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Volumn 186, Issue 20, 2004, Pages 6728-6737

Murein (peptidoglycan) binding property of the essential cell division protein FtsN from Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

AMIDASE; AMINO ACID DERIVATIVE; BACTERIAL PROTEIN; CELL PROTEIN; GLYCAN; MUTANT PROTEIN; NEUROPEPTIDE; OUTER MEMBRANE PROTEIN; OUTER MEMBRANE PROTEIN A; PEPTIDE DERIVATIVE; PEPTIDOGLYCAN; PROTEIN FTSN; UNCLASSIFIED DRUG;

EID: 4944223117     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.186.20.6728-6737.2004     Document Type: Article
Times cited : (101)

References (64)
  • 1
    • 0030856502 scopus 로고    scopus 로고
    • FtsN, a late recruit to the septum in Escherichia coli
    • Addinall, S. G., C. Cao, and J. Lutkenhaus. 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
  • 2
    • 0030448723 scopus 로고    scopus 로고
    • FtsA is localized to the septum in an FtsZ-dependent manner
    • Addinall, S. G., and J. Lutkenhaus. 1996. FtsA is localized to the septum in an FtsZ-dependent manner. J. Bacteriol. 178:7167-7172.
    • (1996) J. Bacteriol. , vol.178 , pp. 7167-7172
    • Addinall, S.G.1    Lutkenhaus, J.2
  • 3
    • 0028839886 scopus 로고
    • A new Escherichia coli cell division gene, ftsK
    • Begg, K. J., S. J. Dewar, and W. D. Donachie. 1995. A new Escherichia coli cell division gene, ftsK. J. Bacteriol. 177:6211-6222.
    • (1995) J. Bacteriol. , vol.177 , pp. 6211-6222
    • Begg, K.J.1    Dewar, S.J.2    Donachie, W.D.3
  • 4
    • 0037783310 scopus 로고    scopus 로고
    • The Escherichia coli amidase AmiC is a periplasmic septal ring component exported via the twin-arginine transport pathway
    • Bernhardt, T. G., and P. A. de Boer. 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
  • 5
    • 0026059127 scopus 로고
    • FtsZ ring structure associated with division in Escherichia coli
    • Bi, E., and J. Lutkenhaus. 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
  • 7
    • 0031752827 scopus 로고    scopus 로고
    • Localization of cell division protein FtsQ by immunofluorescence microscopy in dividing and nondividing cells of Escherichia coli
    • Buddelmeijer, N., M. E. Aarsman, A. H. Kolk, M. Vicente, and N. Nanninga. 1998. Localization of cell division protein FtsQ by immunofluorescence microscopy in dividing and nondividing cells of Escherichia coli. J. Bacteriol. 180:6107-6116.
    • (1998) J. Bacteriol. , vol.180 , pp. 6107-6116
    • Buddelmeijer, N.1    Aarsman, M.E.2    Kolk, A.H.3    Vicente, M.4    Nanninga, N.5
  • 8
    • 0037197976 scopus 로고    scopus 로고
    • YgbQ, a cell division protein in Escherichia coli and Vibrio cholerae, localizes in codependent fashion with FtsL to the division site
    • Buddelmeijer, N., N. Judson, D. Boyd, J. J. Mekalanos, and J. Beckwith. 2002. YgbQ, a cell division protein in Escherichia coli and Vibrio cholerae, localizes in codependent fashion with FtsL to the division site. Proc. Natl. Acad. Sci. USA 99:6316-6321.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 6316-6321
    • Buddelmeijer, N.1    Judson, N.2    Boyd, D.3    Mekalanos, J.J.4    Beckwith, J.5
  • 9
    • 0025803531 scopus 로고
    • The FtsQ protein of Escherichia coli: Membrane topology, abundance, and cell division phenotypes due to overproduction and insertion mutations
    • Carson, M. J., J. Barondess, and J. Beckwith. 1991. The FtsQ protein of Escherichia coli: membrane topology, abundance, and cell division phenotypes due to overproduction and insertion mutations. J. Bacteriol. 173:2187-2195.
