    scopus 로고
    • Modeling the physics of FtsZ assembly and force generation
    • Erickson, H.P. (2009) Modeling the physics of FtsZ assembly and force generation. Proc Natl Acad Sci USA 106: 9238-9243.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 9238-9243
    • Erickson, H.P.1
  • 49
    • 78650078263 scopus 로고    scopus 로고
    • FtsZ in bacterial cytokinesis: cytoskeleton and force generator all in one
    • Erickson, H.P., Anderson, D.E., and Osawa, M. (2010) FtsZ in bacterial cytokinesis: cytoskeleton and force generator all in one. Microbiol Mol Biol Rev 74: 504-528.
    • (2010) Microbiol Mol Biol Rev , vol.74 , pp. 504-528
    • Erickson, H.P.1    Anderson, D.E.2    Osawa, M.3
  • 50
    • 0242582268 scopus 로고    scopus 로고
    • A physical and functional interaction between Escherichia coli FtsK and topoisomerase IV
    • Espéli, O., Lee, C., and Marians, K.J. (2003) A physical and functional interaction between Escherichia coli FtsK and topoisomerase IV. J Biol Chem 278: 44639-44644.
    • (2003) J Biol Chem , vol.278 , pp. 44639-44644
    • Espéli, O.1    Lee, C.2    Marians, K.J.3
  • 51
    • 84864147092 scopus 로고    scopus 로고
    • A MatP-divisome interaction coordinates chromosome segregation with cell division in E. coli
    • Espéli, O., Borne, R., Dupaigne, P., Thiel, A., Gigant, E., Mercier, R., and Boccard, F. (2012) A MatP-divisome interaction coordinates chromosome segregation with cell division in E. coli. EMBO J 31: 3198-3211.
    • (2012) EMBO J , vol.31 , pp. 3198-3211
    • Espéli, O.1    Borne, R.2    Dupaigne, P.3    Thiel, A.4    Gigant, E.5    Mercier, R.6    Boccard, F.7
  • 52
    • 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.
    • (2013) EMBO J , vol.32 , pp. 1953-1965
    • Fenton, A.K.1    Gerdes, K.2
  • 53
    • 77958525927 scopus 로고    scopus 로고
    • In vivo structure of the E. coli FtsZ-ring revealed by photoactivated localization microscopy (PALM)
    • Fu, G., Huang, T., Buss, J., Coltharp, C., Hensel, Z., and Xiao, J. (2010) In vivo structure of the E. coli FtsZ-ring revealed by photoactivated localization microscopy (PALM). PLoS ONE 5: e12682.
    • (2010) PLoS ONE , vol.5
    • Fu, G.1    Huang, T.2    Buss, J.3    Coltharp, C.4    Hensel, Z.5    Xiao, J.6
  • 54
    • 77953494296 scopus 로고    scopus 로고
    • Spatial resolution of two bacterial cell division proteins: ZapA recruits ZapB to the inner face of the Z-ring
    • Galli, E., and Gerdes, K. (2010) Spatial resolution of two bacterial cell division proteins: ZapA recruits ZapB to the inner face of the Z-ring. Mol Microbiol 76: 1514-1526.
    • (2010) Mol Microbiol , vol.76 , pp. 1514-1526
    • Galli, E.1    Gerdes, K.2
  • 55
    • 84855881444 scopus 로고    scopus 로고
    • FtsZ-ZapA-ZapB interactome of Escherichia coli
    • Galli, E., and Gerdes, K. (2012) FtsZ-ZapA-ZapB interactome of Escherichia coli. J Bacteriol 194: 292-302.
    • (2012) J Bacteriol , vol.194 , pp. 292-302
    • Galli, E.1    Gerdes, K.2
  • 56
    • 26944444295 scopus 로고    scopus 로고
    • Evidence for functional overlap among multiple bacterial cell division proteins: compensating for the loss of FtsK
    • Geissler, B., and Margolin, W. (2005) Evidence for functional overlap among multiple bacterial cell division proteins: compensating for the loss of FtsK. Mol Microbiol 58: 596-612.
    • (2005) Mol Microbiol , vol.58 , pp. 596-612
    • Geissler, B.1    Margolin, W.2
  • 57
    • 0037386678 scopus 로고    scopus 로고
    • A gain-of-function mutation in ftsA bypasses the requirement for the essential cell division gene zipA in Escherichia coli
    • Geissler, B., Elraheb, D., and Margolin, W. (2003) A gain-of-function mutation in ftsA bypasses the requirement for the essential cell division gene zipA in Escherichia coli. Proc Natl Acad Sci USA 100: 4197-4202.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 4197-4202
    • Geissler, B.1    Elraheb, D.2    Margolin, W.3
  • 58
    • 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. (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.
    • (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.6
  • 59
    • 33846237649 scopus 로고    scopus 로고
    • Mutants, suppressors, and wrinkled colonies: mutant alleles of the cell division gene ftsQ point to functional domains in FtsQ and a role for domain 1C of FtsA in divisome assembly
    • Goehring, N.W., Petrovska, I., Boyd, D., and Beckwith, J. (2007a) Mutants, suppressors, and wrinkled colonies: mutant alleles of the cell division gene ftsQ point to functional domains in FtsQ and a role for domain 1C of FtsA in divisome assembly. J Bacteriol 189: 633-645.
    • (2007) J Bacteriol , vol.189 , pp. 633-645
    • Goehring, N.W.1    Petrovska, I.2    Boyd, D.3    Beckwith, J.4
  • 60
    • 33846198296 scopus 로고    scopus 로고
    • Role for the nonessential N terminus of FtsN in divisome assembly
    • Goehring, N.W., Robichon, C., and Beckwith, J. (2007b) Role for the nonessential N terminus of FtsN in divisome assembly. J Bacteriol 189: 646-649.
    • (2007) J Bacteriol , vol.189 , pp. 646-649
    • Goehring, N.W.1    Robichon, C.2    Beckwith, J.3
  • 61
    • 65249155295 scopus 로고    scopus 로고
    • Divisome under construction: distinct domains of the small membrane protein FtsB are necessary for interaction with multiple cell division proteins
    • Gonzalez, M.D., and Beckwith, J. (2009) Divisome under construction: distinct domains of the small membrane protein FtsB are necessary for interaction with multiple cell division proteins. J Bacteriol 191: 2815-2825.
