메뉴 건너뛰기




Volumn 194, Issue 8, 2012, Pages 1989-2000

The Early Divisome Protein FtsA Interacts Directly through Its 1c: Subdomain with the Cytoplasmic Domain of the Late Divisome: Protein FtsN

Author keywords

[No Author keywords available]

Indexed keywords

CYTOPLASM PROTEIN; ESCHERICHIA COLI PROTEIN; FTSA PROTEIN; FTSN PROTEIN; FTSZ PROTEIN; LEUCINE ZIPPER PROTEIN; UNCLASSIFIED DRUG;

EID: 84861204197     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.06683-11     Document Type: Article
Times cited : (77)

References (60)
  • 1
    • 15944362608 scopus 로고    scopus 로고
    • Maturation of the Escherichia coli divisome occurs in two steps
    • Aarsman ME, et al. 2005. Maturation of the Escherichia coli divisome occurs in two steps. Mol. Microbiol. 55:1631-1645.
    • (2005) Mol. Microbiol. , vol.55 , pp. 1631-1645
    • Aarsman, M.E.1
  • 2
    • 0030856502 scopus 로고    scopus 로고
    • FtsN, a late recruit to the septum in Escherichia coli
    • Addinall SG, Cao C, 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
  • 3
    • 77954376358 scopus 로고    scopus 로고
    • Direct interactions of early and late assembling division proteins in Escherichia coli cells resolved by FRET
    • Alexeeva S, Gadella TW, Jr, Verheul J, Verhoeven GS, 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
  • 4
    • 73849120353 scopus 로고    scopus 로고
    • Discovery and characterization of three new Escherichia coli septal ring proteins that contain a SPOR domain: DamX, DedD, and RlpA
    • Arends SJ, et al. 2010. Discovery and characterization of three new Escherichia coli septal ring proteins that contain a SPOR domain: DamX, DedD, and RlpA. J. Bacteriol. 192:242-255.
    • (2010) J. Bacteriol. , vol.192 , pp. 242-255
    • Arends, S.J.1
  • 5
    • 34249811807 scopus 로고    scopus 로고
    • An altered FtsA can compensate for the loss of essential cell division protein FtsN in Escherichia coli
    • Bernard CS, Sadasivam M, Shiomi D, Margolin W. 2007. An altered FtsA can compensate for the loss of essential cell division protein FtsN in Escherichia coli. Mol. Microbiol. 64:1289-1305.
    • (2007) Mol. Microbiol. , vol.64 , pp. 1289-1305
    • Bernard, C.S.1    Sadasivam, M.2    Shiomi, D.3    Margolin, W.4
  • 6
    • 0037783310 scopus 로고    scopus 로고
    • The Escherichia coli amidase AmiC is a periplasmic septal ring component exported via the twin-arginine transport pathway
    • Bernhardt TG, de Boer PA. 2003. The Escherichia coli amidase AmiC is a periplasmic septal ring component exported via the twin-arginine transport pathway. Mol. Microbiol. 48:1171-1182.
    • (2003) Mol. Microbiol. , vol.48 , pp. 1171-1182
    • Bernhardt, T.G.1    de Boer, P.A.2
  • 7
    • 67649744023 scopus 로고    scopus 로고
    • Adenine nucleotide-dependent regulation of assembly of bacterial tubulin-like FtsZ by a hypermorph of bacterial actinlike FtsA
    • Beuria TK, et al. 2009. Adenine nucleotide-dependent regulation of assembly of bacterial tubulin-like FtsZ by a hypermorph of bacterial actinlike FtsA. J. Biol. Chem. 284:14079-14086.
    • (2009) J. Biol. Chem. , vol.284 , pp. 14079-14086
    • Beuria, T.K.1
  • 8
    • 0026059127 scopus 로고
    • FtsZ ring structure associated with division in Escherichia coli
    • Bi E, 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.1    Lutkenhaus, J.2
  • 9
    • 0033748351 scopus 로고    scopus 로고
    • Mapping protein-protein interaction domains using ordered fragment ladder far-Western analysis of hexahistidine-tagged fusion proteins
    • Burgess RR, Arthur TM, Pietz BC. 2000. Mapping protein-protein interaction domains using ordered fragment ladder far-Western analysis of hexahistidine-tagged fusion proteins. Methods Enzymol. 328:141-157.
