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Volumn 189, Issue 22, 2007, Pages 8044-8052

Role of SufI (FtsP) in cell division of Escherichia coli: Evidence for its involvement in stabilizing the assembly of the divisome

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; FTSZ PROTEIN; PENICILLIN BINDING PROTEIN; PENICILLIN BINDING PROTEIN 3; PERIPLASMIC PROTEIN; PROTEIN FTSA 12; PROTEIN FTSK 44; PROTEIN FTSQ 1C; PROTEIN SUFI; UNCLASSIFIED DRUG;

EID: 36549022665     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00773-07     Document Type: Article
Times cited : (57)

References (50)
  • 2
    • 10744228022 scopus 로고    scopus 로고
    • Differential interactions between a twin-arginine signal peptide and its translocase in Escherichia coli
    • Alami, M., I. Luke, S. Deitermann, G. Eisner, H.-G. Koch, J. Brunner, and M. Muller. 2003. Differential interactions between a twin-arginine signal peptide and its translocase in Escherichia coli. Mol. Cell 12:937-946.
    • (2003) Mol. Cell , vol.12 , pp. 937-946
    • Alami, M.1    Luke, I.2    Deitermann, S.3    Eisner, G.4    Koch, H.-G.5    Brunner, J.6    Muller, M.7
  • 3
    • 15744405122 scopus 로고    scopus 로고
    • Protein targeting by the bacterial twin-arginine translocation (Tat) pathway
    • Berks, B. C., T. Palmer, and F. Sargent. 2005. Protein targeting by the bacterial twin-arginine translocation (Tat) pathway. Curr. Opin. Microbiol. 8:174-181.
    • (2005) Curr. Opin. Microbiol , vol.8 , pp. 174-181
    • Berks, B.C.1    Palmer, T.2    Sargent, F.3
  • 4
    • 34249811807 scopus 로고    scopus 로고
    • An altered FtsA can compensate for the loss of essential cell division protein FtsN in Escherichia coli
    • Bernard, C. S., M. Sadasivam, D. Shiomi, and W. Margolin. 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
  • 5
    • 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
  • 6
    • 2942538589 scopus 로고    scopus 로고
    • Screening for synthetic lethal mutants in Escherichia coli and identification of EnvC (YibP) as a periplasmic septal ring factor with murein hydrolase activity
    • Bernhardt, T. G., and P. A. de Boer. 2004. Screening for synthetic lethal mutants in Escherichia coli and identification of EnvC (YibP) as a periplasmic septal ring factor with murein hydrolase activity. Mol. Microbiol. 52: 1255-1269.
    • (2004) Mol. Microbiol , vol.52 , pp. 1255-1269
    • Bernhardt, T.G.1    de Boer, P.A.2
  • 7
    • 0026758369 scopus 로고
    • Cloning, characterization, and expression of the dapE gene of Escherichia coli
    • Bouvier, J., C. Richaud, W. Higgins, O. Bogler, and P. Stragier. 1992. Cloning, characterization, and expression of the dapE gene of Escherichia coli. J. Bacteriol. 174:5265-5271.
    • (1992) J. Bacteriol , vol.174 , pp. 5265-5271
    • Bouvier, J.1    Richaud, C.2    Higgins, W.3    Bogler, O.4    Stragier, P.5
  • 9
    • 0036900016 scopus 로고    scopus 로고
    • Assembly of cell division proteins at the E. coli cell center
    • Buddelmeijer, N., and J. Beckwith. 2002. Assembly of cell division proteins at the E. coli cell center. Curr. Opin. Microbiol. 5:553-557.
    • (2002) Curr. Opin. Microbiol , vol.5 , pp. 553-557
    • Buddelmeijer, N.1    Beckwith, J.2
  • 10
    • 0022683672 scopus 로고
    • Isolation of superoxide dismutase mutants in Escherichia coli: Is superoxide dismutase necessary for aerobic life?
