메뉴 건너뛰기




Volumn 46, Issue 4, 2002, Pages 1107-1122

Autoregulation of Helicobacter pylori Fur revealed by functional analysis of the iron-binding site

Author keywords

[No Author keywords available]

Indexed keywords

IRON BINDING PROTEIN;

EID: 0036436311     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.2002.03227.x     Document Type: Article
Times cited : (65)

References (56)
  • 1
    • 0031045576 scopus 로고    scopus 로고
    • The fur gene from Klebsiella pneumoniae: Characterization, genomic organization and phylogenetic analysis
    • Achenbach, L.A., and Yang, W. (1997) The fur gene from Klebsiella pneumoniae: Characterization, genomic organization and phylogenetic analysis. Gene 185: 201-207.
    • (1997) Gene , vol.185 , pp. 201-207
    • Achenbach, L.A.1    Yang, W.2
  • 2
    • 0033545903 scopus 로고    scopus 로고
    • Spectroscopic and saturation magnetization properties of the manganese- and cobalt-substituted Fur (ferric uptake regulation) protein from Escherichia coli
    • Adrait, A., Jacquamet, L., Le Pape, L., Gonzalez de Peredo, A., Aberdam, D., Hazemann, J.L., et al. (1999) Spectroscopic and saturation magnetization properties of the manganese- and cobalt-substituted Fur (ferric uptake regulation) protein from Escherichia coli. Biochemistry 38: 6248-6260.
    • (1999) Biochemistry , vol.38 , pp. 6248-6260
    • Adrait, A.1    Jacquamet, L.2    Le Pape, L.3    Gonzalez de Peredo, A.4    Aberdam, D.5    Hazemann, J.L.6
  • 3
    • 0033580683 scopus 로고    scopus 로고
    • The ferric uptake regulation (Fur) repressor is a zinc metalloprotein
    • Althaus, E.W., Outten, C.E., Olson, K.E., Cao, H., and O'Halloran, T.V. (1999) The ferric uptake regulation (Fur) repressor is a zinc metalloprotein. Biochemistry 38: 6559-6569.
    • (1999) Biochemistry , vol.38 , pp. 6559-6569
    • Althaus, E.W.1    Outten, C.E.2    Olson, K.E.3    Cao, H.4    O'Halloran, T.V.5
  • 4
    • 0023664923 scopus 로고
    • Ferric uptake regulation protein acts as a repressor, employing iron (II) as a cofactor to bind the operon in Eschericia coli
    • Bagg, A., and Neilands, J.B. (1987) Ferric uptake regulation protein acts as a repressor, employing iron (II) as a cofactor to bind the operon in Eschericia coli. Biochemistry 26: 5471-5477.
    • (1987) Biochemistry , vol.26 , pp. 5471-5477
    • Bagg, A.1    Neilands, J.B.2
  • 5
    • 0029798283 scopus 로고    scopus 로고
    • Ferric uptake regulator mutants of Pseudomonas aeruginosa with distinct alterations in the iron-dependent repression of exotoxin A and siderophores in aerobic and microaerobic environments
    • Barton, H.A., Johnson, Z., Cox, C.D., Vasil, A.I., and Vasil, M.L. (1996) Ferric uptake regulator mutants of Pseudomonas aeruginosa with distinct alterations in the iron-dependent repression of exotoxin A and siderophores in aerobic and microaerobic environments. Mol Microbiol 21: 1001-1017.
    • (1996) Mol Microbiol , vol.21 , pp. 1001-1017
    • Barton, H.A.1    Johnson, Z.2    Cox, C.D.3    Vasil, A.I.4    Vasil, M.L.5
  • 6
    • 0027874441 scopus 로고
    • Isolation of lambda repressor mutants with defects in cooperative operator binding
    • Beckett, D., Burz, D.S., Ackers, G.K., and Sauer, R.T. (1993) Isolation of lambda repressor mutants with defects in cooperative operator binding. Biochemistry 32: 9073-9079.
    • (1993) Biochemistry , vol.32 , pp. 9073-9079
    • Beckett, D.1    Burz, D.S.2    Ackers, G.K.3    Sauer, R.T.4
  • 7
    • 0031696507 scopus 로고    scopus 로고
    • Functional analysis of the Helicobacter pylori principal sigma subunit of RNA polymerase reveals that the spacer region is important for efficient transcription
    • Beier, D., Spohn, G., Rappuoli, R., and Scarlato, V. (1998) Functional analysis of the Helicobacter pylori principal sigma subunit of RNA polymerase reveals that the spacer region is important for efficient transcription. Mol Microbiol 30: 121-134.
