메뉴 건너뛰기




Volumn 162, Issue 2-4, 2013, Pages 831-841

Analysis of a ferric uptake regulator (Fur) knockout mutant in Aeromonas salmonicida subsp. salmonicida

Author keywords

Aeromonas salmonicida; Ferric uptake regulator; Iron regulated; Outer membrane proteins; Proteomics

Indexed keywords

FERRIC UPTAKE REGULATOR; IRON; OUTER MEMBRANE PROTEIN C; SIDEROPHORE;

EID: 84872490975     PISSN: 03781135     EISSN: 18732542     Source Type: Journal    
DOI: 10.1016/j.vetmic.2012.10.038     Document Type: Article
Times cited : (26)

References (59)
  • 1
    • 0031045576 scopus 로고    scopus 로고
    • The fur gene from Klebsiella pneumoniae: characterization, genomic organization and phylogenetic analysis
    • Achenbach L.A., Yang W. The fur gene from Klebsiella pneumoniae: characterization, genomic organization and phylogenetic analysis. Gene 1997, 185:201-207.
    • (1997) Gene , vol.185 , pp. 201-207
    • Achenbach, L.A.1    Yang, W.2
  • 3
    • 0030586726 scopus 로고    scopus 로고
    • Effect of iron on expression of superoxide dismutase by Aeromonas salmonicida and associated resistance to superoxide anion
    • Barnes A.C., Horne M.C., Ellis A.E. Effect of iron on expression of superoxide dismutase by Aeromonas salmonicida and associated resistance to superoxide anion. FEMS Microbiol. Lett. 1996, 142:19-26.
    • (1996) FEMS Microbiol. Lett. , vol.142 , pp. 19-26
    • Barnes, A.C.1    Horne, M.C.2    Ellis, A.E.3
  • 4
    • 0027440781 scopus 로고
    • Identification and cloning of a fur homolog from Neisseria gonorrhoeae
    • Berish S.A., Subbarao S., Chen C.Y., Trees D.L., Morse S.A. Identification and cloning of a fur homolog from Neisseria gonorrhoeae. Infect. Immun. 1993, 61:4599-4606.
    • (1993) Infect. Immun. , vol.61 , pp. 4599-4606
    • Berish, S.A.1    Subbarao, S.2    Chen, C.Y.3    Trees, D.L.4    Morse, S.A.5
  • 5
    • 0035862444 scopus 로고    scopus 로고
    • Cloning, overexpression and interaction of recombinant Fur from the cyanobacterium Anabaena PCC 7119 with isiB and its own promoter
    • Bes M.T., Hernandez J.A., Peleato M.L., Fillat M.F. Cloning, overexpression and interaction of recombinant Fur from the cyanobacterium Anabaena PCC 7119 with isiB and its own promoter. FEMS Microbiol. Lett. 2001, 194:187-192.
    • (2001) FEMS Microbiol. Lett. , vol.194 , pp. 187-192
    • Bes, M.T.1    Hernandez, J.A.2    Peleato, M.L.3    Fillat, M.F.4
  • 9
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 10
    • 0032946645 scopus 로고    scopus 로고
    • Bacterial solutions to the iron-supply problem
    • Braun V., Killmann H. Bacterial solutions to the iron-supply problem. Trends Biochem. Sci. 1999, 24:104-109.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 104-109
    • Braun, V.1    Killmann, H.2
  • 11
    • 3242881125 scopus 로고    scopus 로고
    • Responsiveness to acidity via metal ion regulators mediates virulence in the gastric pathogen Helicobacter pylori
    • Bury-Mone S., Thiberge J.M., Contreras M., Maitournam A., Labigne A., De Reuse H. Responsiveness to acidity via metal ion regulators mediates virulence in the gastric pathogen Helicobacter pylori. Mol. Microbiol. 2004, 53:623-638.
    • (2004) Mol. Microbiol. , vol.53 , pp. 623-638
    • Bury-Mone, S.1    Thiberge, J.M.2    Contreras, M.3    Maitournam, A.4    Labigne, A.5    De Reuse, H.6
  • 12
    • 0021052962 scopus 로고
    • Acquisition of iron by Aeromonas salmonicida
    • Chart H., Trust T.J. Acquisition of iron by Aeromonas salmonicida. J. Bacteriol. 1983, 156:758-764.
