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Volumn 20, Issue 3-4, 2007, Pages 485-499

Functional specialization within the fur family of metalloregulators

Author keywords

Fur; Metal homeostasis; Metalloregulation

Indexed keywords

FERRIC UPTAKE REGULATOR PROTEIN; IRON; MANGANESE; NICKEL; PROTEIN; UNCLASSIFIED DRUG; ZINC;

EID: 34248669001     PISSN: 09660844     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10534-006-9070-7     Document Type: Conference Paper
Times cited : (353)

References (101)
  • 1
    • 0033025239 scopus 로고    scopus 로고
    • Ferritin mutants of Escherichia coli are iron deficient and growth impaired, and fur mutants are iron deficient
    • Abdul-Tehrani H, Hudson AJ, Chang YS et al (1999) Ferritin mutants of Escherichia coli are iron deficient and growth impaired, and fur mutants are iron deficient. J Bacteriol 181:1415-1428
    • (1999) J Bacteriol , vol.181 , pp. 1415-1428
    • Abdul-Tehrani, H.1    Hudson, A.J.2    Chang, Y.S.3
  • 2
    • 33645467335 scopus 로고    scopus 로고
    • Nur, a nickel-responsive regulator of the fur family, regulates superoxide dismutases and nickel transport in Streptomyces coelicolor
    • Ahn BE, Cha J, Lee EJ, Han AR, Thompson CJ, Roe JH (2006) Nur, a nickel-responsive regulator of the Fur family, regulates superoxide dismutases and nickel transport in Streptomyces coelicolor. Mol Microbiol 59:1848-1858
    • (2006) Mol Microbiol , vol.59 , pp. 1848-1858
    • Ahn, B.E.1    Cha, J.2    Lee, E.J.3    Han, A.R.4    Thompson, C.J.5    Roe, J.H.6
  • 3
    • 33645242873 scopus 로고    scopus 로고
    • Liberation of zinc-containing L31 (RpmE) from ribosomes by its paralogous gene product, YtiA, in Bacillus subtilis
    • Akanuma G, Nanamiya H, Natori Y, Nomura N, Kawamura F (2006) Liberation of zinc-containing L31 (RpmE) from ribosomes by its paralogous gene product, YtiA, in Bacillus subtilis. J Bacteriol 188:2715-2720
    • (2006) J Bacteriol , vol.188 , pp. 2715-2720
    • Akanuma, G.1    Nanamiya, H.2    Natori, Y.3    Nomura, N.4    Kawamura, F.5
  • 4
    • 33745901282 scopus 로고    scopus 로고
    • Regulation of the Helicobacter pylori Fe-S cluster synthesis protein NifS by iron, oxidative stress conditions, and fur
    • Alamuri P, Mehta N, Burk A, Maier RJ (2006) Regulation of the Helicobacter pylori Fe-S cluster synthesis protein NifS by iron, oxidative stress conditions, and Fur. J Bacteriol 188:5325-5330
    • (2006) J Bacteriol , vol.188 , pp. 5325-5330
    • Alamuri, P.1    Mehta, N.2    Burk, A.3    Maier, R.J.4
  • 6
    • 0023664923 scopus 로고
    • Ferric uptake regulation protein acts as a repressor, employing iron (II) as a cofactor to bind the operator of an iron transport operon in Escherichia coli
    • Bagg A, Neilands JB (1987a) Ferric uptake regulation protein acts as a repressor, employing iron (II) as a cofactor to bind the operator of an iron transport operon in Escherichia coli. Biochemistry 26:5471-5477
    • (1987) Biochemistry , vol.26 , pp. 5471-5477
    • Bagg, A.1    Neilands, J.B.2
  • 7
    • 0023576859 scopus 로고
    • Molecular mechanism of regulation of siderophore-mediated iron assimilation
    • Bagg A, Neilands JB (1987b) Molecular mechanism of regulation of siderophore-mediated iron assimilation. Microbiol Rev 51:509-518
    • (1987) Microbiol Rev , vol.51 , pp. 509-518
    • Bagg, A.1    Neilands, J.B.2
  • 8
    • 0036837766 scopus 로고    scopus 로고
    • Recognition of DNA by Fur: A reinterpretation of the fur box consensus sequence
    • Baichoo N, Helmann JD (2002) Recognition of DNA by Fur: a reinterpretation of the Fur box consensus sequence. J Bacteriol 184:5826-5832
    • (2002) J Bacteriol , vol.184 , pp. 5826-5832
    • Baichoo, N.1    Helmann, J.D.2
  • 9
    • 0036035079 scopus 로고    scopus 로고
    • Global analysis of the Bacillus subtilis fur regulon and the iron starvation stimulon
    • Baichoo N, Wang T, Ye R, Helmann JD (2002) Global analysis of the Bacillus subtilis Fur regulon and the iron starvation stimulon. Mol Microbiol 45:1613-1629
    • (2002) Mol Microbiol , vol.45 , pp. 1613-1629