    • Carloz, A., and D. Touati. 1986. Isolation of superoxide dismutase mutants in Escherichia coli: is superoxide dismutase necessary for aerobic life? EMBO J. 5:623-630.
    • (1986) EMBO J , vol.5 , pp. 623-630
    • Carloz, A.1    Touati, D.2
  • 11
    • 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
  • 13
    • 34547743871 scopus 로고    scopus 로고
    • Filamentous morphology in GroE-depleted Escherichia coli induced by impaired folding of FtsE
    • Fujiwara, K., and H. Taguchi. 2007. Filamentous morphology in GroE-depleted Escherichia coli induced by impaired folding of FtsE. J. Bacteriol. 189:5860-5866.
    • (2007) J. Bacteriol , vol.189 , pp. 5860-5866
    • Fujiwara, K.1    Taguchi, H.2
  • 14
    • 26944444295 scopus 로고    scopus 로고
    • Evidence for functional overlap among multiple bacterial cell division proteins: Compensating for the loss of FtsK
    • Geissler, B., and W. Margolin. 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
  • 15
    • 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., D. Elraheb, and W. Margolin. 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
  • 16
    • 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., D. Shiomi, and W. Margolin. 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.1    Shiomi, D.2    Margolin, W.3
  • 17
    • 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, M. A., Y. Ogata, N. D. Pecora, H. Niki, and P. A. de Boer. 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
  • 18
    • 21844441637 scopus 로고    scopus 로고
    • Diverse paths to midcell: Assembly of the bacterial cell division machinery
    • Goehring, N. W., and J. Beckwith. 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
  • 19
    • 0032934815 scopus 로고    scopus 로고
    • The regulation and role of the periplasmic copper, zinc superoxide dismutase of Escherichia coli
    • Gort, A. S., D. M. Ferber, and J. A. Imlay. 1999. The regulation and role of the periplasmic copper, zinc superoxide dismutase of Escherichia coli. Mol. Microbiol. 32:179-191.
    • (1999) Mol. Microbiol , vol.32 , pp. 179-191
    • Gort, A.S.1    Ferber, D.M.2    Imlay, J.A.3
  • 20
    • 0034817086 scopus 로고    scopus 로고
    • CueO is a multi-copper oxidase that confers copper tolerance in Escherichia coli
    • Grass, G., and C. Rensing. 2001. CueO is a multi-copper oxidase that confers copper tolerance in Escherichia coli. Biochem. Biophys. Res. Commun. 286: 902-908.
    • (2001) Biochem. Biophys. Res. Commun , vol.286 , pp. 902-908
    • Grass, G.1    Rensing, C.2
  • 21
    • 0025003789 scopus 로고
    • Trigger factor depletion or overproduction causes defective cell division but does not block protein export
    • Guthrie, B., and W. Wickner. 1990. Trigger factor depletion or overproduction causes defective cell division but does not block protein export. J. Bacteriol. 172:5555-5562.
    • (1990) J. Bacteriol , vol.172 , pp. 5555-5562
    • Guthrie, B.1    Wickner, W.2
  • 24
    • 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
  • 25
    • 0024075832 scopus 로고
    • Gene organization in the region containing a new gene involved in chromosome partition in Escherichia coli
    • Kato, J., Y. Nishimura, M. Yamada, H. Suzuki, and Y. Hirota. 1988. Gene organization in the region containing a new gene involved in chromosome partition in Escherichia coli. J. Bacteriol. 170:3967-3977.
    • (1988) J. Bacteriol , vol.170 , pp. 3967-3977
    • Kato, J.1    Nishimura, Y.2    Yamada, M.3    Suzuki, H.4    Hirota, Y.5
  • 26
    • 33749017348 scopus 로고    scopus 로고
    • Detection and quantification of superoxide formed within the periplasm of Escherichia coli
    • Korshunov, S., and J. A. Imlay. 2006. Detection and quantification of superoxide formed within the periplasm of Escherichia coli. J. Bacteriol. 188: 6326-6334.