    • (1991) J. Bacteriol. , vol.173 , pp. 2187-2195
    • Carson, M.J.1    Barondess, J.2    Beckwith, J.3
  • 10
    • 0018956590 scopus 로고
    • Analysis of gene control signals by DNA fusion and cloning in Escherichia coli
    • Casabadan, M. J., and S. N. Cohen. 1980. Analysis of gene control signals by DNA fusion and cloning in Escherichia coli. J. Mol. Biol. 138:179-207.
    • (1980) J. Mol. Biol. , vol.138 , pp. 179-207
    • Casabadan, M.J.1    Cohen, S.N.2
  • 11
    • 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 J. Beckwith. 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
  • 12
    • 0025720073 scopus 로고
    • Synthesis of the cell surface during the division cycle of rod-shaped, gram-negative bacteria
    • Cooper, S. 1991. Synthesis of the cell surface during the division cycle of rod-shaped, gram-negative bacteria. Microbiol. Rev. 55:649-674.
    • (1991) Microbiol. Rev. , vol.55 , pp. 649-674
    • Cooper, S.1
  • 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., Y. Xu, and J. Lutkenhaus. 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., Y. Xu, and J. Lutkenhaus. 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
    • 0031824694 scopus 로고    scopus 로고
    • Characterization of the essential cell division gene ftsL(yIID) of Bacillus subtilis and its role in the assembly of the division apparatus
    • Daniel, R. A., E. J. Harry, V. L. Katis, R. G. Wake, and J. Errington. 1998. Characterization of the essential cell division gene ftsL(yIID) of Bacillus subtilis and its role in the assembly of the division apparatus. Mol. Microbiol. 29:593-604.
    • (1998) Mol. Microbiol. , vol.29 , pp. 593-604
    • Daniel, R.A.1    Harry, E.J.2    Katis, V.L.3    Wake, R.G.4    Errington, J.5
  • 16
    • 0026705484 scopus 로고
    • The essential bacterial cell-division protein FtsZ is a GTPase
    • de Boer, P., R. Crossley, and L. Rothfield. 1992. The essential bacterial cell-division protein FtsZ is a GTPase. Nature 359:254-256.
    • (1992) Nature , vol.359 , pp. 254-256
    • De Boer, P.1    Crossley, R.2    Rothfield, L.3
  • 18
    • 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., M. Fagioli, D. Barionovi, P. Ghelardini, and L. Paolozzi. 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
    • 0029956443 scopus 로고    scopus 로고
    • Direct quantitation of the number of individual penicillin-binding proteins per cell in Escherichia coli
    • Dougherty, T. J., K. Kennedy, R. E. Kessler, and M. J. Pucci. 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
  • 21
    • 0035146299 scopus 로고    scopus 로고
    • The FtsZ protofilament and attachment of ZipA-structural constraints on the FtsZ power stroke
    • Erickson, H. P. 2001. The FtsZ protofilament and attachment of ZipA-structural constraints on the FtsZ power stroke. Curr. Opin. Cell Biol. 13:55-60.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 55-60
    • Erickson, H.P.1
  • 22
    • 0025123204 scopus 로고
    • Differential effect of mutational impairment of penicillin-binding proteins 1A and 1B on Escherichia coli strains harboring thermosensitive mutations in the cell division genes ftsA, ftsQ, ftsZ, and pbpB
    • Garcia del Portillo, F., and M. A. de Pedro. 1990. Differential effect of mutational impairment of penicillin-binding proteins 1A and 1B on Escherichia coli strains harboring thermosensitive mutations in the cell division genes ftsA, ftsQ, ftsZ, and pbpB. J. Bacteriol. 172:5863-5870.