    • (1998) Mol Microbiol , vol.30 , pp. 121-134
    • Beier, D.1    Spohn, G.2    Rappuoli, R.3    Scarlato, V.4
  • 8
    • 0032519447 scopus 로고    scopus 로고
    • Cloning and characterization of the fur gene from Helicobacter pylori
    • Bereswill, S., Lichte, F., Vey, T., Fassbinder, F., and Kist, M. (1998) Cloning and characterization of the fur gene from Helicobacter pylori. FEMS Microbiol Lett 159: 193-200.
    • (1998) FEMS Microbiol Lett , vol.159 , pp. 193-200
    • Bereswill, S.1    Lichte, F.2    Vey, T.3    Fassbinder, F.4    Kist, M.5
  • 9
    • 0033759351 scopus 로고    scopus 로고
    • Regulation of ferritin-mediated cytoplasmic iron storage by the ferric uptake regulator homolog (Fur) of Helicobacter pylori
    • Bereswill, S., Greiner, S., van Vliet, A.H., Waidner, B., Fassbinder, F., Schiltz, E., et al. (2000) Regulation of ferritin-mediated cytoplasmic iron storage by the ferric uptake regulator homolog (Fur) of Helicobacter pylori. J Bacteriol 182: 5948-5953.
    • (2000) J Bacteriol , vol.182 , pp. 5948-5953
    • Bereswill, S.1    Greiner, S.2    Van Vliet, A.H.3    Waidner, B.4    Fassbinder, F.5    Schiltz, E.6
  • 10
    • 0036156091 scopus 로고    scopus 로고
    • The Helicobacter pylori homologue of the ferric uptake regulator is involved in acid resistance
    • Bijlsma, J.J., Waidner, B., Vliet, A.H., Hughes, N.J., Hag, S., Bereswill, S., et al. (2002) The Helicobacter pylori homologue of the ferric uptake regulator is involved in acid resistance. Infect Immun 70: 606-611.
    • (2002) Infect Immun , vol.70 , pp. 606-611
    • Bijlsma, J.J.1    Waidner, B.2    Vliet, A.H.3    Hughes, N.J.4    Hag, S.5    Bereswill, S.6
  • 11
    • 0032811011 scopus 로고    scopus 로고
    • Interaction of Bacillus subtilis Fur (ferric uptake repressor) with the dhb operator in vitro and in vivo
    • Bsat, N., and Helmann, J.D. (1999) Interaction of Bacillus subtilis Fur (ferric uptake repressor) with the dhb operator in vitro and in vivo. J Bacteriol 181: 4299-4307.
    • (1999) J Bacteriol , vol.181 , pp. 4299-4307
    • Bsat, N.1    Helmann, J.D.2
  • 12
    • 0029155913 scopus 로고
    • The interaction of the ferric uptake regulation protein with DNA
    • Coy, M. (1995) The interaction of the ferric uptake regulation protein with DNA. Biochem Biophys Res Commun 212: 784-792.
    • (1995) Biochem Biophys Res Commun , vol.212 , pp. 784-792
    • Coy, M.1
  • 13
    • 0025942194 scopus 로고
    • Structural dynamics and functional domains of the fur protein
    • Coy, M., and Neilands, J.B. (1991) Structural dynamics and functional domains of the fur protein. Biochemistry 30: 8201-8210.
    • (1991) Biochemistry , vol.30 , pp. 8201-8210
    • Coy, M.1    Neilands, J.B.2
  • 14
    • 0028151003 scopus 로고
    • Site-directed mutagenesis of the ferric uptake regulation gene of Escherichia coli
    • Coy, M., Doyle, C., Besser, J., and Neilands, J.B. (1994) Site-directed mutagenesis of the ferric uptake regulation gene of Escherichia coli. Biometals 7: 292-298.