    • (2006) J. Bacteriol , vol.188 , pp. 6326-6334
    • Korshunov, S.1    Imlay, J.A.2
  • 27
    • 0025769570 scopus 로고
    • Growth phase-regulated expression of bolA and morphology of stationary-phase Escherichia coli cells are controlled by the novel sigma factor sigma S
    • Lange, R., and R. Hengge-Aronis. 1991. Growth phase-regulated expression of bolA and morphology of stationary-phase Escherichia coli cells are controlled by the novel sigma factor sigma S. J. Bacteriol. 173:4474-4481.
    • (1991) J. Bacteriol , vol.173 , pp. 4474-4481
    • Lange, R.1    Hengge-Aronis, R.2
  • 28
  • 29
    • 0025088052 scopus 로고
    • Low copy number plasmids for regulated low-level expression of cloned genes in Escherichia coli with blue/white insert screening capability
    • Lerner, C. G., and M. Inouye. 1990. Low copy number plasmids for regulated low-level expression of cloned genes in Escherichia coli with blue/white insert screening capability. Nucleic Acids Res. 18:4631.
    • (1990) Nucleic Acids Res , vol.18 , pp. 4631
    • Lerner, C.G.1    Inouye, M.2
  • 30
    • 0031902183 scopus 로고    scopus 로고
    • FtsK is a bifunctional protein involved in cell division and chromosome localization in Escherichia coli
    • Liu, G., G. C. Draper, and W. D. Donachie. 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
  • 31
    • 0030956145 scopus 로고    scopus 로고
    • Bacterial cell division and the Z-ring
    • Lutkenhaus, J., and S. G. Addinall. 1997. Bacterial cell division and the Z-ring. Annu. Rev. Biochem. 66:93-116.
    • (1997) Annu. Rev. Biochem , vol.66 , pp. 93-116
    • Lutkenhaus, J.1    Addinall, S.G.2
  • 32
    • 0027954650 scopus 로고
    • DnaK mutants defective in ATPase activity are defective in negative regulation of the heat shock response: Expression of mutant DnaK proteins results in filamentation
    • McCarty, J. S., and G. C. Walker. 1994. DnaK mutants defective in ATPase activity are defective in negative regulation of the heat shock response: expression of mutant DnaK proteins results in filamentation. J. Bacteriol. 176:764-780.
    • (1994) J. Bacteriol , vol.176 , pp. 764-780
    • McCarty, J.S.1    Walker, G.C.2
  • 34
    • 0032539813 scopus 로고    scopus 로고
    • Inhibition of FtsZ polymerization by SulA, an inhibitor of cell septation in Escherichia coli
    • Mukherjee, A., C. Cao, and J. Lutkenhaus. 1998. Inhibition of FtsZ polymerization by SulA, an inhibitor of cell septation in Escherichia coli. Proc. Natl. Acad. Sci. USA 95:2885-2890.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 2885-2890
    • Mukherjee, A.1    Cao, C.2    Lutkenhaus, J.3
  • 35
    • 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
  • 37
    • 0032933919 scopus 로고    scopus 로고
    • SufS is a NifS-like protein, and SufD is necessary for stability of the [2Fe-2S] FhuF protein in Escherichia coli
    • Patzer, S. I., and K. Hantke. 1999. SufS is a NifS-like protein, and SufD is necessary for stability of the [2Fe-2S] FhuF protein in Escherichia coli. J. Bacteriol. 181:3307-3309.
    • (1999) J. Bacteriol , vol.181 , pp. 3307-3309
    • Patzer, S.I.1    Hantke, K.2
  • 38
    • 33845944955 scopus 로고    scopus 로고
    • Role of FtsEX in cell division of Escherichia coli: Viability of ftsEX mutants is dependent on functional SufI or high osmotic strength
    • Reddy, M. 2007. Role of FtsEX in cell division of Escherichia coli: viability of ftsEX mutants is dependent on functional SufI or high osmotic strength. J. Bacteriol. 189:98-108.