    • Baichoo, N.1    Wang, T.2    Ye, R.3    Helmann, J.D.4
  • 10
    • 33644541097 scopus 로고    scopus 로고
    • In vitro characterization of a bacterial manganese uptake regulator of the fur superfamily
    • Bellini P, Hemmings AM (2006) In vitro characterization of a bacterial manganese uptake regulator of the fur superfamily. Biochemistry 45:2686-2698
    • (2006) Biochemistry , vol.45 , pp. 2686-2698
    • Bellini, P.1    Hemmings, A.M.2
  • 11
    • 3142749997 scopus 로고    scopus 로고
    • Iron uptake by Escherichia coli
    • Braun V (2003) Iron uptake by Escherichia coli. Front Biosci 8:s1409-s1421
    • (2003) Front Biosci , vol.8
    • Braun, V.1
  • 12
    • 12344298832 scopus 로고    scopus 로고
    • The PerR regulon in peroxide resistance and virulence of Streptococcus pyogenes
    • Brenot A, King KY, Caparon MG (2005) The PerR regulon in peroxide resistance and virulence of Streptococcus pyogenes. Mol Microbiol 55:221-234
    • (2005) Mol Microbiol , vol.55 , pp. 221-234
    • Brenot, A.1    King, K.Y.2    Caparon, M.G.3
  • 13
    • 0029854169 scopus 로고    scopus 로고
    • Mutation of the Bacillus subtilis alkyl hydroperoxide reductase (ahpCF) operon reveals compensatory interactions among hydrogen peroxide stress genes
    • Bsat N, Chen L, Helmann JD (1996) Mutation of the Bacillus subtilis alkyl hydroperoxide reductase (ahpCF) operon reveals compensatory interactions among hydrogen peroxide stress genes. J Bacteriol 178:6579-6586
    • (1996) J Bacteriol , vol.178 , pp. 6579-6586
    • Bsat, N.1    Chen, L.2    Helmann, J.D.3
  • 14
    • 0032811011 scopus 로고    scopus 로고
    • Interaction of Bacillus subtilis fur (ferric uptake repressor) with the dhb operator in vitro and in vivo
    • Bsat N, Helmann JD (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
  • 15
    • 0031850630 scopus 로고    scopus 로고
    • Bacillus subtilis contains multiple fur homologues:identification of the iron uptake (Fur) and peroxide regulon (PerR) repressors
    • Bsat N, Herbig A, Casillas-Martinez L, Setlow P, Helmann JD (1998) Bacillus subtilis contains multiple Fur homologues:identification of the iron uptake (Fur) and peroxide regulon (PerR) repressors. Mol Microbiol 29:189-198
    • (1998) Mol Microbiol , vol.29 , pp. 189-198
    • Bsat, N.1    Herbig, A.2    Casillas-Martinez, L.3    Setlow, P.4    Helmann, J.D.5
  • 16
    • 0028861959 scopus 로고
    • Bacillus subtilis MrgA is a Dps(PexB) homologue: Evidence for metalloregulation of an oxidative-stress gene
    • Chen L, Helmann JD (1995) Bacillus subtilis MrgA is a Dps(PexB) homologue: evidence for metalloregulation of an oxidative-stress gene. Mol Microbiol 18:295-300
    • (1995) Mol Microbiol , vol.18 , pp. 295-300
    • Chen, L.1    Helmann, J.D.2
  • 17
    • 0027218065 scopus 로고
    • Metalloregulation in Bacillus subtilis: Isolation and characterization of two genes differentially repressed by metal ions
    • Chen L, James LP, Helmann JD (1993) Metalloregulation in Bacillus subtilis: isolation and characterization of two genes differentially repressed by metal ions. J Bacteriol 175:5428-5437
    • (1993) J Bacteriol , vol.175 , pp. 5428-5437
    • Chen, L.1    James, L.P.2    Helmann, J.D.3
  • 18
    • 0029152774 scopus 로고
    • Coordinate regulation of Bacillus subtilis peroxide stress genes by hydrogen peroxide and metal ions
    • Chen L, Keramati L, Helmann JD (1995) Coordinate regulation of Bacillus subtilis peroxide stress genes by hydrogen peroxide and metal ions. Proc Natl Acad Sci USA 92:8190-8204
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 8190-8204
    • Chen, L.1    Keramati, L.2    Helmann, J.D.3
  • 19
    • 0028151003 scopus 로고
    • Site-directed mutagenesis of the ferric uptake regulation gene of Escherichia coli
    • Coy M, Doyle C, Besser J, Neilands JB (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
  • 20
    • 0037168511 scopus 로고    scopus 로고
    • Direct inhibition by nitric oxide of the transcriptional ferric uptake regulation protein via nitrosylation of the iron