    • (1994) Biometals , vol.7 , pp. 292-298
    • Coy, M.1    Doyle, C.2    Besser, J.3    Neilands, J.B.4
  • 15
    • 0035724513 scopus 로고    scopus 로고
    • The Fur repressor controls transcription of iron-activated and iron-repressed genes in Helicobacter pylori
    • Delany, I., Spohn, G., Rappuoli, R., and Scarlato, V. (2001a) The Fur repressor controls transcription of iron-activated and iron-repressed genes in Helicobacter pylori. Mol Microbiol 42: 1297-1309.
    • (2001) Mol Microbiol , vol.42 , pp. 1297-1309
    • Delany, I.1    Spohn, G.2    Rappuoli, R.3    Scarlato, V.4
  • 16
    • 0034902772 scopus 로고    scopus 로고
    • Iron-dependent transcription of the frpB gene of Helicobacter pylori is controlled by the Fur repressor protein
    • Delany, I., Pacheco, A.B.F., Spohn, G., Rappuol, R., and Scarlato, V. (2001b) Iron-dependent transcription of the frpB gene of Helicobacter pylori is controlled by the Fur repressor protein. J Bacteriol 183: 4932-4937.
    • (2001) J Bacteriol , vol.183 , pp. 4932-4937
    • Delany, I.1    Pacheco, A.B.F.2    Spohn, G.3    Rappuol, R.4    Scarlato, V.5
  • 17
    • 0036718563 scopus 로고    scopus 로고
    • Growth phase-dependent regulation of target gene promoters for binding of the essential orphan response regulator HP1043 of Helicobacter pylori
    • Delany, I., Spohn, G., Rappuoli, R., and Scarlato, V. (2002) Growth phase-dependent regulation of target gene promoters for binding of the essential orphan response regulator HP1043 of Helicobacter pylori. J Bacteriol 184: 4800-4810.
    • (2002) J Bacteriol , vol.184 , pp. 4800-4810
    • Delany, I.1    Spohn, G.2    Rappuoli, R.3    Scarlato, V.4
  • 18
    • 0034046748 scopus 로고    scopus 로고
    • Fur positive regulation of iron superoxide dismutase in Escherichia coli: Functional analysis of the sodB promoter
    • Dubrac, S., and Touati, D. (2000) Fur positive regulation of iron superoxide dismutase in Escherichia coli: Functional analysis of the sodB promoter. J Bacteriol 182: 3802-3808.
    • (2000) J Bacteriol , vol.182 , pp. 3802-3808
    • Dubrac, S.1    Touati, D.2
  • 19
    • 0030663311 scopus 로고    scopus 로고
    • Metalloregulation in vitro of the aerobactin promoter of Escherichia coli by the Fur (ferric uptake regulation) protein
    • Escolar, L., de Lorenzo, V., and Perez-Martin, J. (1997) Metalloregulation in vitro of the aerobactin promoter of Escherichia coli by the Fur (ferric uptake regulation) protein. Mol Microbiol 26: 799-808.
    • (1997) Mol Microbiol , vol.26 , pp. 799-808
    • Escolar, L.1    De Lorenzo, V.2    Perez-Martin, J.3
  • 20
    • 0032582478 scopus 로고    scopus 로고
    • Binding of the fur (ferric uptake regulator) repressor of Escherichia coli to arrays of the GATAAT sequence
    • Escolar, L., Perez-Martin, J., and de Lorenzo, V. (1998) Binding of the fur (ferric uptake regulator) repressor of Escherichia coli to arrays of the GATAAT sequence. J Mol Biol 283: 537-547.
    • (1998) J Mol Biol , vol.283 , pp. 537-547
    • Escolar, L.1    Perez-Martin, J.2    De Lorenzo, V.3
  • 21
    • 0344172832 scopus 로고    scopus 로고
    • Opening the iron box: Transcriptional metalloregulation by the Fur protein
    • Escolar, L., Perez-Martin, J., and de Lorenzo, V. (1999) Opening the iron box: Transcriptional metalloregulation by the Fur protein. J Bacteriol 181: 6223-6229.
    • (1999) J Bacteriol , vol.181 , pp. 6223-6229
    • Escolar, L.1    Perez-Martin, J.2    De Lorenzo, V.3
  • 22
    • 0034637480 scopus 로고    scopus 로고
    • Evidence of an unusually long operator for the fur repressor in the aerobactin promoter of Escherichia coli
    • Escolar, L., Perez-Martin, J., and de Lorenzo, V. (2000) Evidence of an unusually long operator for the fur repressor in the aerobactin promoter of Escherichia coli. J Biol Chem 275: 24709-24714.