    • (1983) J. Bacteriol. , vol.156 , pp. 758-764
    • Chart, H.1    Trust, T.J.2
  • 13
    • 1842870790 scopus 로고    scopus 로고
    • Cloning, characterisation and phylogenetic analysis of the fur gene in Vibrio salmonicida and Vibrio logei
    • Colquhoun D.J., Sorum H. Cloning, characterisation and phylogenetic analysis of the fur gene in Vibrio salmonicida and Vibrio logei. Gene 2002, 296:213-220.
    • (2002) Gene , vol.296 , pp. 213-220
    • Colquhoun, D.J.1    Sorum, H.2
  • 14
    • 0025942194 scopus 로고
    • Structural dynamics and functional domains of the fur protein
    • Coy M., Neilands J.B. Structural dynamics and functional domains of the fur protein. Biochemistry 1991, 30:8201-8210.
    • (1991) Biochemistry , vol.30 , pp. 8201-8210
    • Coy, M.1    Neilands, J.B.2
  • 15
  • 16
    • 0024276112 scopus 로고
    • Fur (ferric uptake regulation) protein and CAP (catabolite-activator protein) modulate transcription of fur gene in Escherichia coli
    • De Lorenzo V., Herrero M., Giovannini F., Neilands J.B. Fur (ferric uptake regulation) protein and CAP (catabolite-activator protein) modulate transcription of fur gene in Escherichia coli. Eur. J. Biochem. 1988, 173:537-546.
    • (1988) Eur. J. Biochem. , vol.173 , pp. 537-546
    • De Lorenzo, V.1    Herrero, M.2    Giovannini, F.3    Neilands, J.B.4
  • 18
    • 0036436311 scopus 로고    scopus 로고
    • Autoregulation of Helicobacter pylori Fur revealed by functional analysis of the iron-binding site
    • Delany I., Spohn G., Pacheco A.B., Ieva R., Alaimo C., Rappuoli R., Scarlato V. Autoregulation of Helicobacter pylori Fur revealed by functional analysis of the iron-binding site. Mol. Microbiol. 2002, 46:1107-1122.
    • (2002) Mol. Microbiol. , vol.46 , pp. 1107-1122
    • Delany, I.1    Spohn, G.2    Pacheco, A.B.3    Ieva, R.4    Alaimo, C.5    Rappuoli, R.6    Scarlato, V.7
  • 19
    • 1842476060 scopus 로고    scopus 로고
    • Differential proteomic analysis of Aeromonas salmonicida outer membrane proteins in response to low iron and in vivo growth conditions
    • Ebanks R.O., Dacanay A., Goguen M., Pinto D.M., Ross N.W. Differential proteomic analysis of Aeromonas salmonicida outer membrane proteins in response to low iron and in vivo growth conditions. Proteomics 2004, 4:1074-1085.
    • (2004) Proteomics , vol.4 , pp. 1074-1085
    • Ebanks, R.O.1    Dacanay, A.2    Goguen, M.3    Pinto, D.M.4    Ross, N.W.5
  • 20
    • 0344172832 scopus 로고    scopus 로고
    • Opening the iron box: transcriptional metalloregulation by the Fur protein
    • Escolar L., Perez-Martin J., de Lorenzo V. Opening the iron box: transcriptional metalloregulation by the Fur protein. J. Bacteriol. 1999, 181:6223-6229.
    • (1999) J. Bacteriol. , vol.181 , pp. 6223-6229
    • Escolar, L.1    Perez-Martin, J.2    de Lorenzo, V.3
  • 21
    • 0032547113 scopus 로고    scopus 로고
    • Siderophore production by Aeromonas salmonicida subsp. salmonicida. Lack of strain specificity
    • Fernandez A.I., Fernandez A.F., Perez M.J., Nieto T.P., Ellis A.E. Siderophore production by Aeromonas salmonicida subsp. salmonicida. Lack of strain specificity. Dis. Aquat. Organ. 1998, 33:87-92.