    • D'Autreaux B, Touati D, Bersch B, Latour JM, Michaud-Soret I (2002) Direct inhibition by nitric oxide of the transcriptional ferric uptake regulation protein via nitrosylation of the iron. Proc Natl Acad Sci USA 99:16619-16624
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 16619-16624
    • D'Autreaux, B.1    Touati, D.2    Bersch, B.3    Latour, J.M.4    Michaud-Soret, I.5
  • 21
    • 3042816068 scopus 로고    scopus 로고
    • Fur functions as an activator and as a repressor of putative virulence genes in Neisseria meningitidis
    • Delany I, Rappuoli R, Scarlato V (2004) Fur functions as an activator and as a repressor of putative virulence genes in Neisseria meningitidis. Mol Microbiol 52:1081-1090
    • (2004) Mol Microbiol , vol.52 , pp. 1081-1090
    • Delany, I.1    Rappuoli, R.2    Scarlato, V.3
  • 22
    • 0035724513 scopus 로고    scopus 로고
    • The fur repressor controls transcription of iron-activated and -repressed genes in Helicobacter pylori
    • Delany I, Spohn G, Rappuoli R, Scarlato V (2001) The Fur repressor controls transcription of iron-activated and -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
  • 23
    • 0344394987 scopus 로고    scopus 로고
    • An anti-repression fur operator upstream of the promoter is required for iron-mediated transcriptional autoregulation in Helicobacter pylori
    • Delany I, Spohn G, Rappuoli R, Scarlato V (2003) An anti-repression Fur operator upstream of the promoter is required for iron-mediated transcriptional autoregulation in Helicobacter pylori. Mol Microbiol 50:1329-1338
    • (2003) Mol Microbiol , vol.50 , pp. 1329-1338
    • Delany, I.1    Spohn, G.2    Rappuoli, R.3    Scarlato, V.4
  • 24
    • 2942585049 scopus 로고    scopus 로고
    • The Fur-like protein Mur of Rhizobium leguminosarum is a Mn(2+)-responsive transcriptional regulator
    • Diaz-Mireles E, Wexler M, Sawers G, Bellini D, Todd JD, Johnston AW (2004) The Fur-like protein Mur of Rhizobium leguminosarum is a Mn(2+)-responsive transcriptional regulator. Microbiology 150:1447-1456
    • (2004) Microbiology , vol.150 , pp. 1447-1456
    • Diaz-Mireles, E.1    Wexler, M.2    Sawers, G.3    Bellini, D.4    Todd, J.D.5    Johnston, A.W.6
  • 25
    • 29244471715 scopus 로고    scopus 로고
    • The manganese-responsive repressor Mur of Rhizobium leguminosarum is a member of the Fur-superfamily that recognizes an unusual operator sequence
    • Diaz-Mireles E, Wexler M, Todd JD, Bellini D, Johnston AW, Sawers RG (2005) The manganese-responsive repressor Mur of Rhizobium leguminosarum is a member of the Fur-superfamily that recognizes an unusual operator sequence. Microbiology 151:4071-4078
    • (2005) Microbiology , vol.151 , pp. 4071-4078
    • Diaz-Mireles, E.1    Wexler, M.2    Todd, J.D.3    Bellini, D.4    Johnston, A.W.5    Sawers, R.G.6
  • 26
    • 14044268800 scopus 로고    scopus 로고
    • Transcriptional profiling of Helicobacter pylori Fur- and iron-regulated gene expression
    • Ernst FD, Bereswill S, Waidner B et al (2005) Transcriptional profiling of Helicobacter pylori Fur- and iron-regulated gene expression. Microbiology 151:533-546
    • (2005) Microbiology , vol.151 , pp. 533-546
    • Ernst, F.D.1    Bereswill, S.2    Waidner, B.3
  • 27
    • 21044458727 scopus 로고    scopus 로고
    • Iron-responsive regulation of the Helicobacter pylori iron-cofactored superoxide dismutase SodB is mediated by fur
    • Ernst FD, Homuth G, Stoof J et al (2005) Iron-responsive regulation of the Helicobacter pylori iron-cofactored superoxide dismutase SodB is mediated by Fur. J Bacteriol 187:3687-3692
    • (2005) J Bacteriol , vol.187 , pp. 3687-3692
    • Ernst, F.D.1    Homuth, G.2    Stoof, J.3
  • 28
    • 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, 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
  • 29
    • 0344172832 scopus 로고    scopus 로고
    • Opening the iron box: Transcriptional metalloregulation by the fur protein
    • Escolar L, Perez-Martin J, 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
  • 30
    • 0026661296 scopus 로고