    • (2000) J Biol Chem , vol.275 , pp. 24709-24714
    • Escolar, L.1    Perez-Martin, J.2    De Lorenzo, V.3
  • 23
    • 0034653295 scopus 로고    scopus 로고
    • Identification of iron-regulated genes of Helicobacter pylori by a modified fur titration assay (FURTA-Hp)
    • Fassbinder, F., van Vliet, A.H., Gimmel, V., Kusters, J.G., Kist, M., and Bereswill. S. (2000) Identification of iron-regulated genes of Helicobacter pylori by a modified fur titration assay (FURTA-Hp). FEMS Microbiol Lett 184: 225-229.
    • (2000) FEMS Microbiol Lett , vol.184 , pp. 225-229
    • Fassbinder, F.1    Van Vliet, A.H.2    Gimmel, V.3    Kusters, J.G.4    Kist, M.5    Bereswill, S.6
  • 24
    • 0028227788 scopus 로고
    • Fur (ferric uptake regulation) protein interaction with target DNA: Comparison of gel retardation, footprinting and electron microscopy analyses
    • Frechon, D., and Le Cam, E. (1994) Fur (ferric uptake regulation) protein interaction with target DNA: Comparison of gel retardation, footprinting and electron microscopy analyses. Biochem Biophys Res Commun 201: 346-355.
    • (1994) Biochem Biophys Res Commun , vol.201 , pp. 346-355
    • Frechon, D.1    Le Cam, E.2
  • 25
    • 0034532857 scopus 로고    scopus 로고
    • Characterisation of Vibrio parahaemolyticus manganese-resistant mutants in reference to the function of the ferric uptake regulatory protein
    • Funahashi, T., Fukiwara, C., Okada, M., Miyoshi, S., Shinoda, S., Narimatsu, S., and Yamamoto, S. (2000) Characterisation of Vibrio parahaemolyticus manganese-resistant mutants in reference to the function of the ferric uptake regulatory protein. Microbiol Immunol 44: 963-970.
    • (2000) Microbiol Immunol , vol.44 , pp. 963-970
    • Funahashi, T.1    Fukiwara, C.2    Okada, M.3    Miyoshi, S.4    Shinoda, S.5    Narimatsu, S.6    Yamamoto, S.7
  • 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., and Forest, E. (1999) Identification of the two zinc-bound cysteines in the ferric uptake regulation protein from Escherichia coli: Chemical modification and mass spectrometry analysis. Biochemistry 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
    • 0035967907 scopus 로고    scopus 로고
    • Conformational changes of the ferric uptake regulation protein upon metal activation and DNA binding; first evidence of structural homologies with the diphtheria toxin repressor
    • Gonzalez de Peredo, A., Saint-Pierre, C., Latour, J.M., Michaud-Soret, I., and Forest, E. (2001) Conformational changes of the ferric uptake regulation protein upon metal activation and DNA binding; first evidence of structural homologies with the diphtheria toxin repressor. J Mol Biol 310: 83-91.
    • (2001) J Mol Biol , vol.310 , pp. 83-91
    • Gonzalez de Peredo, A.1    Saint-Pierre, C.2    Latour, J.M.3    Michaud-Soret, I.4    Forest, E.5
  • 28
    • 0029818614 scopus 로고    scopus 로고
    • The role of fur. The acid tolerance response of Salmonella typhimurium is physiologically and genetically separable from its role in iron acquisition
    • Hall, H.K., and Foster, J.W. (1996) The role of fur. the acid tolerance response of Salmonella typhimurium is physiologically and genetically separable from its role in iron acquisition. J Bacteriol 178: 5683-5691.
    • (1996) J Bacteriol , vol.178 , pp. 5683-5691
    • Hall, H.K.1    Foster, J.W.2
  • 29
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan, D. (1983) Studies on transformation of Escherichia coli with plasmids. J Mol Biol 166: 557-580.
    • (1983) J Mol Biol , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 30
    • 0032562131 scopus 로고    scopus 로고
    • X-ray absorption spectroscopy of a new zinc site in the Fur protein from Escherichia coli
    • Jacquamet, L., Aberdam, D., Adrait, A., Hazemann, J.L., Latour, J.M., and Michaud-Soret, I. (1998) X-ray absorption spectroscopy of a new zinc site in the Fur protein from Escherichia coli. Biochemistry 37: 2564-2571.