    • (1990) J. Bacteriol. , vol.172 , pp. 5863-5870
    • Garcia Del Portillo, F.1    De Pedro, M.A.2
  • 23
    • 0033986953 scopus 로고    scopus 로고
    • Cell division in Escherichia coli: Role of FtsL domains in septal localization, function, and oligomerization
    • Ghigo, J. M., and J. Beckwith. 2000. Cell division in Escherichia coli: role of FtsL domains in septal localization, function, and oligomerization. J. Bacteriol. 182:116-129.
    • (2000) J. Bacteriol. , vol.182 , pp. 116-129
    • Ghigo, J.M.1    Beckwith, J.2
  • 24
    • 0023765918 scopus 로고
    • Separation and quantification of muropeptides with high-performance liquid chromatography
    • Glauner, B. 1988. Separation and quantification of muropeptides with high-performance liquid chromatography. Anal. Biochem. 172:451-464.
    • (1988) Anal. Biochem. , vol.172 , pp. 451-464
    • Glauner, B.1
  • 25
    • 0025168851 scopus 로고
    • Growth pattern of the murein sacculus of Escherichia coli
    • Glauner, B., and J. V. Höltje. 1990. Growth pattern of the murein sacculus of Escherichia coli. J. Biol. Chem. 265:18988-18996.
    • (1990) J. Biol. Chem. , vol.265 , pp. 18988-18996
    • Glauner, B.1    Höltje, J.V.2
  • 26
    • 0023677844 scopus 로고
    • The composition of the murein of Escherichia coli
    • Glauner, B., J. V. Höltje, and U. Schwarz. 1988. The composition of the murein of Escherichia coli. J. Biol. Chem. 263:10088-10095.
    • (1988) J. Biol. Chem. , vol.263 , pp. 10088-10095
    • Glauner, B.1    Höltje, J.V.2    Schwarz, U.3
  • 27
    • 0027062784 scopus 로고
    • FtsL, an essential cytoplasmic membrane protein involved in cell division in Escherichia coli
    • Guzman, L. M., J. J. Barondess, and J. Beckwith. 1992. FtsL, an essential cytoplasmic membrane protein involved in cell division in Escherichia coli. J. Bacteriol. 174:7716-7728.
    • (1992) J. Bacteriol. , vol.174 , pp. 7716-7728
    • Guzman, L.M.1    Barondess, J.J.2    Beckwith, J.3
  • 29
    • 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 P. A. de Boer. 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
  • 30
    • 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 P. A. de Boer. 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
  • 31
    • 0003448569 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Harlow, E., and D. Lane. 1988. Antibodies: a laboratory manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1988) Antibodies: A Laboratory Manual
    • Harlow, E.1    Lane, D.2
  • 32
    • 0015522555 scopus 로고
    • Targets of penicillin action in Escherichia coli
    • Hartmann, R., J. V. Höltje, and U. Schwarz. 1972. Targets of penicillin action in Escherichia coli. Nature 235:426-429.
    • (1972) Nature , vol.235 , pp. 426-429
    • Hartmann, R.1    Höltje, J.V.2    Schwarz, U.3
  • 33
    • 0025012287 scopus 로고
    • Isolation und separation of the glycan strands from murein of Escherichia coli by reversed phase high-performance liquid chromatography
    • Harz, H., K. Burgdorf, and J. V. Höltje. 1990. Isolation und separation of the glycan strands from murein of Escherichia coli by reversed phase high-performance liquid chromatography. Anal. Biochem. 190:120-128.
    • (1990) Anal. Biochem. , vol.190 , pp. 120-128
    • Harz, H.1    Burgdorf, K.2    Höltje, J.V.3
  • 35
    • 0038460119 scopus 로고    scopus 로고
    • Role of the Escherichia coli Tat pathway in outer membrane integrity
    • Ize, B., N. R. Stanley, G. Buchanan, and T. Palmer. 2003. Role of the Escherichia coli Tat pathway in outer membrane integrity. Mol. Microbiol. 48:1183-1193.