    • (1998) Dis. Aquat. Organ. , vol.33 , pp. 87-92
    • Fernandez, A.I.1    Fernandez, A.F.2    Perez, M.J.3    Nieto, T.P.4    Ellis, A.E.5
  • 22
    • 0026661296 scopus 로고
    • Effect of Salmonella typhimurium ferric uptake regulator (fur) mutations on iron- and pH-regulated protein synthesis
    • Foster J.W., Hall H.K. Effect of Salmonella typhimurium ferric uptake regulator (fur) mutations on iron- and pH-regulated protein synthesis. J. Bacteriol. 1992, 174:4317-4323.
    • (1992) J. Bacteriol. , vol.174 , pp. 4317-4323
    • Foster, J.W.1    Hall, H.K.2
  • 23
    • 0028293026 scopus 로고
    • Regulatory circuits involved with pH-regulated gene expression in Salmonella typhimurium
    • Foster J.W., Park Y.K., Bang I.S., Karem K., Betts H., Hall H.K., Shaw E. Regulatory circuits involved with pH-regulated gene expression in Salmonella typhimurium. Microbiology 1994, 140(Pt 2):341-352.
    • (1994) Microbiology , vol.140 , Issue.PART 2 , pp. 341-352
    • Foster, J.W.1    Park, Y.K.2    Bang, I.S.3    Karem, K.4    Betts, H.5    Hall, H.K.6    Shaw, E.7
  • 24
    • 0020039866 scopus 로고
    • Isolation of intracellular membranes by means of sodium carbonate treatment: application to endoplasmic reticulum
    • Fujiki Y., Hubbard A.L., Fowler S., Lazarow P.B. Isolation of intracellular membranes by means of sodium carbonate treatment: application to endoplasmic reticulum. J. Cell Biol. 1982, 93:97-102.
    • (1982) J. Cell Biol. , vol.93 , pp. 97-102
    • Fujiki, Y.1    Hubbard, A.L.2    Fowler, S.3    Lazarow, P.B.4
  • 25
    • 0027485163 scopus 로고
    • Role of acid tolerance response genes in Salmonella typhimurium virulence
    • Garcia-del Portillo F., Foster J.W., Finlay B.B. Role of acid tolerance response genes in Salmonella typhimurium virulence. Infect. Immun. 1993, 61:4489-4492.
    • (1993) Infect. Immun. , vol.61 , pp. 4489-4492
    • Garcia-del Portillo, F.1    Foster, J.W.2    Finlay, B.B.3
  • 26
    • 0000311380 scopus 로고    scopus 로고
    • Identification of the two zinc-bound cysteines in the ferric uptake regulation protein from Escherichia coli: chemical modification and mass spectrometry analysis
    • Gonzalez de Peredo A., Saint-Pierre C., Adrait A., Jacquamet L., Latour J.M., Michaud-Soret I., Forest E. Identification of the two zinc-bound cysteines in the ferric uptake regulation protein from Escherichia coli: chemical modification and mass spectrometry analysis. Biochemistry 1999, 38:8582-8589.
    • (1999) Biochemistry , vol.38 , pp. 8582-8589
    • Gonzalez de Peredo, A.1    Saint-Pierre, C.2    Adrait, A.3    Jacquamet, L.4    Latour, J.M.5    Michaud-Soret, I.6    Forest, E.7
  • 27
    • 0021294830 scopus 로고
    • Role of iron in oxygen radical reactions
    • Halliwell B., Gutteridge J.M. Role of iron in oxygen radical reactions. Methods Enzymol. 1984, 105:47-56.
    • (1984) Methods Enzymol. , vol.105 , pp. 47-56
    • Halliwell, B.1    Gutteridge, J.M.2
  • 28
    • 0023443062 scopus 로고
    • Selection procedure for deregulated iron transport mutants (fur) in Escherichia coli K 12: fur not only affects iron metabolism
    • Hantke K. Selection procedure for deregulated iron transport mutants (fur) in Escherichia coli K 12: fur not only affects iron metabolism. Mol. Gen. Genet. 1987, 210:135-139.