    • (1998) Biochemistry , vol.37 , pp. 2564-2571
    • Jacquamet, L.1    Aberdam, D.2    Adrait, A.3    Hazemann, J.L.4    Latour, J.M.5    Michaud-Soret, I.6
  • 31
    • 0023917709 scopus 로고
    • Gene disruption and replacement as a feasible approach for mutagenesis of Campylobacter jejuni
    • Labigne-Roussel, A., Courcoux, P., and Tompkins, L. (1988) Gene disruption and replacement as a feasible approach for mutagenesis of Campylobacter jejuni. J Bacteriol 170: 1704-1708.
    • (1988) J Bacteriol , vol.170 , pp. 1704-1708
    • Labigne-Roussel, A.1    Courcoux, P.2    Tompkins, L.3
  • 32
    • 0028068734 scopus 로고
    • Vibrio cholerae fur mutations associated with loss of repressor activity: Implications for the structural-functional relationships of fur
    • Lam, M.S., Litwin, C.M., Carroll, P.A., and Calderwood, S.B. (1994) Vibrio cholerae fur mutations associated with loss of repressor activity: Implications for the structural-functional relationships of fur. J Bacteriol 176: 5108-5115.
    • (1994) J Bacteriol , vol.176 , pp. 5108-5115
    • Lam, M.S.1    Litwin, C.M.2    Carroll, P.A.3    Calderwood, S.B.4
  • 33
    • 0028113847 scopus 로고
    • Observation of binding and polymerization of Fur repressor onto operator-containing DNA with electron and atomic force microscopes
    • Le Cam, E., Frechon, D., Barray, M., Fourcade, A., and Delain, E. (1994) Observation of binding and polymerization of Fur repressor onto operator-containing DNA with electron and atomic force microscopes. Proc Natl Acad Sci USA 91: 11816-11820.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 11816-11820
    • Le Cam, E.1    Frechon, D.2    Barray, M.3    Fourcade, A.4    Delain, E.5
  • 34
    • 0023258960 scopus 로고
    • Operator sequences of the aerobactin operon of plasmid ColV-K30 binding the ferric uptake regulation (fur) repressor
    • de Lorenzo, V., Wee, S., Herrero, M., and Neilands, J.B. (1987) Operator sequences of the aerobactin operon of plasmid ColV-K30 binding the ferric uptake regulation (fur) repressor. J Bacteriol 169: 2624-2630.
    • (1987) J Bacteriol , vol.169 , pp. 2624-2630
    • De Lorenzo, V.1    Wee, S.2    Herrero, M.3    Neilands, J.B.4
  • 35
    • 0023692463 scopus 로고
    • Metal ion regulation of gene expression. Fur repressor-operator interaction at the promoter region of the aerobactin system of pColV-K30
    • de Lorenzo, V., Giovannini, F., Herrero, M., and Neilands, J.B. (1988a) Metal ion regulation of gene expression. Fur repressor-operator interaction at the promoter region of the aerobactin system of pColV-K30. J Mol Biol 203: 875-884.
    • (1988) J Mol Biol , vol.203 , pp. 875-884
    • De Lorenzo, V.1    Giovannini, F.2    Herrero, M.3    Neilands, J.B.4
  • 36
    • 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., and Neilands, J.B. (1988b) Fur (ferric uptake regulation) protein and CAP (catabolite-activator protein) modulate transcription of fur gene in Escherichia coli. Eur J Biochem 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
  • 37
    • 0034996994 scopus 로고    scopus 로고
    • The Burkholderia cepacia fur gene: Co-localization with omlA and absence of regulation by iron
    • Lowe, C.A., Asghar, A.H., Shalom, G., Shaw, J.G., and Thomas, M.S. (2001) The Burkholderia cepacia fur gene: Co-localization with omlA and absence of regulation by iron. Microbiology 147: 1303-1314.
    • (2001) Microbiology , vol.147 , pp. 1303-1314
    • Lowe, C.A.1    Asghar, A.H.2    Shalom, G.3    Shaw, J.G.4    Thomas, M.S.5
  • 38
  • 39
    • 0030805985 scopus 로고    scopus 로고
    • Electrospray ionization mass spectrometry analysis of the apo- and metal-substituted forms of the Fur protein
    • Michaud-Soret, I., Adrait, A., Jaquinod, M., Forest, E., Touati, D., and Latour, J.M. (1997) Electrospray ionization mass spectrometry analysis of the apo- and metal-substituted forms of the Fur protein. FEBS Lett 413: 473-476.