    • (2003) Mol. Microbiol. , vol.48 , pp. 1183-1193
    • Ize, B.1    Stanley, N.R.2    Buchanan, G.3    Palmer, T.4
  • 36
    • 0032720310 scopus 로고    scopus 로고
    • Interference with murein turnover has no effect on growth but reduces β-lactamase induction in Escherichia coli
    • Kraft, A. R., J. Prabhu, A. Ursinus, and J. V. Höltje. 1999. Interference with murein turnover has no effect on growth but reduces β-lactamase induction in Escherichia coli. J. Bacteriol. 181:7192-7198.
    • (1999) J. Bacteriol. , vol.181 , pp. 7192-7198
    • Kraft, A.R.1    Prabhu, J.2    Ursinus, A.3    Höltje, J.V.4
  • 37
    • 0026621146 scopus 로고
    • Interactions of Escherichia coli membrane lipoproteins with the murein sacculus
    • Leduc, M., K. Ishidate, N. Shakibai, and L. Rothfield. 1992. Interactions of Escherichia coli membrane lipoproteins with the murein sacculus. J. Bacteriol. 174:7982-7988.
    • (1992) J. Bacteriol. , vol.174 , pp. 7982-7988
    • Leduc, M.1    Ishidate, K.2    Shakibai, N.3    Rothfield, L.4
  • 38
    • 0033028421 scopus 로고    scopus 로고
    • Recruitment of ZipA to the division site by interaction with FtsZ
    • Liu, Z., A. Mukherjee, and J. Lutkenhaus. 1999. Recruitment of ZipA to the division site by interaction with FtsZ. Mol. Microbiol. 31:1853-1861.
    • (1999) Mol. Microbiol. , vol.31 , pp. 1853-1861
    • Liu, Z.1    Mukherjee, A.2    Lutkenhaus, J.3
  • 39
    • 2642593025 scopus 로고    scopus 로고
    • Crystal structure of the bacterial cell-division protein FtsZ
    • Lowe, J., and L. A. Amos. 1998. Crystal structure of the bacterial cell-division protein FtsZ. Nature 391:203-206.
    • (1998) Nature , vol.391 , pp. 203-206
    • Lowe, J.1    Amos, L.A.2
  • 40
    • 0037495314 scopus 로고    scopus 로고
    • 2+-induced FtsZ sheets
    • 2+-induced FtsZ sheets. EMBO J. 18:2364-2371.
    • (1999) EMBO J. , vol.18 , pp. 2364-2371
    • Lowe, J.1    Amos, L.A.2
  • 41
    • 0016841078 scopus 로고
    • Electrophoretic resolution of the "major outer membrane protein" of Escherichia coli K12 into four bands
    • Lutgenberg, B. J., J. Meijers, R. Peters, P. van der Hoek. and L. van Alphen. 1975. Electrophoretic resolution of the "major outer membrane protein" of Escherichia coli K12 into four bands. FEBS Lett. 58:254-258.
    • (1975) FEBS Lett. , vol.58 , pp. 254-258
    • Lutgenberg, B.J.1    Meijers, J.2    Peters, R.3    Van Der Hoek, P.4    Van Alphen, L.5
  • 42
    • 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., D. W. Ehrhardt, and W. Margolin. 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 93:12998-13003.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12998-13003
    • Ma, X.1    Ehrhardt, D.W.2    Margolin, W.3
  • 43
    • 0030681278 scopus 로고    scopus 로고
    • Interactions between heterologous FtsA and FtsZ proteins at the FtsZ ring
    • Ma, X., Q. Sun, R. Wang, G. Singh, E. L. Jonietz, and W. Margolin. 1997. Interactions between heterologous FtsA and FtsZ proteins at the FtsZ ring. J. Bacteriol. 179:6788-6797.