    • Effect of Salmonella typhimurium ferric uptake regulator (fur) mutations on iron- and pH-regulated protein synthesis
    • Foster JW, Hall HK (1992) Effect of Salmonella typhimurium ferric uptake regulator (fur) mutations on iron- and pH-regulated protein synthesis. J Bacteriol 174:4317-4323
    • (1992) J Bacteriol , vol.174 , pp. 4317-4323
    • Foster, J.W.1    Hall, H.K.2
  • 31
    • 3543030412 scopus 로고    scopus 로고
    • The ferric uptake regulator (Fur) protein from Bradyrhizobium japonicum is an iron-responsive transcriptional repressor in vitro
    • Friedman YE, O'Brian MR (2004) The ferric uptake regulator (Fur) protein from Bradyrhizobium japonicum is an iron-responsive transcriptional repressor in vitro. J Biol Chem 279:32100-32105
    • (2004) J Biol Chem , vol.279 , pp. 32100-32105
    • Friedman, Y.E.1    O'Brian, M.R.2
  • 32
    • 0142214661 scopus 로고    scopus 로고
    • Recognition of DNA by three ferric uptake regulator (Fur) homologs in Bacillus subtilis
    • Fuangthong M, Helmann JD (2003) Recognition of DNA by three ferric uptake regulator (Fur) homologs in Bacillus subtilis. J Bacteriol 185:6348-6357
    • (2003) J Bacteriol , vol.185 , pp. 6348-6357
    • Fuangthong, M.1    Helmann, J.D.2
  • 33
    • 0036267391 scopus 로고    scopus 로고
    • Regulation of the Bacillus subtilis fur and perR genes by PerR: Not all members of the PerR regulon are peroxide inducible
    • Fuangthong M, Herbig AF, Bsat N, Helmann JD (2002) Regulation of the Bacillus subtilis fur and perR genes by PerR: not all members of the PerR regulon are peroxide inducible. J Bacteriol 184:3276-3286
    • (2002) J Bacteriol , vol.184 , pp. 3276-3286
    • Fuangthong, M.1    Herbig, A.F.2    Bsat, N.3    Helmann, J.D.4
  • 34
    • 0031733646 scopus 로고    scopus 로고
    • Identification of a zinc-specific metalloregulatory protein, Zur, controlling zinc transport operons in Bacillus subtilis
    • Gaballa A, Helmann JD (1998) Identification of a zinc-specific metalloregulatory protein, Zur, controlling zinc transport operons in Bacillus subtilis. J Bacteriol 180:5815-5821
    • (1998) J Bacteriol , vol.180 , pp. 5815-5821
    • Gaballa, A.1    Helmann, J.D.2
  • 35
    • 0036041795 scopus 로고    scopus 로고
    • A peroxide-induced zinc uptake system plays an important role in protection against oxidative stress in Bacillus subtilis
    • Gaballa A, Helmann JD (2002) A peroxide-induced zinc uptake system plays an important role in protection against oxidative stress in Bacillus subtilis. Mol Microbiol 45:997-1005
    • (2002) Mol Microbiol , vol.45 , pp. 997-1005
    • Gaballa, A.1    Helmann, J.D.2
  • 36
    • 0036889461 scopus 로고    scopus 로고
    • Functional analysis of the Bacillus subtilis Zur regulon
    • Gaballa A, Wang T, Ye RW, Helmann JD (2002) Functional analysis of the Bacillus subtilis Zur regulon. J Bacteriol 184:6508-6514
    • (2002) J Bacteriol , vol.184 , pp. 6508-6514
    • Gaballa, A.1    Wang, T.2    Ye, R.W.3    Helmann, J.D.4
  • 37
    • 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 et al (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
    • De Gonzalez Peredo, A.1    Saint-Pierre, C.2    Adrait, A.3
  • 38
    • 0042423728 scopus 로고    scopus 로고
    • Identification of iron-activated and -repressed Fur-dependent genes by transcriptome analysis of Neisseria meningitidis group B
    • Grifantini R, Sebastian S, Frigimelica E et al (2003) Identification of iron-activated and -repressed Fur-dependent genes by transcriptome analysis of Neisseria meningitidis group B. Proc Natl Acad Sci USA 100:9542-9547
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 9542-9547
    • Grifantini, R.1    Sebastian, S.2    Frigimelica, E.3
  • 39
    • 0038349048 scopus 로고    scopus 로고
    • Origins of metal ion selectivity in the DtxR/MntR family of metalloregulators
    • Guedon E, Helmann JD (2003) Origins of metal ion selectivity in the DtxR/MntR family of metalloregulators. Mol Microbiol 48:495-506
    • (2003) Mol Microbiol , vol.48 , pp. 495-506
    • Guedon, E.1    Helmann, J.D.2
  • 40
    • 0034623713 scopus 로고    scopus 로고