    • (1997) FEBS Lett , vol.413 , pp. 473-476
    • Michaud-Soret, I.1    Adrait, A.2    Jaquinod, M.3    Forest, E.4    Touati, D.5    Latour, J.M.6
  • 40
    • 0025278585 scopus 로고
    • Control of Escherichia coli superoxide dismutase (sodA andsodB) genes by the ferric uptake regulation (fur) locus
    • Niederhoffer, E.C., Naranjo, C.M., Bradley, K.L., and Fee, J.A. (1990) Control of Escherichia coli superoxide dismutase (sodA andsodB) genes by the ferric uptake regulation (fur) locus. J Bacteriol 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
  • 41
    • 0029966305 scopus 로고    scopus 로고
    • Gene repression by the ferric uptake regulator in Pseudomonas aeruginosa: Cycle selection of iron-regulated genes
    • Ochsner, U.A., and Vasil, M.L. (1996) Gene repression by the ferric uptake regulator in Pseudomonas aeruginosa: Cycle selection of iron-regulated genes. Proc Natl Acad Sci USA 93: 4409-4414.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 4409-4414
    • Ochsner, U.A.1    Vasil, M.L.2
  • 42
    • 0027251630 scopus 로고
    • Coordinate regulation of siderophore and exotoxin A production: Molecular cloning and sequencing of the Pseudomonas aeruginosa furgene
    • Prince, R.W., Cox, C.D., and Vasil, M.L. (1993) Coordinate regulation of siderophore and exotoxin A production: Molecular cloning and sequencing of the Pseudomonas aeruginosa furgene. J Bacteriol 175: 2589-2598.
    • (1993) J Bacteriol , vol.175 , pp. 2589-2598
    • Prince, R.W.1    Cox, C.D.2    Vasil, M.L.3
  • 44
    • 0030728522 scopus 로고    scopus 로고
    • Transcriptional analysis of the divergent cagAB genes encoded by the pathogenicity island of Helicobacter pylori
    • Spohn, G., Beier, D., Rappuoli, R., and Scarlato, V. (1997) Transcriptional analysis of the divergent cagAB genes encoded by the pathogenicity island of Helicobacter pylori. Mol Microbiol 26: 361-372.
    • (1997) Mol Microbiol , vol.26 , pp. 361-372
    • Spohn, G.1    Beier, D.2    Rappuoli, R.3    Scarlato, V.4
  • 45
    • 0030976054 scopus 로고    scopus 로고
    • The oligomeric structure of nucleoid protein H-NS is necessary for recognition of intrinsically curved DNA for DNA bending
    • Spurio, R., Falconi, M., Brandi, A., Pon, C.L., and Gualerzi, C.O. (1997) The oligomeric structure of nucleoid protein H-NS is necessary for recognition of intrinsically curved DNA for DNA bending. EMBO J 16: 1795-1805.
    • (1997) EMBO J , vol.16 , pp. 1795-1805
    • Spurio, R.1    Falconi, M.2    Brandi, A.3    Pon, C.L.4    Gualerzi, C.O.5
  • 46
    • 0028960213 scopus 로고
    • Functional domains of the Escherichia coli ferric uptake regulator protein (Fur)
    • Stojiljkovic, I., and Hantke, K. (1995) Functional domains of the Escherichia coli ferric uptake regulator protein (Fur). Mol Gen Genet 247: 199-205.
    • (1995) Mol Gen Genet , vol.247 , pp. 199-205
    • Stojiljkovic, I.1    Hantke, K.2
  • 47
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier, F.W., and Moffatt, B.A. (1986) Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J Mol Biol 189: 113-130.
    • (1986) J Mol Biol , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 49
    • 0029164719 scopus 로고
    • Fur regulon of Salmonella typhimurium: Identification of new iron-regulated genes
    • Tsolis, R.M., Baumler, A.J., Stojiljkovic, I., and Heffron, F. (1995) Fur regulon of Salmonella typhimurium: Identification of new iron-regulated genes. J Bacteriol 177: 4628-4637.