    • (2000) Methods Enzymol , vol.328 , pp. 141-157
    • Burgess, R.R.1    Arthur, T.M.2    Pietz, B.C.3
  • 10
    • 0037296380 scopus 로고    scopus 로고
    • Phage-display and correlated mutations identify an essential region of subdomain 1C involved in homodimerization of Escherichia coli FtsA
    • Carettoni D, et al. 2003. Phage-display and correlated mutations identify an essential region of subdomain 1C involved in homodimerization of Escherichia coli FtsA. Proteins 50:192-206.
    • (2003) Proteins , vol.50 , pp. 192-206
    • Carettoni, D.1
  • 11
    • 7744230898 scopus 로고    scopus 로고
    • A Z-ringindependent interaction between a subdomain of FtsA and late septation proteins as revealed by a polar recruitment assay
    • Corbin BD, Geissler B, Sadasivam M, Margolin W. 2004. A Z-ringindependent interaction between a subdomain of FtsA and late septation proteins as revealed by a polar recruitment assay. J. Bacteriol. 186:7736-7744.
    • (2004) J. Bacteriol. , vol.186 , pp. 7736-7744
    • Corbin, B.D.1    Geissler, B.2    Sadasivam, M.3    Margolin, W.4
  • 12
    • 34247859209 scopus 로고    scopus 로고
    • Interaction between cell division proteins FtsE and FtsZ
    • Corbin BD, Wang Y, Beuria TK, 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
  • 13
    • 0027167446 scopus 로고
    • Cloning and characterization of ftsN, an essential cell division gene in Escherichia coli isolated as a multicopy suppressor of ftsA12(Ts)
    • Dai K, Xu Y, Lutkenhaus J. 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
  • 14
    • 0029863071 scopus 로고    scopus 로고
    • Topological characterization of the essential Escherichia coli cell division protein FtsN
    • Dai K, Xu Y, Lutkenhaus J. 1996. Topological characterization of the essential Escherichia coli cell division protein FtsN. J. Bacteriol. 178:1328-1334.
    • (1996) J. Bacteriol. , vol.178 , pp. 1328-1334
    • Dai, K.1    Xu, Y.2    Lutkenhaus, J.3
  • 15
    • 0037067757 scopus 로고    scopus 로고
    • Interaction between FtsZ and FtsW of Mycobacterium tuberculosis
    • Datta P, Dasgupta A, Bhakta S, Basu J. 2002. Interaction between FtsZ and FtsW of Mycobacterium tuberculosis. J. Biol. Chem. 277:24983-24987.
    • (2002) J. Biol. Chem. , vol.277 , pp. 24983-24987
    • Datta, P.1    Dasgupta, A.2    Bhakta, S.3    Basu, J.4
  • 17
    • 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, 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.
    • (2003) Microbiology , vol.149 , pp. 3353-3359
    • Di Lallo, G.1    Fagioli, M.2    Barionovi, D.3    Ghelardini, P.4    Paolozzi, L.5
  • 19
    • 0036370454 scopus 로고    scopus 로고
    • Redox flow as an instrument of gene regulation
    • Eraso JM, Kaplan S. 2002. Redox flow as an instrument of gene regulation. Methods Enzymol. 348:216-229.
    • (2002) Methods Enzymol , vol.348 , pp. 216-229
    • Eraso, J.M.1    Kaplan, S.2
  • 20
    • 0030829601 scopus 로고    scopus 로고
    • FtsZ, a tubulin homologue in prokaryote division
    • Erickson HP. 1997. FtsZ, a tubulin homologue in prokaryote division. Trends Cell Biol. 7:362-367.
    • (1997) Trends Cell Biol , vol.7 , pp. 362-367
    • Erickson, H.P.1
  • 21
    • 0037386678 scopus 로고    scopus 로고
    • A gain of function mutation in ftsA bypasses the requirement for the essential cell division gene zipA in Escherichia coli
    • Geissler B, Elraheb D, Margolin W. 2003. A gain of function mutation in ftsA bypasses the requirement for the essential cell division gene zipA in Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 100:4197-4202.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 4197-4202
    • Geissler, B.1    Elraheb, D.2    Margolin, W.3
  • 22
    • 26944444295 scopus 로고    scopus 로고
    • Evidence for functional overlap amongmultiple bacterial cell division proteins: compensating for the loss of FtsK
    • Geissler B, Margolin W. 2005. Evidence for functional overlap amongmultiple 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
  • 23
    • 33947393232 scopus 로고    scopus 로고
    • The ftsA* gain-of-function allele of Escherichia coli and its effects on the stability and dynamics of the Z ring
    • Geissler B, Shiomi D, Margolin W. 2007. The ftsA* gain-of-function allele of Escherichia coli and its effects on the stability and dynamics of the Z ring. Microbiology 153:814-825.