    • (2009) J Bacteriol , vol.191 , pp. 2815-2825
    • Gonzalez, M.D.1    Beckwith, J.2
  • 62
    • 77952577603 scopus 로고    scopus 로고
    • Multiple interaction domains in FtsL, a protein component of the widely conserved bacterial FtsLBQ cell division complex
    • Gonzalez, M.D., Akbay, E.A., Boyd, D., and Beckwith, J. (2010) Multiple interaction domains in FtsL, a protein component of the widely conserved bacterial FtsLBQ cell division complex. J Bacteriol 192: 2757-2768.
    • (2010) J Bacteriol , vol.192 , pp. 2757-2768
    • Gonzalez, M.D.1    Akbay, E.A.2    Boyd, D.3    Beckwith, J.4
  • 63
    • 0036791675 scopus 로고    scopus 로고
    • A widely conserved bacterial cell division protein that promotes assembly of the tubulin-like protein FtsZ
    • Gueiros-Filho, F.J., and Losick, R. (2002) A widely conserved bacterial cell division protein that promotes assembly of the tubulin-like protein FtsZ. Genes Dev 16: 2544-2556.
    • (2002) Genes Dev , vol.16 , pp. 2544-2556
    • Gueiros-Filho, F.J.1    Losick, R.2
  • 64
    • 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., and de Boer, P.A. (1997) Direct binding of FtsZ to ZipA, an essential component of the septal ring structure that mediates cell division in E. coli. Cell 88: 175-185.
    • (1997) Cell , vol.88 , pp. 175-185
    • Hale, C.A.1    de Boer, P.A.2
  • 65
    • 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
  • 66
    • 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. (2002) ZipA is required for recruitment of FtsK, FtsQ, FtsL, and FtsN to the septal ring in Escherichia coli. J Bacteriol 184: 2552-2556.
    • (2002) J Bacteriol , vol.184 , pp. 2552-2556
    • Hale, C.A.1    de Boer, P.A.2
  • 67
    • 79952401787 scopus 로고    scopus 로고
    • Identification of Escherichia coli ZapC (YcbW) as a component of the division apparatus that binds and bundles FtsZ polymers
    • Hale, C.A., Shiomi, D., Liu, B., Bernhardt, T.G., Margolin, W., Niki, H., and de Boer, P.A. (2011) Identification of Escherichia coli ZapC (YcbW) as a component of the division apparatus that binds and bundles FtsZ polymers. J Bacteriol 193: 1393-1404.
    • (2011) J Bacteriol , vol.193 , pp. 1393-1404
    • Hale, C.A.1    Shiomi, D.2    Liu, B.3    Bernhardt, T.G.4    Margolin, W.5    Niki, H.6    de Boer, P.A.7
  • 68
    • 84868504605 scopus 로고    scopus 로고
    • Reconstitution of the Escherichia coli cell division ZipA-FtsZ complexes in nanodiscs as revealed by electron microscopy
    • Hernández-Rocamora, V.M., García-Montañées, C., Rivas, G., and Llorca, O. (2012a) Reconstitution of the Escherichia coli cell division ZipA-FtsZ complexes in nanodiscs as revealed by electron microscopy. J Struct Biol 180: 531-538.
    • (2012) J Struct Biol , vol.180 , pp. 531-538
    • Hernández-Rocamora, V.M.1    García-Montañées, C.2    Rivas, G.3    Llorca, O.4
  • 69
    • 84865737007 scopus 로고    scopus 로고
    • Dynamic interaction of the Escherichia coli cell division ZipA and FtsZ proteins evidenced in nanodiscs
    • Hernández-Rocamora, V.M., Reija, B., García, C., Natale, P., Alfonso, C., Minton, A.P., etal. (2012b) Dynamic interaction of the Escherichia coli cell division ZipA and FtsZ proteins evidenced in nanodiscs. J Biol Chem 287: 30097-30104.
    • (2012) J Biol Chem , vol.287 , pp. 30097-30104
    • Hernández-Rocamora, V.M.1    Reija, B.2    García, C.3    Natale, P.4    Alfonso, C.5    Minton, A.P.6
  • 70
    • 0035118119 scopus 로고    scopus 로고
    • Enzymology of elongation and constriction of the murein sacculus of Escherichia coli
    • Höltje, J.V., and Heidrich, C. (2001) Enzymology of elongation and constriction of the murein sacculus of Escherichia coli. Biochimie 83: 103-108.
    • (2001) Biochimie , vol.83 , pp. 103-108
    • Höltje, J.V.1    Heidrich, C.2
  • 71
    • 84876189962 scopus 로고    scopus 로고
    • FtsZ-ring stability: of bundles, tubules, crosslinks and curves
    • Huang, K.H., Durand-Heredia, J., and Janakiraman, A. (2013) FtsZ-ring stability: of bundles, tubules, crosslinks and curves. J Bacteriol 195: 1859-1868.
    • (2013) J Bacteriol , vol.195 , pp. 1859-1868
    • Huang, K.H.1    Durand-Heredia, J.2    Janakiraman, A.3
  • 72
    • 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., and Gottesman, S. (1984) 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: 4490-4494.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 4490-4494
    • Huisman, O.1    D'Ari, R.2    Gottesman, S.3
  • 73
    • 0025314797 scopus 로고
    • Rule governing the division pattern in Escherichia coli minB and wild-type filaments
    • Jaffé, A., Boye, E., and D'Ari, R. (1990) Rule governing the division pattern in Escherichia coli minB and wild-type filaments. J Bacteriol 172: 3500-3502.
    • (1990) J Bacteriol , vol.172 , pp. 3500-3502
    • Jaffé, A.1    Boye, E.2    D'Ari, R.3
  • 74
    • 70449564517 scopus 로고    scopus 로고
    • SpoIIIE and a novel type of DNA translocase, SftA, couple chromosome segregation with cell division in Bacillus subtilis
    • Kaimer, C., Gonzalez-Pastor, J.E., and Graumann, P.L. (2009) SpoIIIE and a novel type of DNA translocase, SftA, couple chromosome segregation with cell division in Bacillus subtilis. Mol Microbiol 74: 810-825.