    • (1987) Mol. Gen. Genet. , vol.210 , pp. 135-139
    • Hantke, K.1
  • 29
    • 0036263534 scopus 로고    scopus 로고
    • Molecular cloning of the fur gene from Actinobacillus actinomycetemcomitans
    • Haraszthy V.I., Lally E.T., Haraszthy G.G., Zambon J.J. Molecular cloning of the fur gene from Actinobacillus actinomycetemcomitans. Infect. Immun. 2002, 70:3170-3179.
    • (2002) Infect. Immun. , vol.70 , pp. 3170-3179
    • Haraszthy, V.I.1    Lally, E.T.2    Haraszthy, G.G.3    Zambon, J.J.4
  • 30
    • 0031058129 scopus 로고    scopus 로고
    • An operon containing fumC and sodA encoding fumarase C and manganese superoxide dismutase is controlled by the ferric uptake regulator in Pseudomonas aeruginosa: fur mutants produce elevated alginate levels
    • Hassett D.J., Howell M.L., Ochsner U.A., Vasil M.L., Johnson Z., Dean G.E. An operon containing fumC and sodA encoding fumarase C and manganese superoxide dismutase is controlled by the ferric uptake regulator in Pseudomonas aeruginosa: fur mutants produce elevated alginate levels. J. Bacteriol. 1997, 179:1452-1459.
    • (1997) J. Bacteriol. , vol.179 , pp. 1452-1459
    • Hassett, D.J.1    Howell, M.L.2    Ochsner, U.A.3    Vasil, M.L.4    Johnson, Z.5    Dean, G.E.6
  • 31
    • 0029898120 scopus 로고    scopus 로고
    • Ferric uptake regulator (Fur) mutants of Pseudomonas aeruginosa demonstrate defective siderophore-mediated iron uptake, altered aerobic growth, and decreased superoxide dismutase and catalase activities
    • Hassett D.J., Sokol P.A., Howell M.L., Ma J.F., Schweizer H.T., Ochsner U., Vasil M.L. Ferric uptake regulator (Fur) mutants of Pseudomonas aeruginosa demonstrate defective siderophore-mediated iron uptake, altered aerobic growth, and decreased superoxide dismutase and catalase activities. J. Bacteriol. 1996, 178:3996-4003.
    • (1996) J. Bacteriol. , vol.178 , pp. 3996-4003
    • Hassett, D.J.1    Sokol, P.A.2    Howell, M.L.3    Ma, J.F.4    Schweizer, H.T.5    Ochsner, U.6    Vasil, M.L.7
  • 32
    • 0025731112 scopus 로고
    • Siderophore production by Aeromonas salmonicida
    • Hirst I.D., Hastings T.S., Ellis A.E. Siderophore production by Aeromonas salmonicida. J. Gen. Microbiol. 1991, 137:1185-1192.
    • (1991) J. Gen. Microbiol. , vol.137 , pp. 1185-1192
    • Hirst, I.D.1    Hastings, T.S.2    Ellis, A.E.3
  • 33
    • 0028670767 scopus 로고
    • LexA repressor and iron uptake regulator from Escherichia coli: new members of the CAP-like DNA binding domain superfamily
    • Holm L., Sander C., Ruterjans H., Schnarr M., Fogh R., Boelens R., Kaptein R. LexA repressor and iron uptake regulator from Escherichia coli: new members of the CAP-like DNA binding domain superfamily. Protein Eng. 1994, 7:1449-1453.
    • (1994) Protein Eng. , vol.7 , pp. 1449-1453
    • Holm, L.1    Sander, C.2    Ruterjans, H.3    Schnarr, M.4    Fogh, R.5    Boelens, R.6    Kaptein, R.7
  • 34
    • 0035150765 scopus 로고    scopus 로고
    • In Staphylococcus aureus, fur is an interactive regulator with PerR, contributes to virulence, and is necessary for oxidative stress resistance through positive regulation of catalase and iron homeostasis
    • Horsburgh M.J., Ingham E., Foster S.J. In Staphylococcus aureus, fur is an interactive regulator with PerR, contributes to virulence, and is necessary for oxidative stress resistance through positive regulation of catalase and iron homeostasis. J. Bacteriol. 2001, 183:468-475.