    • (1997) J. Bacteriol. , vol.179 , pp. 6788-6797
    • Ma, X.1    Sun, Q.2    Wang, R.3    Singh, G.4    Jonietz, E.L.5    Margolin, W.6
  • 44
    • 0033823009 scopus 로고    scopus 로고
    • Themes and variations in prokaryotic cell division
    • Margolin, W. 2000. Themes and variations in prokaryotic cell division. FEMS Microbiol. Rev. 24:531-548.
    • (2000) FEMS Microbiol. Rev. , vol.24 , pp. 531-548
    • Margolin, W.1
  • 45
    • 0141994975 scopus 로고    scopus 로고
    • Cryotransmission electron microscopy of frozen-hydrated sections of Escherichia coli and Pseudomonas aeruginosa
    • Matias, V. R., A. Al-Amoudi, J. Dubochet, and T. J. Beveridge. 2003. Cryotransmission electron microscopy of frozen-hydrated sections of Escherichia coli and Pseudomonas aeruginosa, J. Bacteriol. 185:6112-6118.
    • (2003) J. Bacteriol. , vol.185 , pp. 6112-6118
    • Matias, V.R.1    Al-Amoudi, A.2    Dubochet, J.3    Beveridge, T.J.4
  • 46
    • 0036155122 scopus 로고    scopus 로고
    • The Escherichia coli cell division protein FtsW is required to recruit its cognate transpeptidase, FtsI (PBP3), to the division site
    • Mercer, K. L., and D. S. Weiss. 2002. The Escherichia coli cell division protein FtsW is required to recruit its cognate transpeptidase, FtsI (PBP3), to the division site. J. Bacteriol. 184:904-912.
    • (2002) J. Bacteriol. , vol.184 , pp. 904-912
    • Mercer, K.L.1    Weiss, D.S.2
  • 47
    • 0034966992 scopus 로고    scopus 로고
    • Cytokinesis in prokaryotes and eukaryotes: Common principles and different solutions
    • Nanninga, N. 2001. Cytokinesis in prokaryotes and eukaryotes: common principles and different solutions. Microbiol. Mol. Biol. Rev. 65:319-333.
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 319-333
    • Nanninga, N.1
  • 49
    • 0037084109 scopus 로고    scopus 로고
    • Unique and overlapping roles for ZipA and FtsA in septal ring assembly in Escherichia coli
    • Pichoff, S., and J. Lutkenhaus. 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
  • 50
    • 0030806966 scopus 로고    scopus 로고
    • MinCD-independent inhibition of cell division by a protein that fuses MalE to the topological specificity factor MinE
    • Pichoff, S., B. Vollrath, and J. P. Bouche. 1997. MinCD-independent inhibition of cell division by a protein that fuses MalE to the topological specificity factor MinE. J. Bacteriol. 179:4616-4619.
    • (1997) J. Bacteriol. , vol.179 , pp. 4616-4619
    • Pichoff, S.1    Vollrath, B.2    Bouche, J.P.3
  • 51
    • 0038010148 scopus 로고    scopus 로고
    • Protein-peptidoglycan interactions modulate the assembly of the needle complex in the Salmonella invasion-associated type III secretion system
    • Pucciarelli, M. G., and F. Garcia del Portillo. 2003. Protein-peptidoglycan interactions modulate the assembly of the needle complex in the Salmonella invasion-associated type III secretion system. Mol. Microbiol. 48:573-585.
    • (2003) Mol. Microbiol. , vol.48 , pp. 573-585
    • Pucciarelli, M.G.1    Garcia Del Portillo, F.2
  • 52
    • 0026778964 scopus 로고
    • Escherichia coli cell division gene ftsZ encodes a novel GTP-binding protein
    • Raychaudhuri, D., and J. T. Park. 1992. Escherichia coli cell division gene ftsZ encodes a novel GTP-binding protein. Nature 359:251-254.