    • (2009) Mol Microbiol , vol.74 , pp. 810-825
    • Kaimer, C.1    Gonzalez-Pastor, J.E.2    Graumann, P.L.3
  • 75
    • 12344306119 scopus 로고    scopus 로고
    • The morphogenetic MreBCD proteins of Escherichia coli form an essential membrane-bound complex
    • Kruse, T., Bork-Jensen, J., and Gerdes, K. (2005) The morphogenetic MreBCD proteins of Escherichia coli form an essential membrane-bound complex. Mol Microbiol 55: 78-89.
    • (2005) Mol Microbiol , vol.55 , pp. 78-89
    • Kruse, T.1    Bork-Jensen, J.2    Gerdes, K.3
  • 76
    • 84876277724 scopus 로고    scopus 로고
    • Structural organization of FtsB, a transmembrane protein of the bacterial divisome
    • Lapointe, L.M., Taylor, K.C., Subramaniam, S., Khadria, A., Rayment, I., and Senes, A. (2013) Structural organization of FtsB, a transmembrane protein of the bacterial divisome. Biochemistry 52: 2574-2585.
    • (2013) Biochemistry , vol.52 , pp. 2574-2585
    • Lapointe, L.M.1    Taylor, K.C.2    Subramaniam, S.3    Khadria, A.4    Rayment, I.5    Senes, A.6
  • 77
    • 0037195381 scopus 로고    scopus 로고
    • Topological characterization of the essential Escherichia coli cell division protein FtsW
    • Lara, B., and Ayala, J.A. (2002) Topological characterization of the essential Escherichia coli cell division protein FtsW. FEMS Microbiol Lett 216: 23-32.
    • (2002) FEMS Microbiol Lett , vol.216 , pp. 23-32
    • Lara, B.1    Ayala, J.A.2
  • 79
    • 0035881478 scopus 로고    scopus 로고
    • The extrusion-capture model for chromosome partitioning in bacteria
    • Lemon, K.P., and Grossman, A.D. (2001) The extrusion-capture model for chromosome partitioning in bacteria. Genes Dev 15: 2031-2041.
    • (2001) Genes Dev , vol.15 , pp. 2031-2041
    • Lemon, K.P.1    Grossman, A.D.2
  • 80
    • 36248938686 scopus 로고    scopus 로고
    • The structure of FtsZ filaments in vivo suggests a force-generating role in cell division
    • Li, Z., Trimble, M.J., Brun, Y.V., and Jensen, G.J. (2007) The structure of FtsZ filaments in vivo suggests a force-generating role in cell division. EMBO J 26: 4694-4708.
    • (2007) EMBO J , vol.26 , pp. 4694-4708
    • Li, Z.1    Trimble, M.J.2    Brun, Y.V.3    Jensen, G.J.4
  • 81
    • 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., and Donachie, W.D. (1998) FtsK is a bifunctional protein involved in cell division and chromosome localization in Escherichia coli. Mol Microbiol 29: 893-903.
    • (1998) Mol Microbiol , vol.29 , pp. 893-903
    • Liu, G.1    Draper, G.C.2    Donachie, W.D.3
  • 82
    • 44049091101 scopus 로고    scopus 로고
    • Spatial regulators for bacterial cell division self-organize into surface waves in vitro
    • Loose, M., Fischer-Friedrich, E., Ries, J., Kruse, K., and Schwille, P. (2008) Spatial regulators for bacterial cell division self-organize into surface waves in vitro. Science 320: 789-792.
    • (2008) Science , vol.320 , pp. 789-792
    • Loose, M.1    Fischer-Friedrich, E.2    Ries, J.3    Kruse, K.4    Schwille, P.5
  • 83
    • 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.
    • (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
  • 84
    • 84880526897 scopus 로고    scopus 로고
    • Intrinsic disorder of the bacterial cell division protein ZipA: coil-to-brush conformational transition
    • López-Montero, I., López-Navajas, P., Mingorance, J., Rivas, G., Vélez, M., Vicente, M., and Monroy, F. (2013) Intrinsic disorder of the bacterial cell division protein ZipA: coil-to-brush conformational transition. FASEB J 27: 3363-3375.
    • (2013) FASEB J , vol.27 , pp. 3363-3375
    • López-Montero, I.1    López-Navajas, P.2    Mingorance, J.3    Rivas, G.4    Vélez, M.5    Vicente, M.6    Monroy, F.7
  • 85
    • 4344620117 scopus 로고    scopus 로고
    • The crystal structure of ZapA and its modulation of FtsZ polymerisation
    • Low, H.H., Moncrieffe, M.C., and Löwe, J. (2004) The crystal structure of ZapA and its modulation of FtsZ polymerisation. J Mol Biol 341: 839-852.
    • (2004) J Mol Biol , vol.341 , pp. 839-852
    • Low, H.H.1    Moncrieffe, M.C.2    Löwe, J.3
  • 86
    • 0035111095 scopus 로고    scopus 로고
    • Conserved sequence motif at the C-terminus of the bacterial cell-division protein FtsA
    • Löwe, J., and van den Ent, F. (2001) Conserved sequence motif at the C-terminus of the bacterial cell-division protein FtsA. Biochimie 83: 117-120.
    • (2001) Biochimie , vol.83 , pp. 117-120
    • Löwe, J.1    van den Ent, F.2
  • 87
    • 19044391883 scopus 로고    scopus 로고
    • Site-specific mutations of FtsZ - effects on GTPase and in vitro assembly
    • Lu, C., Stricker, J., and Erickson, H.P. (2001) Site-specific mutations of FtsZ - effects on GTPase and in vitro assembly. BMC Microbiol 1: 7.
    • (2001) BMC Microbiol , vol.1 , pp. 7
    • Lu, C.1    Stricker, J.2    Erickson, H.P.3
  • 88
    • 34548630230 scopus 로고    scopus 로고
    • Assembly dynamics of the bacterial MinCDE system and spatial regulation of the Z ring
    • Lutkenhaus, J. (2007) Assembly dynamics of the bacterial MinCDE system and spatial regulation of the Z ring. Annu Rev Biochem 76: 539-562.
    • (2007) Annu Rev Biochem , vol.76 , pp. 539-562
    • Lutkenhaus, J.1
  • 89
    • 55949084028 scopus 로고    scopus 로고
    • Min oscillation in bacteria
    • Lutkenhaus, J. (2008) Min oscillation in bacteria. Adv Exp Med Biol 641: 49-61.