    • (2001) J. Bacteriol. , vol.183 , pp. 468-475
    • Horsburgh, M.J.1    Ingham, E.2    Foster, S.J.3
  • 36
    • 29744459466 scopus 로고    scopus 로고
    • Petrobactin is the primary siderophore synthesized by Bacillus anthracis Str. Sterne under conditions of iron starvation
    • Koppisch A.T., Browder C.C., Moe A.L., Shelley J.T., Kinkel B.A., Hersman L.E., Lyer S., Ruggiero C.E. Petrobactin is the primary siderophore synthesized by Bacillus anthracis Str. Sterne under conditions of iron starvation. Biometals 2005, 18:577-585.
    • (2005) Biometals , vol.18 , pp. 577-585
    • Koppisch, A.T.1    Browder, C.C.2    Moe, A.L.3    Shelley, J.T.4    Kinkel, B.A.5    Hersman, L.E.6    Lyer, S.7    Ruggiero, C.E.8
  • 37
    • 0028181626 scopus 로고
    • Analysis of the complexity of gene regulation by fur in Vibrio cholerae
    • Litwin C.M., Calderwood S.B. Analysis of the complexity of gene regulation by fur in Vibrio cholerae. J. Bacteriol. 1994, 176:240-248.
    • (1994) J. Bacteriol. , vol.176 , pp. 240-248
    • Litwin, C.M.1    Calderwood, S.B.2
  • 38
    • 0032733344 scopus 로고    scopus 로고
    • Characterization of a ferric uptake regulator (fur) gene from Xanthomonas campestris pv. phaseoli with unusual primary structure, genome organization, and expression patterns
    • Loprasert S., Sallabhan R., Atichartpongkul S., Mongkolsuk S. Characterization of a ferric uptake regulator (fur) gene from Xanthomonas campestris pv. phaseoli with unusual primary structure, genome organization, and expression patterns. Gene 1999, 239:251-258.
    • (1999) Gene , vol.239 , pp. 251-258
    • Loprasert, S.1    Sallabhan, R.2    Atichartpongkul, S.3    Mongkolsuk, S.4
  • 40
    • 0028338411 scopus 로고
    • Diversity of siderophore genes encoding biosynthesis of 2,3-dihydroxybenzoic acid in Aeromonas spp
    • Massad G., Arceneaux J.E., Byers B.R. Diversity of siderophore genes encoding biosynthesis of 2,3-dihydroxybenzoic acid in Aeromonas spp. Biometals 1994, 7:227-236.
    • (1994) Biometals , vol.7 , pp. 227-236
    • Massad, G.1    Arceneaux, J.E.2    Byers, B.R.3
  • 41
    • 28444438519 scopus 로고    scopus 로고
    • Iron and fur regulation in Vibrio cholerae and the role of fur in virulence
    • Mey A.R., Wyckoff E.E., Kanukurthy V., Fisher C.R., Payne S.M. Iron and fur regulation in Vibrio cholerae and the role of fur in virulence. Infect. Immun. 2005, 73:8167-8178.
    • (2005) Infect. Immun. , vol.73 , pp. 8167-8178
    • Mey, A.R.1    Wyckoff, E.E.2    Kanukurthy, V.3    Fisher, C.R.4    Payne, S.M.5
  • 42
    • 0041893905 scopus 로고    scopus 로고
    • Biogenesis of iron-sulfur proteins in eukaryotes: a novel task of mitochondria that is inherited from bacteria
    • Muhlenhoff U., Lill R. Biogenesis of iron-sulfur proteins in eukaryotes: a novel task of mitochondria that is inherited from bacteria. Biochim. Biophys. Acta 2000, 1459:370-382.
    • (2000) Biochim. Biophys. Acta , vol.1459 , pp. 370-382
    • Muhlenhoff, U.1    Lill, R.2
  • 43
    • 0025278585 scopus 로고
    • Control of Escherichia coli superoxide dismutase (sodA and sodB) genes by the ferric uptake regulation (fur) locus
    • Niederhoffer E.C., Naranjo C.M., Bradley K.L., Fee J.A. Control of Escherichia coli superoxide dismutase (sodA and sodB) genes by the ferric uptake regulation (fur) locus. J. Bacteriol. 1990, 172:1930-1938.