    • 2-sensitive fur-like repressor CatR regulating the major catalase gene in Streptomyces coelicolor
    • 2-sensitive fur-like repressor CatR regulating the major catalase gene in Streptomyces coelicolor. J Biol Chem 275:38254-38260
    • (2000) J Biol Chem , vol.275 , pp. 38254-38260
    • Hahn, J.S.1    Oh, S.Y.2    Chater, K.F.3    Cho, Y.H.4    Roe, J.H.5
  • 41
    • 0029818614 scopus 로고    scopus 로고
    • The role of fur in the acid tolerance response of Salmonella typhimurium is physiologically and genetically separable from its role in iron acquisition
    • Hall HK, Foster JW (1996) The role of fur in 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
  • 42
    • 0032555562 scopus 로고    scopus 로고
    • The bacterial Irr protein is required for coordination of heme biosynthesis with iron availability
    • Hamza I, Chauhan S, Hassett R, O'Brian MR (1998) The bacterial Irr protein is required for coordination of heme biosynthesis with iron availability. J Biol Chem 273:21669-21674
    • (1998) J Biol Chem , vol.273 , pp. 21669-21674
    • Hamza, I.1    Chauhan, S.2    Hassett, R.3    O'Brian, M.R.4
  • 43
    • 0032884580 scopus 로고    scopus 로고
    • Identification of a functional fur gene in Bradyrhizobium japonicum
    • Hamza I, Hassett R, O'Brian MR (1999) Identification of a functional fur gene in Bradyrhizobium japonicum. J Bacteriol 181:5843-5846
    • (1999) J Bacteriol , vol.181 , pp. 5843-5846
    • Hamza, I.1    Hassett, R.2    O'Brian, M.R.3
  • 44
    • 0019447069 scopus 로고
    • Regulation of ferric iron transport in Escherichia coli K12: Isolation of a constitutive mutant
    • Hantke K (1981) Regulation of ferric iron transport in Escherichia coli K12: isolation of a constitutive mutant. Mol Gen Genet 182:288-292
    • (1981) Mol Gen Genet , vol.182 , pp. 288-292
    • Hantke, K.1
  • 45
    • 0023443062 scopus 로고
    • Selection Procedure for deregulated iron transport mutants (fur) in Escherichia coli K (12): Fur not only affects iron metabolism
    • Hantke K (1987) Selection Procedure for deregulated iron transport mutants (fur) in Escherichia coli K (12): fur not only affects iron metabolism. Mol Gen Genet 210:135-139
    • (1987) Mol Gen Genet , vol.210 , pp. 135-139
    • Hantke, K.1
  • 46
    • 0035069457 scopus 로고    scopus 로고
    • Iron and metal regulation in bacteria
    • Hantke K (2001) Iron and metal regulation in bacteria. Curr Opin Microbiol 4:172-177
    • (2001) Curr Opin Microbiol , vol.4 , pp. 172-177
    • Hantke, K.1
  • 48
    • 0037215627 scopus 로고    scopus 로고
    • The global transcriptional response of Bacillus subtilis to peroxide stress is coordinated by three transcription factors
    • Helmann JD, Wu MF, Gaballa A et al (2003) The global transcriptional response of Bacillus subtilis to peroxide stress is coordinated by three transcription factors. J Bacteriol 185:243-253
    • (2003) J Bacteriol , vol.185 , pp. 243-253
    • Helmann, J.D.1    Wu, M.F.2    Gaballa3
  • 49
    • 0035723780 scopus 로고    scopus 로고
    • Roles of metal ions and hydrogen peroxide in modulating the interaction of the Bacillus subtilis PerR peroxide regulon repressor with operator DNA
    • Herbig AF, Helmann JD (2001) Roles of metal ions and hydrogen peroxide in modulating the interaction of the Bacillus subtilis PerR peroxide regulon repressor with operator DNA. Mol Microbiol 41:849-859
    • (2001) Mol Microbiol , vol.41 , pp. 849-859
    • Herbig, A.F.1    Helmann, J.D.2
  • 51
    • 0035013928 scopus 로고    scopus 로고
    • PerR controls oxidative stress resistance and iron storage proteins and is required for virulence in Staphylococcus aureus
    • Horsburgh MJ, Clements MO, Crossley H, Ingham E, Foster SJ (2001) PerR controls oxidative stress resistance and iron storage proteins and is required for virulence in Staphylococcus aureus. Infect Immun 69:3744-3754
    • (2001) Infect Immun , vol.69 , pp. 3744-3754
    • Horsburgh, M.J.1    Clements, M.O.2    Crossley, H.3    Ingham, E.4    Foster, S.J.5
  • 52
    • 0036015643 scopus 로고    scopus 로고