    • (2007) Microbiology , vol.153 , pp. 814-825
    • Geissler B.Shiomi, D.1    Margolin, W.2
  • 24
    • 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 MA, et al. 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
  • 25
    • 33846650968 scopus 로고    scopus 로고
    • The trans-envelope Tol-Pal complex is part of the cell division machinery and required for proper outer-membrane invagination during cell constriction in E. coli
    • Gerding MA, Ogata Y, Pecora ND, Niki H, de Boer PA. 2007. The trans-envelope Tol-Pal complex is part of the cell division machinery and required for proper outer-membrane invagination during cell constriction in E. coli. Mol. Microbiol. 63:1008-1025.
    • (2007) Mol. Microbiol. , vol.63 , pp. 1008-1025
    • Gerding, M.A.1    Ogata, Y.2    Pecora, N.D.3    Niki, H.4    de Boer, P.A.5
  • 26
    • 0035861738 scopus 로고    scopus 로고
    • Crystal structure of MtaN, a global multidrug transporter gene activator
    • Godsey MH, Baranova NN, Neyfakh AA, Brennan RG. 2001. Crystal structure of MtaN, a global multidrug transporter gene activator. J. Biol. Chem. 276:47178-47184.
    • (2001) J. Biol. Chem. , vol.276 , pp. 47178-47184
    • Godsey, M.H.1    Baranova, N.N.2    Neyfakh, A.A.3    Brennan, R.G.4
  • 27
    • 21844441637 scopus 로고    scopus 로고
    • Diverse paths to midcell: assembly of the bacterial cell division machinery
    • Goehring NW, Beckwith J. 2005. Diverse paths to midcell: assembly of the bacterial cell division machinery. Curr. Biol. 15:514-526.
    • (2005) Curr. Biol. , vol.15 , pp. 514-526
    • Goehring, N.W.1    Beckwith, J.2
  • 28
    • 33745195461 scopus 로고    scopus 로고
    • Premature targeting of cell division proteins to midcell reveals hierarchies of protein interactions involved in divisome assembly
    • Goehring NW, Gonzalez MD, Beckwith J. 2006. Premature targeting of cell division proteins to midcell reveals hierarchies of protein interactions involved in divisome assembly. Mol. Microbiol. 61:33-45.
    • (2006) Mol. Microbiol. , vol.61 , pp. 33-45
    • Goehring, N.W.1    Gonzalez, M.D.2    Beckwith, J.3
  • 29
    • 11844267151 scopus 로고    scopus 로고
    • Premature targeting of a cell division protein to midcell allows dissection of divisome assembly in Escherichia coli
    • Goehring NW, Gueiros-Filho F, Beckwith J. 2005. Premature targeting of a cell division protein to midcell allows dissection of divisome assembly in Escherichia coli. Genes Dev. 19:127-137.
    • (2005) Genes Dev , vol.19 , pp. 127-137
    • Goehring, N.W.1    Gueiros-Filho, F.2    Beckwith, J.3
  • 30
    • 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 NW, Petrovska I, Boyd D, Beckwith J. 2007. 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
  • 31
    • 33846198296 scopus 로고    scopus 로고
    • A role for the nonessential N-terminus of FtsN in divisome assembly
    • Goehring NW, Robichon C, Beckwith J. 2007. A 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
  • 33
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter
    • Guzman LM, Belin D, Carson MJ, Beckwith J. 1995. Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. J. Bacteriol. 177:4121-4130.
    • (1995) J. Bacteriol. , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 34
    • 0025598302 scopus 로고
    • Sequence requirements for coiled-coils: analysis with lambda repressor-GCN4 leucine zipper fusions
    • Hu JC, O'Shea EK, Kim PS, Sauer RT. 1990. Sequence requirements for coiled-coils: analysis with lambda repressor-GCN4 leucine zipper fusions. Science 250:1400-1403.