    • (1995) J Bacteriol , vol.177 , pp. 4628-4637
    • Tsolis, R.M.1    Baumler, A.J.2    Stojiljkovic, I.3    Heffron, F.4
  • 50
    • 0034662454 scopus 로고    scopus 로고
    • The iron-responsive regulator Fur of Campylobacter jejuni is expressed from two separate promoters
    • van Vliet, A.H., Rock, J.D., Madeleine, L.N., and Ketley, J.M. (2000) The iron-responsive regulator Fur of Campylobacter jejuni is expressed from two separate promoters. FEMS Microbiol Lett 188: 115-118.
    • (2000) FEMS Microbiol Lett , vol.188 , pp. 115-118
    • Van Vliet, A.H.1    Rock, J.D.2    Madeleine, L.N.3    Ketley, J.M.4
  • 51
    • 0025132642 scopus 로고
    • Chloramphenicol resistance in Campylobacter coli: Nucleotide sequence, expression, and cloning vector construction
    • Wang, Y., and Taylor, D.E. (1990) Chloramphenicol resistance in Campylobacter coli: Nucleotide sequence, expression, and cloning vector construction. Gene 94: 23-28.
    • (1990) Gene , vol.94 , pp. 23-28
    • Wang, Y.1    Taylor, D.E.2
  • 52
    • 0031033529 scopus 로고    scopus 로고
    • Purification of Vibrio cholerae Fur and estimation of its intracellular abundance by antibody sandwich enzyme-linked immunosorbent assay
    • Watnick, P.I., Eto, T., Takahashi, H., and Calderwood, S.B. (1997) Purification of Vibrio cholerae Fur and estimation of its intracellular abundance by antibody sandwich enzyme-linked immunosorbent assay. J Bacteriol 179: 243-247.
    • (1997) J Bacteriol , vol.179 , pp. 243-247
    • Watnick, P.I.1    Eto, T.2    Takahashi, H.3    Calderwood, S.B.4
  • 53
    • 0027936183 scopus 로고
    • Structural and functional analyses of mutant Fur proteins with impaired regulatory function
    • Wertheimer, A.M., Tolmasky, M.E., Actis, L.A., and Crosa, J.H. (1994) Structural and functional analyses of mutant Fur proteins with impaired regulatory function. J Bacteriol 176: 5116-5122.
    • (1994) J Bacteriol , vol.176 , pp. 5116-5122
    • Wertheimer, A.M.1    Tolmasky, M.E.2    Actis, L.A.3    Crosa, J.H.4
  • 54
    • 0028860071 scopus 로고
    • Analysis of expression of CagA and VacA Virulence Factors in 43 strains of Helicobacter pylori reveals that clinical isolates can be divided into two major types and that CagA is not necessary for expression of the vacuolating cytotoxin
    • Xiang, Z., Censini, S., Babeli, P.F., Telford, J.L., Figura, N., Rappuoli, R., and Covacci, A. (1995) Analysis of expression of CagA and VacA Virulence Factors in 43 strains of Helicobacter pylori reveals that clinical isolates can be divided into two major types and that CagA is not necessary for expression of the vacuolating cytotoxin. Infect Immun 63: 94-98.
    • (1995) Infect Immun , vol.63 , pp. 94-98
    • Xiang, Z.1    Censini, S.2    Babeli, P.F.3    Telford, J.L.4    Figura, N.5    Rappuoli, R.6    Covacci, A.7
  • 55
    • 0031045215 scopus 로고    scopus 로고
    • Detection of tetramerization domains in vivo by cooperative DNA binding to tandem lambda operator sites
    • Zeng, X., and Hu, J. (1997) Detection of tetramerization domains in vivo by cooperative DNA binding to tandem lambda operator sites. Gene 185: 745-749.
    • (1997) Gene , vol.185 , pp. 745-749
    • Zeng, X.1    Hu, J.2
  • 56
    • 0033758935 scopus 로고    scopus 로고
    • Characterization of the DNA- and metal-binding properties of Vibrio anguillarum fur reveals conservation of a structural Zn (2+) ion
    • Zheleznova, E.E., Crosa, J.H., and Brennan, R.G. (2000) Characterization of the DNA- and metal-binding properties of Vibrio anguillarum fur reveals conservation of a structural Zn (2+) ion. J Bacteriol 182: 6264-6267.
    • (2000) J Bacteriol , vol.182 , pp. 6264-6267
    • Zheleznova, E.E.1    Crosa, J.H.2    Brennan, R.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.