    • (2008) Adv Exp Med Biol , vol.641 , pp. 49-61
    • Lutkenhaus, J.1
  • 90
    • 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.
    • (2012) Cytoskeleton (Hoboken) , vol.69 , pp. 778-790
    • Lutkenhaus, J.1    Pichoff, S.2    Du, S.3
  • 91
    • 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, 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 USA 93: 13003.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 13003
    • Ma, X.1    Ehrhardt, W.2    Margolin, W.3
  • 92
    • 84871060283 scopus 로고    scopus 로고
    • The price of tags in protein localization studies
    • Margolin, W. (2012) The price of tags in protein localization studies. J Bacteriol 194: 6369-6371.
    • (2012) J Bacteriol , vol.194 , pp. 6369-6371
    • Margolin, W.1
  • 93
    • 70350437278 scopus 로고    scopus 로고
    • Central domain of DivIB caps the C-terminal regions of the FtsL/DivIC coiled-coil rod
    • Masson, S., Kern, T., Le Gouellec, A., Giustini, C., Simorre, J.P., Callow, P., etal. (2009) Central domain of DivIB caps the C-terminal regions of the FtsL/DivIC coiled-coil rod. J Biol Chem 284: 27687-27700.
    • (2009) J Biol Chem , vol.284 , pp. 27687-27700
    • Masson, S.1    Kern, T.2    Le Gouellec, A.3    Giustini, C.4    Simorre, J.P.5    Callow, P.6
  • 95
    • 0035807879 scopus 로고    scopus 로고
    • Pattern formation in Escherichia coli: a model for the pole-to-pole oscillations of Min proteins and the localization of the division site
    • Meinhardt, H., and de Boer, P.A. (2001) Pattern formation in Escherichia coli: a model for the pole-to-pole oscillations of Min proteins and the localization of the division site. Proc Natl Acad Sci USA 98: 14202-14207.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 14202-14207
    • Meinhardt, H.1    de Boer, P.A.2
  • 96
    • 67349175712 scopus 로고    scopus 로고
    • Structural and functional model for ionic (K(+)/Na(+)) and pH dependence of GTPase activity and polymerization of FtsZ, the prokaryotic ortholog of tubulin
    • Mendieta, J., Rico, A.I., López-Viñas, E., Vicente, M., Mingorance, J., and Gómez-Puertas, P. (2009) Structural and functional model for ionic (K(+)/Na(+)) and pH dependence of GTPase activity and polymerization of FtsZ, the prokaryotic ortholog of tubulin. J Mol Biol 390: 17-25.
    • (2009) J Mol Biol , vol.390 , pp. 17-25
    • Mendieta, J.1    Rico, A.I.2    López-Viñas, E.3    Vicente, M.4    Mingorance, J.5    Gómez-Puertas, P.6
  • 97
    • 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., and Espeli, O. (2008) The MatP/matS site-specific system organizes the terminus region of the E.coli chromosome into a macrodomain. Cell 135: 475-485.
    • (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    Espeli, O.7
  • 98
    • 69249213558 scopus 로고    scopus 로고
    • Cryo-electron tomography of bacteria: progress, challenges and future prospects
    • Milne, J.L., and Subramaniam, S. (2009) Cryo-electron tomography of bacteria: progress, challenges and future prospects. Nat Rev Microbiol 7: 666-675.
    • (2009) Nat Rev Microbiol , vol.7 , pp. 666-675
    • Milne, J.L.1    Subramaniam, S.2
  • 99
    • 33646573759 scopus 로고    scopus 로고
    • Bacterial morphogenes
    • Vicente, M., Tamames, J., Valencia, A., and Mingorance, J. (eds). New York, USA: Kluwer Academic/Plenum Publishers
    • Mingorance, J., Rico, A.I., and Gómez-Puertas, P. (2004) Bacterial morphogenes. In Molecules in Time and Space Bacterial Shape, Division and Phylogeny. Vicente, M., Tamames, J., Valencia, A., and Mingorance, J. (eds). New York, USA: Kluwer Academic/Plenum Publishers, pp. 173-194.
    • (2004) Molecules in Time and Space Bacterial Shape, Division and Phylogeny , pp. 173-194
    • Mingorance, J.1    Rico, A.I.2    Gómez-Puertas, P.3
  • 101
    • 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., Verheul, J., Comvalius, A.D., Martos, A., Alfonso, C., etal. (2009) The GTPase activity of Escherichia coli FtsZ determines the magnitude of the FtsZ polymer bundling by ZapA in vitro. Biochemistry 48: 11056-11066.
    • (2009) Biochemistry , vol.48 , pp. 11056-11066
    • Mohammadi, T.1    Ploeger, G.E.2    Verheul, J.3    Comvalius, A.D.4    Martos, A.5    Alfonso, C.6
  • 102
    • 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., Bouhss, A., etal. (2011) Identification of FtsW as a transporter of lipid-linked cell wall precursors across the membrane. EMBO J 30: 1425-1432.
    • (2011) EMBO J , vol.30 , pp. 1425-1432
    • Mohammadi, T.1    van Dam, V.2    Sijbrandi, R.3    Vernet, T.4    Zapun, A.5    Bouhss, A.6
  • 103
    • 70449586634 scopus 로고    scopus 로고
    • Lateral FtsZ association and the assembly of the cytokinetic Z ring in bacteria
    • Monahan, L.G., Robinson, A., and Harry, E.J. (2009) Lateral FtsZ association and the assembly of the cytokinetic Z ring in bacteria. Mol Microbiol 74: 1004-1017.
    • (2009) Mol Microbiol , vol.74 , pp. 1004-1017
    • Monahan, L.G.1    Robinson, A.2    Harry, E.J.3
  • 104
    • 0034600952 scopus 로고    scopus 로고
    • The bacterial cell-division protein ZipA and its interaction with an FtsZ fragment revealed by X-ray crystallography
    • Mosyak, L., Zhang, Y., Glasfeld, E., Haney, S., Stahl, M., Seehra, J., and Somers, W.S. (2000) The bacterial cell-division protein ZipA and its interaction with an FtsZ fragment revealed by X-ray crystallography. EMBO J 19: 3179-3191.