    • (1990) J. Bacteriol. , vol.172 , pp. 1930-1938
    • Niederhoffer, E.C.1    Naranjo, C.M.2    Bradley, K.L.3    Fee, J.A.4
  • 44
    • 3042855363 scopus 로고    scopus 로고
    • Iron acquisition and regulation in Campylobacter jejuni
    • Palyada K., Threadgill D., Stintzi A. Iron acquisition and regulation in Campylobacter jejuni. J. Bacteriol. 2004, 186:4714-4729.
    • (2004) J. Bacteriol. , vol.186 , pp. 4714-4729
    • Palyada, K.1    Threadgill, D.2    Stintzi, A.3
  • 45
    • 33746455962 scopus 로고    scopus 로고
    • Structural changes of Escherichia coli ferric uptake regulator during metal-dependent dimerization and activation explored by NMR and X-ray crystallography
    • Pecqueur L., D'Autreaux B., Dupuy J., Nicolet Y., Jacquamet L., Brutscher B., Michaud-Soret I., Bersch B. Structural changes of Escherichia coli ferric uptake regulator during metal-dependent dimerization and activation explored by NMR and X-ray crystallography. J. Biol. Chem. 2006, 281:21286-21295.
    • (2006) J. Biol. Chem. , vol.281 , pp. 21286-21295
    • Pecqueur, L.1    D'Autreaux, B.2    Dupuy, J.3    Nicolet, Y.4    Jacquamet, L.5    Brutscher, B.6    Michaud-Soret, I.7    Bersch, B.8
  • 46
    • 0027251630 scopus 로고
    • Coordinate regulation of siderophore and exotoxin A production: molecular cloning and sequencing of the Pseudomonas aeruginosa fur gene
    • Prince R.W., Cox C.D., Vasil M.L. Coordinate regulation of siderophore and exotoxin A production: molecular cloning and sequencing of the Pseudomonas aeruginosa fur gene. J. Bacteriol. 1993, 175:2589-2598.
    • (1993) J. Bacteriol. , vol.175 , pp. 2589-2598
    • Prince, R.W.1    Cox, C.D.2    Vasil, M.L.3
  • 47
    • 0033759220 scopus 로고    scopus 로고
    • Iron metabolism in pathogenic bacteria
    • Ratledge C., Dover L.G. Iron metabolism in pathogenic bacteria. Annu. Rev. Microbiol. 2000, 54:881-941.
    • (2000) Annu. Rev. Microbiol. , vol.54 , pp. 881-941
    • Ratledge, C.1    Dover, L.G.2
  • 48
    • 0842327149 scopus 로고    scopus 로고
    • Disruption of putative regulatory loci in Listeria monocytogenes demonstrates a significant role for Fur and PerR in virulence
    • Rea R.B., Gahan C.G., Hill C. Disruption of putative regulatory loci in Listeria monocytogenes demonstrates a significant role for Fur and PerR in virulence. Infect. Immun. 2004, 72:717-727.
    • (2004) Infect. Immun. , vol.72 , pp. 717-727
    • Rea, R.B.1    Gahan, C.G.2    Hill, C.3
  • 51
    • 0023127806 scopus 로고
    • Universal chemical assay for the detection and determination of siderophores
    • Schwyn B., Neilands J.B. Universal chemical assay for the detection and determination of siderophores. Anal. Biochem. 1987, 160:47-56.
    • (1987) Anal. Biochem. , vol.160 , pp. 47-56
    • Schwyn, B.1    Neilands, J.B.2
  • 52
    • 38149147950 scopus 로고
    • Methodology for implanting cortisol in Atlantic salmon and effects of chronically elevated cortisol on osmoregulatory physiology
    • Specker J.L., Portesi D.M., Cornell S.C., Veillette P.A. Methodology for implanting cortisol in Atlantic salmon and effects of chronically elevated cortisol on osmoregulatory physiology. Aquaculture 1994, 121:181-193.