    • MntR modulates expression of the PerR regulon and superoxide resistance in Staphylococcus aureus through control of manganese uptake
    • Horsburgh MJ, Wharton SJ, Cox AG, Ingham E, Peacock S, Foster SJ (2002) MntR modulates expression of the PerR regulon and superoxide resistance in Staphylococcus aureus through control of manganese uptake. Mol Microbiol 44:1269-1286
    • (2002) Mol Microbiol , vol.44 , pp. 1269-1286
    • Horsburgh, M.J.1    Wharton, S.J.2    Cox, A.G.3    Ingham, E.4    Peacock, S.5    Foster, S.J.6
  • 54
    • 0030465238 scopus 로고    scopus 로고
    • Superoxide accelerates DNA damage by elevating free-iron levels
    • Keyer K, Imlay JA (1996) Superoxide accelerates DNA damage by elevating free-iron levels Proc Natl Acad Sci USA 93:13635-13640
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 13635-13640
    • Keyer, K.1    Imlay, J.A.2
  • 55
    • 14044259281 scopus 로고    scopus 로고
    • Exploiting thiol modifications
    • Kiley PJ, Storz G (2004) Exploiting thiol modifications. PLoS Biol 2:e400
    • (2004) PLoS Biol , vol.2 , pp. 400
    • Kiley, P.J.1    Storz, G.2
  • 56
    • 0033797110 scopus 로고    scopus 로고
    • Aerotolerance and peroxide resistance in peroxidase and PerR mutants of Streptococcus pyogenes
    • King KY, Horenstein JA, Caparon MG (2000) Aerotolerance and peroxide resistance in peroxidase and PerR mutants of Streptococcus pyogenes. J Bacteriol 182:5290-5299
    • (2000) J Bacteriol , vol.182 , pp. 5290-5299
    • King, K.Y.1    Horenstein, J.A.2    Caparon, M.G.3
  • 57
    • 0028068734 scopus 로고
    • Vibrio cholerae fur mutations associated with loss of repressor activity:implications for the structural-functional relationships of fur
    • Lam MS, Litwin CM, Carroll PA, Calderwood SB (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
  • 58
    • 0036415664 scopus 로고    scopus 로고
    • Fur-DNA interactions at the bidirectional fepDGC-entS promoter region in Escherichia coli
    • Lavrrar JL, Christoffersen CA, McIntosh MA (2002) Fur-DNA interactions at the bidirectional fepDGC-entS promoter region in Escherichia coli. J Mol Biol 322:983-995
    • (2002) J Mol Biol , vol.322 , pp. 983-995
    • Lavrrar, J.L.1    Christoffersen, C.A.2    McIntosh, M.A.3
  • 59
    • 0037381732 scopus 로고    scopus 로고
    • Architecture of a fur binding site: A comparative analysis
    • Lavrrar JL, McIntosh MA (2003) Architecture of a fur binding site: a comparative analysis. J Bacteriol 185:2194-2202
    • (2003) J Bacteriol , vol.185 , pp. 2194-2202
    • Lavrrar, J.L.1    McIntosh, M.A.2
  • 60
    • 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, 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
  • 61
    • 33747722767 scopus 로고    scopus 로고
    • 2+ site in the Bacillus subtilis peroxide sensor PerR
    • 2+ site in the Bacillus subtilis peroxide sensor PerR. J Biol Chem 281:23567-23578
    • (2006) J Biol Chem , vol.281 , pp. 23567-23578
    • Lee, J.W.1    Helmann, J.D.2
  • 62
    • 33645037891 scopus 로고    scopus 로고
    • 2 by metal-catalysed histidine oxidation
    • 2 by metal-catalysed histidine oxidation. Nature 440:363-367
    • (2006) Nature , vol.440 , pp. 363-367
    • Lee, J.W.1    Helmann, J.D.2
  • 63
    • 0036667431 scopus 로고    scopus 로고
    • The ferric uptake regulator of Pseudomonas aeruginosa has no essential cysteine residues and does not contain a structural zinc ion
    • Lewin AC, Doughty PA, Flegg L, Moore GR, Spiro S (2002) The ferric uptake regulator of Pseudomonas aeruginosa has no essential cysteine residues and does not contain a structural zinc ion. Microbiology 148:2449-2456
    • (2002) Microbiology , vol.148 , pp. 2449-2456
    • Lewin, A.C.1    Doughty, P.A.2    Flegg, L.3    Moore, G.R.4    Spiro, S.5
  • 64
    • 0028181626 scopus 로고
    • Analysis of the complexity of gene regulation by fur in Vibrio cholerae
    • Litwin CM, Calderwood SB (1994) Analysis of the complexity of gene regulation by fur in Vibrio cholerae. J Bacteriol 176:240-248
    • (1994) J Bacteriol , vol.176 , pp. 240-248
    • Litwin, C.M.1    Calderwood, S.B.2