    • (1990) Science , vol.250 , pp. 1400-1403
    • Hu, J.C.1    O'Shea, E.K.2    Kim, P.S.3    Sauer, R.T.4
  • 35
    • 24944469539 scopus 로고    scopus 로고
    • Cell division in Bacillus subtilis: FtsZ and FtsA association is Z-ring independent, and FtsA is required for efficient midcell Z-ring assembly
    • Jensen SO, Thompson LS, Harry EJ. 2005. Cell division in Bacillus subtilis: FtsZ and FtsA association is Z-ring independent, and FtsA is required for efficient midcell Z-ring assembly. J. Bacteriol. 187:6536-6544.
    • (2005) J. Bacteriol. , vol.187 , pp. 6536-6544
    • Jensen, S.O.1    Thompson, L.S.2    Harry, E.J.3
  • 36
    • 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, 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.
    • (2005) J. Bacteriol. , vol.187 , pp. 2233-2243
    • Karimova, G.1    Dautin, N.2    Ladant, D.3
  • 37
    • 0032510783 scopus 로고    scopus 로고
    • A bacterial twohybrid system based on a reconstituted signal transduction pathway
    • Karimova G, Pidoux J, Ullmann A, Ladant D. 1998. A bacterial twohybrid system based on a reconstituted signal transduction pathway. Proc. Natl. Acad. Sci. U. S. A. 95:5752-5756.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 5752-5756
    • Karimova, G.1    Pidoux, J.2    Ullmann, A.3    Ladant, D.4
  • 38
    • 79959912261 scopus 로고    scopus 로고
    • Structure of the PilM-PilN inner membrane type IV pilus biogenesis complex from Thermus thermophilus
    • Karuppiah V, Derrick JP. 2011. Structure of the PilM-PilN inner membrane type IV pilus biogenesis complex from Thermus thermophilus. J. Biol. Chem. 286:24434-24442.
    • (2011) J. Biol. Chem. , vol.286 , pp. 24434-24442
    • Karuppiah, V.1    Derrick, J.P.2
  • 39
    • 72449131554 scopus 로고    scopus 로고
    • FtsN-trigger for septation
    • Lutkenhaus J. 2009. FtsN-trigger for septation. J. Bacteriol. 191:7381-7392.
    • (2009) J. Bacteriol. , vol.191 , pp. 7381-7392
    • Lutkenhaus, J.1
  • 40
    • 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 DW, 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.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 12998-13003
    • Ma, X.1    Ehrhardt, D.W.2    Margolin, W.3
  • 41
    • 0032786248 scopus 로고    scopus 로고
    • Genetic and functional analyses of the conserved C-terminal core domain of Escherichia coli FtsZ
    • Ma X, Margolin W. 1999. Genetic and functional analyses of the conserved C-terminal core domain of Escherichia coli FtsZ. J. Bacteriol. 181: 7531-7544.
    • (1999) J. Bacteriol. , vol.181 , pp. 7531-7544
    • Ma, X.1    Margolin, W.2
  • 42
    • 0035210771 scopus 로고    scopus 로고
    • Dissociation and unfolding of GCN4 leucine zipper in the presence of sodium dodecyl sulfate
    • Meng FG, Zeng X, Hong YK, Zhou HM. 2001. Dissociation and unfolding of GCN4 leucine zipper in the presence of sodium dodecyl sulfate. Biochimie 83:953-956.
    • (2001) Biochimie , vol.83 , pp. 953-956
    • Meng, F.G.1    Zeng, X.2    Hong, Y.K.3    Zhou, H.M.4
  • 43
    • 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 NT, Dinh T, Bernhardt TG. 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
  • 44
    • 34248348211 scopus 로고    scopus 로고
    • Identification of a region of FtsA required for interaction with FtsZ
    • Pichoff S, Lutkenhaus J. 2007. Identification of a region of FtsA required for interaction with FtsZ. Mol. Microbiol. 64:1129-1138.