    • (2000) EMBO J , vol.19 , pp. 3179-3191
    • Mosyak, L.1    Zhang, Y.2    Glasfeld, E.3    Haney, S.4    Stahl, M.5    Seehra, J.6    Somers, W.S.7
  • 105
    • 0031912354 scopus 로고    scopus 로고
    • Morphogenesis of Escherichia coli
    • Nanninga, N. (1998) Morphogenesis of Escherichia coli. Microbiol Mol Biol Rev 62: 110-129.
    • (1998) Microbiol Mol Biol Rev , vol.62 , pp. 110-129
    • Nanninga, N.1
  • 106
    • 0034650256 scopus 로고    scopus 로고
    • Dynamic organization of chromosomal DNA in Escherichia coli
    • Niki, H., Yamaichi, Y., and Hiraga, S. (2000) Dynamic organization of chromosomal DNA in Escherichia coli. Genes Dev 14: 212-223.
    • (2000) Genes Dev , vol.14 , pp. 212-223
    • Niki, H.1    Yamaichi, Y.2    Hiraga, S.3
  • 107
    • 84862755531 scopus 로고    scopus 로고
    • Chlamydia co-opts the rod shape-determining proteins MreB and Pbp2 for cell division
    • Ouellette, S.P., Karimova, G., Subtil, A., and Ladant, D. (2012) Chlamydia co-opts the rod shape-determining proteins MreB and Pbp2 for cell division. Mol Microbiol 85: 164-178.
    • (2012) Mol Microbiol , vol.85 , pp. 164-178
    • Ouellette, S.P.1    Karimova, G.2    Subtil, A.3    Ladant, D.4
  • 108
    • 79959599472 scopus 로고    scopus 로고
    • The pH dependence of polymerization and bundling by the essential bacterial cytoskeletal protein FtsZ
    • Pacheco-Gómez, R., Roper, D.I., Dafforn, T.R., and Rodger, A. (2011) The pH dependence of polymerization and bundling by the essential bacterial cytoskeletal protein FtsZ. PLoS ONE 6: e19369.
    • (2011) PLoS ONE , vol.6
    • Pacheco-Gómez, R.1    Roper, D.I.2    Dafforn, T.R.3    Rodger, A.4
  • 110
    • 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., and Bernhardt, T.G. (2010) Lipoprotein cofactors located in the outer membrane activate bacterial cell wall polymerases. Cell 143: 1110-1120.
    • (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    Bernhardt, T.G.7
  • 111
    • 44949258242 scopus 로고    scopus 로고
    • How bacteria consume their own exoskeletons (turnover and recycling of cell wall peptidoglycan)
    • table of contents.
    • Park, J.T., and Uehara, T. (2008) How bacteria consume their own exoskeletons (turnover and recycling of cell wall peptidoglycan). Microbiol Mol Biol Rev 72: 211-227, table of contents.
    • (2008) Microbiol Mol Biol Rev , vol.72 , pp. 211-227
    • Park, J.T.1    Uehara, T.2
  • 112
    • 79961135028 scopus 로고    scopus 로고
    • The Min oscillator uses MinD-dependent conformational changes in MinE to spatially regulate cytokinesis
    • Park, K.T., Wu, W., Battaile, K.P., Lovell, S., Holyoak, T., and Lutkenhaus, J. (2011) The Min oscillator uses MinD-dependent conformational changes in MinE to spatially regulate cytokinesis. Cell 146: 396-407.
    • (2011) Cell , vol.146 , pp. 396-407
    • Park, K.T.1    Wu, W.2    Battaile, K.P.3    Lovell, S.4    Holyoak, T.5    Lutkenhaus, J.6
  • 113
    • 84863564893 scopus 로고    scopus 로고
    • Mechanism of the asymmetric activation of the MinD ATPase by MinE
    • Park, K.T., Wu, W., Lovell, S., and Lutkenhaus, J. (2012) Mechanism of the asymmetric activation of the MinD ATPase by MinE. Mol Microbiol 85: 271-281.
    • (2012) Mol Microbiol , vol.85 , pp. 271-281
    • Park, K.T.1    Wu, W.2    Lovell, S.3    Lutkenhaus, J.4
  • 114
    • 84873286335 scopus 로고    scopus 로고
    • A specific role for the ZipA protein in cell division: stabilization of the FtsZ protein
    • Pazos, M., Natale, P., and Vicente, M. (2013) A specific role for the ZipA protein in cell division: stabilization of the FtsZ protein. J Biol Chem 288: 3219-3226.
    • (2013) J Biol Chem , vol.288 , pp. 3219-3226
    • Pazos, M.1    Natale, P.2    Vicente, M.3
  • 115
    • 78751699495 scopus 로고    scopus 로고
    • A new morphogenesis pathway in bacteria: unbalanced activity of cell wall synthesis machineries leads to coccus-to-rod transition and filamentation in ovococci
    • Pérez-Núñez, D., Briandet, R., David, B., Gautier, C., Renault, P., Hallet, B., etal. (2011) A new morphogenesis pathway in bacteria: unbalanced activity of cell wall synthesis machineries leads to coccus-to-rod transition and filamentation in ovococci. Mol Microbiol 79: 759-771.
    • (2011) Mol Microbiol , vol.79 , pp. 759-771
    • Pérez-Núñez, D.1    Briandet, R.2    David, B.3    Gautier, C.4    Renault, P.5    Hallet, B.6
  • 116
    • 80052525834 scopus 로고    scopus 로고
    • A fail-safe mechanism in the septal ring assembly pathway generated by the sequential recruitment of cell separation amidases and their activators
    • Peters, N.T., Dinh, T., and Bernhardt, T.G. (2011) A fail-safe mechanism in the septal ring assembly pathway generated by the sequential recruitment of cell separation amidases and their activators. J Bacteriol 193: 4973-4983.
    • (2011) J Bacteriol , vol.193 , pp. 4973-4983
    • Peters, N.T.1    Dinh, T.2    Bernhardt, T.G.3
  • 117
    • 0037084109 scopus 로고    scopus 로고
    • Unique and overlapping roles for ZipA and FtsA in septal ring assembly in Escherichia coli
    • Pichoff, S., and Lutkenhaus, J. (2002) Unique and overlapping roles for ZipA and FtsA in septal ring assembly in Escherichia coli. EMBO J 21: 685-693.