  • 65
    • 22744439747 scopus 로고    scopus 로고
    • Ironing out the problem: New mechanisms of iron homeostasis
    • Masse E, Arguin M (2005) Ironing out the problem: new mechanisms of iron homeostasis. Trends Biochem Sci 30:462-468
    • (2005) Trends Biochem Sci , vol.30 , pp. 462-468
    • Masse, E.1    Arguin, M.2
  • 66
    • 0037007078 scopus 로고    scopus 로고
    • A small RNA regulates the expression of genes involved in iron metabolism in Escherichia coli
    • Masse E, Gottesman S (2002) A small RNA regulates the expression of genes involved in iron metabolism in Escherichia coli. Proc Natl Acad Sci USA 99:4620-4625
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 4620-4625
    • Masse, E.1    Gottesman, S.2
  • 67
    • 26444505976 scopus 로고    scopus 로고
    • Effect of RyhB small RNA on global iron use in Escherichia coli
    • Masse E, Vanderpool CK, Gottesman S (2005) Effect of RyhB small RNA on global iron use in Escherichia coli. J Bacteriol 187:6962-6971
    • (2005) J Bacteriol , vol.187 , pp. 6962-6971
    • Masse, E.1    Vanderpool, C.K.2    Gottesman, S.3
  • 69
    • 23944509113 scopus 로고    scopus 로고
    • Characterization of Vibrio cholerae RyhB: The RyhB regulon and role of ryhB in biofilm formation
    • Mey AR, Craig SA, Payne SM (2005) Characterization of Vibrio cholerae RyhB: the RyhB regulon and role of ryhB in biofilm formation. Infect Immun 73:5706-5719
    • (2005) Infect Immun , vol.73 , pp. 5706-5719
    • Mey, A.R.1    Craig, S.A.2    Payne, S.M.3
  • 70
    • 26644471490 scopus 로고    scopus 로고
    • Metal binding characteristics and role of iron oxidation in the ferric uptake regulator from Escherichia coli
    • Mills SA, Marletta MA (2005) Metal binding characteristics and role of iron oxidation in the ferric uptake regulator from Escherichia coli. Biochemistry 44:13553-13559
    • (2005) Biochemistry , vol.44 , pp. 13553-13559
    • Mills, S.A.1    Marletta, M.A.2
  • 71
    • 0036047508 scopus 로고    scopus 로고
    • Regulation of inducible peroxide stress responses
    • Mongkolsuk S, Helmann JD (2002) Regulation of inducible peroxide stress responses. Mol Microbiol 45:9-15
    • (2002) Mol Microbiol , vol.45 , pp. 9-15
    • Mongkolsuk, S.1    Helmann, J.D.2
  • 72
    • 3042855371 scopus 로고    scopus 로고
    • Response of Bacillus subtilis to nitric oxide and the nitrosating agent sodium nitroprusside
    • Moore CM, Nakano MM, Wang T, Ye RW, Helmann JD (2004) Response of Bacillus subtilis to nitric oxide and the nitrosating agent sodium nitroprusside. J Bacteriol 186:4655-4664
    • (2004) J Bacteriol , vol.186 , pp. 4655-4664
    • Moore, C.M.1    Nakano, M.M.2    Wang, T.3    Ye, R.W.4    Helmann, J.D.5
  • 73
    • 0842326281 scopus 로고    scopus 로고
    • The staphylococcal ferritins are differentially regulated in response to iron and manganese and via PerR and fur
    • Morrissey JA, Cockayne A, Brummell K, Williams P (2004) The staphylococcal ferritins are differentially regulated in response to iron and manganese and via PerR and Fur. Infect Immun 72:972-979
    • (2004) Infect Immun , vol.72 , pp. 972-979
    • Morrissey, J.A.1    Cockayne, A.2    Brummell, K.3    Williams, P.4
  • 74
    • 1242318677 scopus 로고    scopus 로고
    • Transcriptome and proteome analysis of Bacillus subtilis gene expression in response to superoxide and peroxide stress
    • Mostertz J, Scharf C, Hecker M, Homuth G (2004) Transcriptome and proteome analysis of Bacillus subtilis gene expression in response to superoxide and peroxide stress. Microbiology 150:497-512
    • (2004) Microbiology , vol.150 , pp. 497-512
    • Mostertz, J.1    Scharf, C.2    Hecker, M.3    Homuth, G.4
  • 75
    • 0035968001 scopus 로고    scopus 로고
    • Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis
    • Outten CE, O'Halloran TV (2001) Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis. Science 292:2488-2492
    • (2001) Science , vol.292 , pp. 2488-2492
    • Outten, C.E.1    O'Halloran, T.V.2
  • 76
    • 0035807029 scopus 로고    scopus 로고