    • (1994) Aquaculture , vol.121 , pp. 181-193
    • Specker, J.L.1    Portesi, D.M.2    Cornell, S.C.3    Veillette, P.A.4
  • 53
    • 0027971405 scopus 로고
    • Pleiotropic effects of a Yersinia pestis fur mutation
    • Staggs T.M., Fetherston J.D., Perry R.D. Pleiotropic effects of a Yersinia pestis fur mutation. J. Bacteriol. 1994, 176:7614-7624.
    • (1994) J. Bacteriol. , vol.176 , pp. 7614-7624
    • Staggs, T.M.1    Fetherston, J.D.2    Perry, R.D.3
  • 54
    • 0028308565 scopus 로고
    • Identification and cloning of a fur homologue from Neisseria meningitidis
    • Thomas C.E., Sparling P.F. Identification and cloning of a fur homologue from Neisseria meningitidis. Mol. Microbiol. 1994, 11:725-737.
    • (1994) Mol. Microbiol. , vol.11 , pp. 725-737
    • Thomas, C.E.1    Sparling, P.F.2
  • 55
    • 0036156696 scopus 로고    scopus 로고
    • Transcriptional and proteomic analysis of a ferric uptake regulator (fur) mutant of Shewanella oneidensis: possible involvement of fur in energy metabolism, transcriptional regulation, and oxidative stress
    • Thompson D.K., Beliaev A.S., Giometti C.S., Tollaksen S.L., Khare T., Lies D.P., Nealson K.H., Lim H., Yates J., Brandt C.C., Tiedje J.M., Zhou J. Transcriptional and proteomic analysis of a ferric uptake regulator (fur) mutant of Shewanella oneidensis: possible involvement of fur in energy metabolism, transcriptional regulation, and oxidative stress. Appl. Environ. Microbiol. 2002, 68:881-892.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 881-892
    • Thompson, D.K.1    Beliaev, A.S.2    Giometti, C.S.3    Tollaksen, S.L.4    Khare, T.5    Lies, D.P.6    Nealson, K.H.7    Lim, H.8    Yates, J.9    Brandt, C.C.10    Tiedje, J.M.11    Zhou, J.12
  • 56
    • 0027955329 scopus 로고
    • Characterization of the Vibrio anguillarum fur gene: role in regulation of expression of the FatA outer membrane protein and catechols
    • Tolmasky M.E., Wertheimer A.M., Actis L.A., Crosa J.H. Characterization of the Vibrio anguillarum fur gene: role in regulation of expression of the FatA outer membrane protein and catechols. J. Bacteriol. 1994, 176:213-220.
    • (1994) J. Bacteriol. , vol.176 , pp. 213-220
    • Tolmasky, M.E.1    Wertheimer, A.M.2    Actis, L.A.3    Crosa, J.H.4
  • 57
    • 0029041226 scopus 로고
    • Lethal oxidative damage and mutagenesis are generated by iron in delta fur mutants of Escherichia coli: protective role of superoxide dismutase
    • Touati D., Jacques M., Tardat B., Bouchard L., Despied S. Lethal oxidative damage and mutagenesis are generated by iron in delta fur mutants of Escherichia coli: protective role of superoxide dismutase. J. Bacteriol. 1995, 177:2305-2314.
    • (1995) J. Bacteriol. , vol.177 , pp. 2305-2314
    • Touati, D.1    Jacques, M.2    Tardat, B.3    Bouchard, L.4    Despied, S.5
  • 59
    • 0036373361 scopus 로고    scopus 로고
    • Effect of fur mutation on acid-tolerance response and in vivo virulence of avian septicemic Escherichia coli
    • Zhu C., Ngeleka M., Potter A.A., Allan B.J. Effect of fur mutation on acid-tolerance response and in vivo virulence of avian septicemic Escherichia coli. Can. J. Microbiol. 2002, 48:458-462.
    • (2002) Can. J. Microbiol. , vol.48 , pp. 458-462
    • Zhu, C.1    Ngeleka, M.2    Potter, A.A.3    Allan, B.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.