    • (2002) EMBO J , vol.21 , pp. 685-693
    • Pichoff, S.1    Lutkenhaus, J.2
  • 118
    • 15744385269 scopus 로고    scopus 로고
    • Tethering the Z ring to the membrane through a conserved membrane targeting sequence in FtsA
    • Pichoff, S., and Lutkenhaus, J. (2005) Tethering the Z ring to the membrane through a conserved membrane targeting sequence in FtsA. Mol Microbiol 55: 1722-1734.
    • (2005) Mol Microbiol , vol.55 , pp. 1722-1734
    • Pichoff, S.1    Lutkenhaus, J.2
  • 119
    • 84155167132 scopus 로고    scopus 로고
    • FtsA mutants impaired for self-interaction bypass ZipA suggesting a model in which FtsA's self-interaction competes with its ability to recruit downstream division proteins
    • Pichoff, S., Shen, B., Sullivan, B., and Lutkenhaus, J. (2012) FtsA mutants impaired for self-interaction bypass ZipA suggesting a model in which FtsA's self-interaction competes with its ability to recruit downstream division proteins. Mol Microbiol 83: 151-167.
    • (2012) Mol Microbiol , vol.83 , pp. 151-167
    • Pichoff, S.1    Shen, B.2    Sullivan, B.3    Lutkenhaus, J.4
  • 120
    • 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., Alexeeva, S., Hoogendoorn, E., Postma, M., etal. (2013) Colocalization and interaction between elongasome and divisome during a preparative cell division phase in Escherichia coli. Mol Microbiol 87: 1074-1087.
    • (2013) Mol Microbiol , vol.87 , pp. 1074-1087
    • van der Ploeg, R.1    Verheul, J.2    Vischer, N.O.3    Alexeeva, S.4    Hoogendoorn, E.5    Postma, M.6
  • 121
    • 84859443989 scopus 로고    scopus 로고
    • Escherichia coli low-molecular-weight penicillin-binding proteins help orient septal FtsZ, and their absence leads to asymmetric cell division and branching
    • Potluri, L.P., de Pedro, M.A., and Young, K.D. (2012a) Escherichia coli low-molecular-weight penicillin-binding proteins help orient septal FtsZ, and their absence leads to asymmetric cell division and branching. Mol Microbiol 84: 203-224.
    • (2012) Mol Microbiol , vol.84 , pp. 203-224
    • Potluri, L.P.1    de Pedro, M.A.2    Young, K.D.3
  • 122
    • 84868326175 scopus 로고    scopus 로고
    • ZipA is required for FtsZ-dependent preseptal peptidoglycan synthesis prior to invagination during cell division
    • Potluri, L.P., Kannan, S., and Young, K.D. (2012b) ZipA is required for FtsZ-dependent preseptal peptidoglycan synthesis prior to invagination during cell division. J Bacteriol 194: 5334-5342.
    • (2012) J Bacteriol , vol.194 , pp. 5334-5342
    • Potluri, L.P.1    Kannan, S.2    Young, K.D.3
  • 123
    • 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. (1999a) Rapid pole-to-pole oscillation of a protein required for directing division to the middle of Escherichia coli. Proc Natl Acad Sci USA 96: 4971-4976.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 4971-4976
    • Raskin, D.M.1    de Boer, P.A.2
  • 124
    • 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. (1999b) 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
  • 125
    • 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. (1999) ZipA is a MAP-Tau homolog and is essential for structural integrity of the cytokinetic FtsZ ring during bacterial cell division. EMBO J 18: 2372-2383.
    • (1999) EMBO J , vol.18 , pp. 2372-2383
    • RayChaudhuri, D.1
  • 127
    • 4444300864 scopus 로고    scopus 로고
    • Role of two essential domains of Escherichia coli FtsA in localization and progression of the division ring
    • Rico, A.I., Garcia-Ovalle, M., Mingorance, J., and Vicente, M. (2004) Role of two essential domains of Escherichia coli FtsA in localization and progression of the division ring. Mol Microbiol 53: 1359-1371.
    • (2004) Mol Microbiol , vol.53 , pp. 1359-1371
    • Rico, A.I.1    Garcia-Ovalle, M.2    Mingorance, J.3    Vicente, M.4
  • 128
    • 77951562635 scopus 로고    scopus 로고
    • Role of Escherichia coli FtsN protein in the assembly and stability of the cell division ring
    • Rico, A.I., Garcia-Ovalle, M., Palacios, P., Casanova, M., and Vicente, M. (2010) Role of Escherichia coli FtsN protein in the assembly and stability of the cell division ring. Mol Microbiol 76: 760-771.
    • (2010) Mol Microbiol , vol.76 , pp. 760-771
    • Rico, A.I.1    Garcia-Ovalle, M.2    Palacios, P.3    Casanova, M.4    Vicente, M.5
  • 129
    • 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.
    • (2003) J Bacteriol , vol.185 , pp. 3344-3351
    • Rueda, S.1    Vicente, M.2    Mingorance, J.3
  • 130
    • 0642377467 scopus 로고    scopus 로고
    • POTRA: a conserved domain in the FtsQ family and a class of beta-barrel outer membrane proteins
    • Sánchez-Pulido, L., Devos, D., Genevrois, S., Vicente, M., and Valencia, A. (2003) POTRA: a conserved domain in the FtsQ family and a class of beta-barrel outer membrane proteins. Trends Biochem Sci 28: 523-526.
    • (2003) Trends Biochem Sci , vol.28 , pp. 523-526
    • Sánchez-Pulido, L.1    Devos, D.2    Genevrois, S.3    Vicente, M.4    Valencia, A.5
  • 131
    • 84888865284 scopus 로고    scopus 로고
    • Spatial control of the cell division site by the Min system in E.coli
    • doi: 10.1111/1462-2920.12119.
    • Shih, Y.L., and Zheng, M. (2013) Spatial control of the cell division site by the Min system in E.coli. Environ Microbiol. doi: 10.1111/1462-2920.12119.