    • (2007) J. Bacteriol , vol.189 , pp. 98-108
    • Reddy, M.1
  • 41
    • 0034820331 scopus 로고    scopus 로고
    • HscA is involved in the dynamics of FtsZ-ring formation in Escherichia coli K12
    • Uehara, T., H. Matsuzawa, and A. Nishimura. 2001. HscA is involved in the dynamics of FtsZ-ring formation in Escherichia coli K12. Genes Cells 6:803-814.
    • (2001) Genes Cells , vol.6 , pp. 803-814
    • Uehara, T.1    Matsuzawa, H.2    Nishimura, A.3
  • 42
    • 4944223117 scopus 로고    scopus 로고
    • Murein (peptidoglycan) binding property of the essential cell division protein FtsN from Escherichia coli
    • Ursinus, A., F. van den Ent, S. Brechtel, M. de Pedro, J. V. Holtje, J. Lowe, and W. Vollmer. 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    Holtje, J.V.5    Lowe, J.6    Vollmer, W.7
  • 43
    • 33745209434 scopus 로고    scopus 로고
    • The order of the ring: Assembly of Escherichia coli cell division components
    • Vicente, M., and A. I. Rico. 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
  • 44
    • 0001078874 scopus 로고    scopus 로고
    • The SOS response of Escherichia coli
    • F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger ed, 2nd ed. American Society for Microbiology, Washington, DC
    • Walker, G. C. 1996. The SOS response of Escherichia coli, p. 1400-1416. In F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed. American Society for Microbiology, Washington, DC.
    • (1996) Escherichia coli and Salmonella: Cellular and molecular biology , pp. 1400-1416
    • Walker, G.C.1
  • 45
    • 0030873136 scopus 로고    scopus 로고
    • Promoters and transcripts associated with the aroP gene of Escherichia coli
    • Wang, P., J. Yang, and A. J. Pittard. 1997. Promoters and transcripts associated with the aroP gene of Escherichia coli. J. Bacteriol. 179:4206-4212.
    • (1997) J. Bacteriol , vol.179 , pp. 4206-4212
    • Wang, P.1    Yang, J.2    Pittard, A.J.3
  • 46
    • 0025941965 scopus 로고
    • A factor that positively regulates cell division by activating transcription of the major cluster of essential cell division genes of Escherichia coli
    • Wang, X. D., P. A. de Boer, and L. I. Rothfield. 1991. A factor that positively regulates cell division by activating transcription of the major cluster of essential cell division genes of Escherichia coli. EMBO J. 10:3363-3372.
    • (1991) EMBO J , vol.10 , pp. 3363-3372
    • Wang, X.D.1    de Boer, P.A.2    Rothfield, L.I.3
  • 47
    • 7644219685 scopus 로고    scopus 로고
    • Bacterial cell division and the septal ring
    • Weiss, D. S. 2004. Bacterial cell division and the septal ring. Mol. Microbiol. 54:588-597.
    • (2004) Mol. Microbiol , vol.54 , pp. 588-597
    • Weiss, D.S.1
  • 48
    • 0026701996 scopus 로고
    • The essential Escherichia coli msgB gene, a multicopy suppressor of a temperature-sensitive allele of the heat shock gene grpE, is identical to dapE
    • Wu, B., C. Georgopoulos, and D. Ang. 1992. The essential Escherichia coli msgB gene, a multicopy suppressor of a temperature-sensitive allele of the heat shock gene grpE, is identical to dapE. J. Bacteriol. 174:5258-5264.
    • (1992) J. Bacteriol , vol.174 , pp. 5258-5264
    • Wu, B.1    Georgopoulos, C.2    Ang, D.3
  • 49
    • 0035873543 scopus 로고    scopus 로고
    • Functional reconstitution of bacterial Tat translocation in vitro
    • Yahr, T. L., and W. T. Wickner. 2001. Functional reconstitution of bacterial Tat translocation in vitro. EMBO J. 20:2472-2479.
    • (2001) EMBO J , vol.20 , pp. 2472-2479
    • Yahr, T.L.1    Wickner, W.T.2


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