    • (1992) Nature , vol.359 , pp. 251-254
    • Raychaudhuri, D.1    Park, J.T.2
  • 53
    • 0016350456 scopus 로고
    • Characterization of the major envelope protein from Escherichia coli. Regular arrangement on the peptidoglycan and unusual dodecyl sulfate binding
    • Rosenbusch, J. P. 1974. Characterization of the major envelope protein from Escherichia coli. Regular arrangement on the peptidoglycan and unusual dodecyl sulfate binding. J. Biol. Chem. 249:8019-8029.
    • (1974) J. Biol. Chem. , vol.249 , pp. 8019-8029
    • Rosenbusch, J.P.1
  • 55
    • 0034675921 scopus 로고    scopus 로고
    • Crystal structure of the cell division protein FtsA from Thermotoga maritima
    • van den Ent, F., and J. Löwe. 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
  • 56
    • 0033525526 scopus 로고    scopus 로고
    • Demonstration of molecular interactions between the murein polymerase PBP1B, the lytic transglycosylase MltA, and the scaffolding protein MipA of Escherichia coli
    • Vollmer, W., M. von Rechenberg, and J. V. Höltje. 1999. Demonstration of molecular interactions between the murein polymerase PBP1B, the lytic transglycosylase MltA, and the scaffolding protein MipA of Escherichia coli. J. Biol. Chem. 274:6726-6734.
    • (1999) J. Biol. Chem. , vol.274 , pp. 6726-6734
    • Vollmer, W.1    Von Rechenberg, M.2    Höltje, J.V.3
  • 57
    • 0032453738 scopus 로고    scopus 로고
    • FtsI and FtsW are localized to the septum in Escherichia coli
    • Wang, L., M. K. Khattar, W. D. Donachie, and J. Lutkenhaus. 1998. FtsI and FtsW are localized to the septum in Escherichia coli. J. Bacteriol. 180:2810-2816.
    • (1998) J. Bacteriol. , vol.180 , pp. 2810-2816
    • Wang, L.1    Khattar, M.K.2    Donachie, W.D.3    Lutkenhaus, J.4
  • 58
    • 0025782890 scopus 로고
    • Construction of versatile low-copy-number vectors for cloning, sequencing and gene expression in Escherichia coli
    • Wang, R. F., and S. R. Kushner. 1991. Construction of versatile low-copy-number vectors for cloning, sequencing and gene expression in Escherichia coli. Gene 100:195-199.
    • (1991) Gene , vol.100 , pp. 195-199
    • Wang, R.F.1    Kushner, S.R.2
  • 59
    • 0030931117 scopus 로고    scopus 로고
    • Analysis of the interaction of FtsZ with itself, GTP, and FtsA
    • Wang, X., J. Huang, A. Mukherjee, C. Cao, and J. Lutkenhaus. 1997. Analysis of the interaction of FtsZ with itself, GTP, and FtsA. J. Bacteriol. 179:5551-5559.
    • (1997) J. Bacteriol. , vol.179 , pp. 5551-5559
    • Wang, X.1    Huang, J.2    Mukherjee, A.3    Cao, C.4    Lutkenhaus, J.5
  • 60
    • 0036291172 scopus 로고    scopus 로고
    • The function of OmpA in Escherichia coli
    • Wang, Y. 2002. The function of OmpA in Escherichia coli. Biochem. Biophys. Res. Commun. 292:396-401.
    • (2002) Biochem. Biophys. Res. Commun. , vol.292 , pp. 396-401
    • Wang, Y.1
  • 61
    • 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., J. C. Chen, J. M. Ghigo, D. Boyd, and J. Beckwith. 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
  • 63
    • 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, M. C., and D. S. Weiss. 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
  • 64
    • 2442631494 scopus 로고    scopus 로고
    • Solution structure and domain architecture of the divisome protein FtsN
    • Yang, J. C., F. van den Ent, D. Neuhaus, J. Brevier, and J. Löwe. 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.