    • (2013) Environ Microbiol
    • Shih, Y.L.1    Zheng, M.2
  • 132
    • 79959577107 scopus 로고    scopus 로고
    • The N-terminal amphipathic helix of the topological specificity factor MinE is associated with shaping membrane curvature
    • Shih, Y.L., Huang, K.F., Lai, H.M., Liao, J.H., Lee, C.S., Chang, C.M., etal. (2011) The N-terminal amphipathic helix of the topological specificity factor MinE is associated with shaping membrane curvature. PLoS ONE 6: e21425.
    • (2011) PLoS ONE , vol.6
    • Shih, Y.L.1    Huang, K.F.2    Lai, H.M.3    Liao, J.H.4    Lee, C.S.5    Chang, C.M.6
  • 133
    • 84873260168 scopus 로고    scopus 로고
    • Glutamate 83 and arginine 85 of helix H3 bend are key residues for FtsZ polymerization, GTPase activity and cellular viability of Escherichia coli: lateral mutations affect FtsZ polymerization and E. coli viability
    • Shin, J.Y., Vollmer, W., Lagos, R., and Monasterio, O. (2013) Glutamate 83 and arginine 85 of helix H3 bend are key residues for FtsZ polymerization, GTPase activity and cellular viability of Escherichia coli: lateral mutations affect FtsZ polymerization and E. coli viability. BMC Microbiol 13: 26.
    • (2013) BMC Microbiol , vol.13 , pp. 26
    • Shin, J.Y.1    Vollmer, W.2    Lagos, R.3    Monasterio, O.4
  • 134
    • 36549087126 scopus 로고    scopus 로고
    • Dimerization or oligomerization of the actin-like FtsA protein enhances the integrity of the cytokinetic Z ring
    • Shiomi, D., and Margolin, W. (2007) Dimerization or oligomerization of the actin-like FtsA protein enhances the integrity of the cytokinetic Z ring. Mol Microbiol 66: 1396-1415.
    • (2007) Mol Microbiol , vol.66 , pp. 1396-1415
    • Shiomi, D.1    Margolin, W.2
  • 135
    • 84857375148 scopus 로고    scopus 로고
    • The Escherichia coli cell division protein ZipA forms homodimers prior to association with FtsZ
    • Skoog, K., and Daley, D.O. (2012) The Escherichia coli cell division protein ZipA forms homodimers prior to association with FtsZ. Biochemistry 51: 1407-1415.
    • (2012) Biochemistry , vol.51 , pp. 1407-1415
    • Skoog, K.1    Daley, D.O.2
  • 136
    • 84855963711 scopus 로고    scopus 로고
    • Sequential closure of the cytoplasm and then the periplasm during cell division in Escherichia coli
    • Skoog, K., Söderström, B., Widengren, J., von Heijne, G., and Daley, D.O. (2012) Sequential closure of the cytoplasm and then the periplasm during cell division in Escherichia coli. J Bacteriol 194: 584-586.
    • (2012) J Bacteriol , vol.194 , pp. 584-586
    • Skoog, K.1    Söderström, B.2    Widengren, J.3    von Heijne, G.4    Daley, D.O.5
  • 137
    • 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., etal. (2007) FtsZ polymer-bundling by the Escherichia coli ZapA orthologue, YgfE, involves a conformational change in bound GTP. J Mol Biol 369: 210-221.
    • (2007) J Mol Biol , vol.369 , pp. 210-221
    • Small, E.1    Marrington, R.2    Rodger, A.3    Scott, D.J.4    Sloan, K.5    Roper, D.6
  • 138
    • 0029149453 scopus 로고
    • Heads or tails - what determines the orientation of proteins in the membrane
    • Spiess, M. (1995) Heads or tails - what determines the orientation of proteins in the membrane. FEBS Lett 369: 76-79.
    • (1995) FEBS Lett , vol.369 , pp. 76-79
    • Spiess, M.1
  • 139
    • 0031974261 scopus 로고    scopus 로고
    • Cell division is required for resolution of dimer chromosomes at the dif locus of Escherichia coli
    • Steiner, W.W., and Kuempel, P.L. (1998) Cell division is required for resolution of dimer chromosomes at the dif locus of Escherichia coli. Mol Microbiol 27: 257-268.
    • (1998) Mol Microbiol , vol.27 , pp. 257-268
    • Steiner, W.W.1    Kuempel, P.L.2
  • 140
    • 84866719247 scopus 로고    scopus 로고
    • 3D-SIM super resolution microscopy reveals a bead-like arrangement for FtsZ and the division machinery: implications for triggering cytokinesis
    • Strauss, M.P., Liew, A.T., Turnbull, L., Whitchurch, C.B., Monahan, L.G., and Harry, E.J. (2012) 3D-SIM super resolution microscopy reveals a bead-like arrangement for FtsZ and the division machinery: implications for triggering cytokinesis. PLoS Biol 10: e1001389.
    • (2012) PLoS Biol , vol.10
    • Strauss, M.P.1    Liew, A.T.2    Turnbull, L.3    Whitchurch, C.B.4    Monahan, L.G.5    Harry, E.J.6
  • 141
    • 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 USA 99: 3171-3175.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 3171-3175
    • Stricker, J.1    Maddox, P.2    Salmon, E.D.3    Erickson, H.P.4
  • 142
    • 84871055385 scopus 로고    scopus 로고
    • The helical MreB cytoskeleton in E. coli MC1000/pLE7 is an artifact of the N-terminal YFP tag
    • Swulius, M.T., and Jensen, G.J. (2012) The helical MreB cytoskeleton in E. coli MC1000/pLE7 is an artifact of the N-terminal YFP tag. J Bacteriol 194: 6382-6386.
    • (2012) J Bacteriol , vol.194 , pp. 6382-6386
    • Swulius, M.T.1    Jensen, G.J.2
  • 143
    • 84861151969 scopus 로고    scopus 로고
    • FtsA forms actin-like protofilaments
    • Szwedziak, P., Wang, Q., Freund, S.M., and Löwe, J. (2012) FtsA forms actin-like protofilaments. EMBO J 31: 2249-2260.
    • (2012) EMBO J , vol.31 , pp. 2249-2260
    • Szwedziak, P.1    Wang, Q.2    Freund, S.M.3    Löwe, J.4
  • 144
    • 0016243975 scopus 로고
    • Quantal behavior of a diffusible factor which initiates septum formation at potential division sites in Escherichia coli
    • Teather, R.M., Collins, J.F., and Donachie, W.D. (1974) Quantal behavior of a diffusible factor which initiates septum formation at potential division sites in Escherichia coli. J Bacteriol 118: 407-413.