    • (2007) Mol. Microbiol. , vol.64 , pp. 1129-1138
    • Pichoff, S.1    Lutkenhaus, J.2
  • 45
    • 15744385269 scopus 로고    scopus 로고
    • Tethering the Z ring to the membrane through a conserved membrane targeting sequence in FtsA
    • Pichoff S, 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
  • 46
    • 0037084109 scopus 로고    scopus 로고
    • Unique and overlapping roles for ZipA and FtsA in septal ring assembly in Escherichia coli
    • Pichoff S, 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
  • 47
    • 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
  • 48
    • 4444300864 scopus 로고    scopus 로고
    • Role of two essential domains of Escherichia coli FtsA in localization and progression of the division ring
    • Rico AI, Garcia-Ovalle M, Mingorance J, 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
  • 49
    • 77951562635 scopus 로고    scopus 로고
    • Role of Escherichia coli FtsN protein in the assembly and stability of the cell division ring
    • Rico AI, Garcia-Ovalle M, Palacios P, Casanova M, 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
  • 50
    • 37749010497 scopus 로고    scopus 로고
    • Compensation for the loss of the conserved membrane targeting sequence of FtsA provides new insights into its function
    • Shiomi D, Margolin W. 2008. Compensation for the loss of the conserved membrane targeting sequence of FtsA provides new insights into its function. Mol. Microbiol. 67:558-569.
    • (2008) Mol. Microbiol. , vol.67 , pp. 558-569
    • Shiomi, D.1    Margolin, W.2
  • 51
    • 36549087126 scopus 로고    scopus 로고
    • Dimerization or oligomerization of the actin-like FtsA protein enhances the integrity of the cytokinetic Z ring
    • Shiomi D, 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
  • 52
    • 77951470447 scopus 로고    scopus 로고
    • Daughter cell separation is controlled by cytokinetic ring-activated cell wall hydrolysis
    • Uehara T, Parzych KR, Dinh T, Bernhardt TG. 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
  • 53
    • 0034675921 scopus 로고    scopus 로고
    • Crystal structure of the cell division protein FtsA from Thermotoga maritima
    • van den Ent F, Lowe 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    Lowe, J.2
  • 54
    • 33745209434 scopus 로고    scopus 로고
    • The order of the ring: assembly of Escherichia coli cell division components
    • Vicente M, Rico AI. 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
  • 55
    • 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 DS, Chen JC, Ghigo JM, Boyd D, 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
  • 56
    • 0030881627 scopus 로고    scopus 로고
    • Localization of the Escherichia coli cell division protein FtsI (PBP3) to the division site and cell pole
    • Weiss DS, et al. 1997. Localization of the Escherichia coli cell division protein FtsI (PBP3) to the division site and cell pole. Mol. Microbiol. 25:671-681.
    • (1997) Mol. Microbiol. , vol.25 , pp. 671-681
    • Weiss, D.S.1
  • 57
    • 0347915664 scopus 로고    scopus 로고
    • Genetic analysis of the cell division protein FtsI (PBP3): amino acid substitutions that impair septal localization of FtsI and recruitment of FtsN
    • Wissel MC, Weiss DS. 2004. Genetic analysis of the cell division protein FtsI (PBP3): amino acid substitutions that impair septal localization of FtsI and recruitment of FtsN. J. Bacteriol. 186:490-502.
    • (2004) J. Bacteriol. , vol.186 , pp. 490-502
    • Wissel, M.C.1    Weiss, D.S.2
  • 58
    • 81055145336 scopus 로고    scopus 로고
    • An ATP-binding cassette transporter-like complex governs cell-wall hydrolysis at the bacterial cytokinetic ring
    • Yang DC, et al. 2011. An ATP-binding cassette transporter-like complex governs cell-wall hydrolysis at the bacterial cytokinetic ring. Proc. Natl. Acad. Sci. U. S. A. 108:E1052-E1060.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108
    • Yang, D.C.1
  • 59
    • 2442631494 scopus 로고    scopus 로고
    • Solution structure and domain architecture of the divisome protein FtsN
    • Yang JC, Van Den Ent F, Neuhaus D, Brevier J, Lowe 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
  • 60
    • 0033760610 scopus 로고    scopus 로고
    • Role of the carboxy terminus of Escherichia coli FtsA in self-interaction and cell division
    • Yim L, et al. 2000. Role of the carboxy terminus of Escherichia coli FtsA in self-interaction and cell division. J. Bacteriol. 182:6366-6373.
    • (2000) J. Bacteriol. , vol.182 , pp. 6366-6373
    • Yim, L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.