    • (1974) J Bacteriol , vol.118 , pp. 407-413
    • Teather, R.M.1    Collins, J.F.2    Donachie, W.D.3
  • 145
    • 3142602980 scopus 로고    scopus 로고
    • FtsZ exhibits rapid movement and oscillation waves in helix-like patterns in Escherichia coli
    • Thanedar, S., and Margolin, W. (2004) FtsZ exhibits rapid movement and oscillation waves in helix-like patterns in Escherichia coli. Curr Biol 14: 1167-1173.
    • (2004) Curr Biol , vol.14 , pp. 1167-1173
    • Thanedar, S.1    Margolin, W.2
  • 146
    • 78650910561 scopus 로고    scopus 로고
    • Molecular mechanism by which the nucleoid occlusion factor, SlmA, keeps cytokinesis in check
    • Tonthat, N.K., Arold, S.T., Pickering, B.F., Van Dyke, M.W., Liang, S., Lu, Y., etal. (2011) Molecular mechanism by which the nucleoid occlusion factor, SlmA, keeps cytokinesis in check. EMBO J 30: 154-164.
    • (2011) EMBO J , vol.30 , pp. 154-164
    • Tonthat, N.K.1    Arold, S.T.2    Pickering, B.F.3    Van Dyke, M.W.4    Liang, S.5    Lu, Y.6
  • 147
    • 84879531614 scopus 로고    scopus 로고
    • SlmA forms a higher-order structure on DNA that inhibits cytokinetic Z-ring formation over the nucleoid
    • Tonthat, N.K., Milam, S.L., Chinnam, N., Whitfill, T., Margolin, W., and Schumacher, M.A. (2013) SlmA forms a higher-order structure on DNA that inhibits cytokinetic Z-ring formation over the nucleoid. Proc Natl Acad Sci USA 110: 10586-10591.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 10586-10591
    • Tonthat, N.K.1    Milam, S.L.2    Chinnam, N.3    Whitfill, T.4    Margolin, W.5    Schumacher, M.A.6
  • 149
    • 77951470447 scopus 로고    scopus 로고
    • Daughter cell separation is controlled by cytokinetic ring-activated cell wall hydrolysis
    • Uehara, T., Parzych, K.R., Dinh, T., and Bernhardt, T.G. (2010) Daughter cell separation is controlled by cytokinetic ring-activated cell wall hydrolysis. EMBO J 29: 1412-1422.
    • (2010) EMBO J , vol.29 , pp. 1412-1422
    • Uehara, T.1    Parzych, K.R.2    Dinh, T.3    Bernhardt, T.G.4
  • 150
    • 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., and Vollmer, W. (2004) Murein (peptidoglycan) binding property of the essential cell division protein FtsN from Escherichia coli. J Bacteriol 186: 6728-6737.
    • (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    Vollmer, W.7
  • 151
    • 33745209434 scopus 로고    scopus 로고
    • The order of the ring: assembly of Escherichia coli cell division components
    • Vicente, M., and Rico, A.I. (2006) The order of the ring: assembly of Escherichia coli cell division components. Mol Microbiol 61: 5-8.
    • (2006) Mol Microbiol , vol.61 , pp. 5-8
    • Vicente, M.1    Rico, A.I.2
  • 152
    • 42549083859 scopus 로고    scopus 로고
    • How similar cell division genes are located and behave in different bacteria
    • Vicente, M., Tamames, J., Valencia, A., and Mingorance, J. (eds). New York, USA: Kluwer Academic/Plenum Publishers
    • Vicente, M., Alvarez, J., and Martínez-Arteaga, R. (2004) How similar cell division genes are located and behave in different bacteria. In Molecules in Time and Space Bacterial Shape, Division and Phylogeny. Vicente, M., Tamames, J., Valencia, A., and Mingorance, J. (eds). New York, USA: Kluwer Academic/Plenum Publishers, pp. 239-248.
    • (2004) Molecules in Time and Space Bacterial Shape, Division and Phylogeny , pp. 239-248
    • Vicente, M.1    Alvarez, J.2    Martínez-Arteaga, R.3
  • 153
  • 156
    • 84876590045 scopus 로고    scopus 로고
    • OrtholugeDB: a bacterial and archaeal orthology resource for improved comparative genomic analysis
    • Whiteside, M.D., Winsor, G.L., Laird, M.R., and Brinkman, F.S. (2013) OrtholugeDB: a bacterial and archaeal orthology resource for improved comparative genomic analysis. Nucleic Acids Res 41: D366-D376.
    • (2013) Nucleic Acids Res , vol.41
    • Whiteside, M.D.1    Winsor, G.L.2    Laird, M.R.3    Brinkman, F.S.4
  • 157
    • 0025813235 scopus 로고
    • Toporegulation of bacterial division according to the nucleoid occlusion model
    • Woldringh, C.L., Mulder, E., Huls, P.G., and Vischer, N. (1991) Toporegulation of bacterial division according to the nucleoid occlusion model. Res Microbiol 142: 309-320.
    • (1991) Res Microbiol , vol.142 , pp. 309-320
    • Woldringh, C.L.1    Mulder, E.2    Huls, P.G.3    Vischer, N.4
  • 158
    • 81055145336 scopus 로고    scopus 로고
    • An ATP-binding cassette transporter-like complex governs cell-wall hydrolysis at the bacterial cytokinetic ring
    • Yang, D.C., Peters, N.T., Parzych, K.R., Uehara, T., Markovski, M., and Bernhardt, T.G. (2011) An ATP-binding cassette transporter-like complex governs cell-wall hydrolysis at the bacterial cytokinetic ring. Proc Natl Acad Sci USA 108: E1052-E1060.
    • (2011) Proc Natl Acad Sci USA , vol.108
    • Yang, D.C.1    Peters, N.T.2    Parzych, K.R.3    Uehara, T.4    Markovski, M.5    Bernhardt, T.G.6
  • 159
    • 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.
    • (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
  • 160
    • 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., and Margolin, W. (1999) 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: 315-326.
    • (1999) Mol Microbiol , vol.32 , pp. 315-326
    • Yu, X.C.1    Margolin, W.2


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