    • Characterization of the metal receptor sites in Escherichia coli Zur, an ultrasensitive zinc(II) metalloregulatory protein
    • Outten CE, Tobin DA, Penner-Hahn JE, O'Halloran TV (2001) Characterization of the metal receptor sites in Escherichia coli Zur, an ultrasensitive zinc(II) metalloregulatory protein. Biochemistry 40:10417-10423
    • (2001) Biochemistry , vol.40 , pp. 10417-10423
    • Outten, C.E.1    Tobin, D.A.2    Penner-Hahn, J.E.3    O'Halloran, T.V.4
  • 77
    • 0141492988 scopus 로고    scopus 로고
    • Thiol-based regulatory switches
    • Paget MS, Buttner MJ (2003) Thiol-based regulatory switches. Annu Rev Genet 37:91-121
    • (2003) Annu Rev Genet , vol.37 , pp. 91-121
    • Paget, M.S.1    Buttner, M.J.2
  • 78
    • 0035945257 scopus 로고    scopus 로고
    • Comparative analysis of fur regulons in gamma-proteobacteria
    • Panina EM, Mironov AA, Gelfand MS (2001) Comparative analysis of FUR regulons in gamma-proteobacteria. Nucleic Acids Res 29:5195-5206
    • (2001) Nucleic Acids Res , vol.29 , pp. 5195-5206
    • Panina, E.M.1    Mironov, A.A.2    Gelfand, M.S.3
  • 79
    • 0043193943 scopus 로고    scopus 로고
    • Comparative genomics of bacterial zinc regulons: Enhanced ion transport, pathogenesis, and rearrangement of ribosomal proteins
    • Panina EM, Mironov AA, Gelfand MS (2003) Comparative genomics of bacterial zinc regulons: enhanced ion transport, pathogenesis, and rearrangement of ribosomal proteins. Proc Natl Acad Sci USA 100:9912-9917
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 9912-9917
    • Panina, E.M.1    Mironov, A.A.2    Gelfand, M.S.3
  • 80
    • 0031798662 scopus 로고    scopus 로고
    • The ZnuABC high-affinity zinc uptake system and its regulator Zur in Escherichia coli
    • Patzer SI, Hantke K (1998) The ZnuABC high-affinity zinc uptake system and its regulator Zur in Escherichia coli. Mol Microbiol 28:1199-1210
    • (1998) Mol Microbiol , vol.28 , pp. 1199-1210
    • Patzer, S.I.1    Hantke, K.2
  • 81
    • 0034637471 scopus 로고    scopus 로고
    • The zinc-responsive regulator Zur and its control of the znu gene cluster encoding the ZnuABC zinc uptake system in Escherichia coli
    • Patzer SI, Hantke K (2000) The zinc-responsive regulator Zur and its control of the znu gene cluster encoding the ZnuABC zinc uptake system in Escherichia coli. J Biol Chem 275:24321-24332
    • (2000) J Biol Chem , vol.275 , pp. 24321-24332
    • Patzer, S.I.1    Hantke, K.2
  • 83
    • 0344321893 scopus 로고    scopus 로고
    • Architecture of a protein central to iron homeostasis: Crystal structure and spectroscopic analysis of the ferric uptake regulator
    • Pohl E, Haller JC, Mijovilovich A, Meyer-Klaucke W, Garman E, Vasil ML (2003) Architecture of a protein central to iron homeostasis: crystal structure and spectroscopic analysis of the ferric uptake regulator. Mol Microbiol 47:903-915
    • (2003) Mol Microbiol , vol.47 , pp. 903-915
    • Pohl, E.1    Haller, J.C.2    Mijovilovich, A.3    Meyer-Klaucke, W.4    Garman, E.5    Vasil, M.L.6
  • 84
    • 11844257593 scopus 로고    scopus 로고
    • Coordinated remodeling of cellular metabolism during iron deficiency through targeted mRNA degradation
    • Puig S, Askeland E, Thiele DJ (2005) Coordinated remodeling of cellular metabolism during iron deficiency through targeted mRNA degradation. Cell 120:99-110
    • (2005) Cell , vol.120 , pp. 99-110
    • Puig, S.1    Askeland, E.2    Thiele, D.J.3
  • 85
    • 0033539642 scopus 로고    scopus 로고
    • Heme is an effector molecule for iron-dependent degradation of the bacterial iron response regulator (Irr) protein
    • Qi Z, Hamza I, O'Brian MR (1999) Heme is an effector molecule for iron-dependent degradation of the bacterial iron response regulator (Irr) protein. Proc Natl Acad Sci USA 96:13056-13061
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 13056-13061
    • Qi, Z.1    Hamza, I.2    O'Brian, M.R.3
  • 86
    • 0036161801 scopus 로고    scopus 로고
    • Interaction between the bacterial iron response regulator and ferrochelatase mediates genetic control of heme biosynthesis
    • Qi Z, O'Brian MR (2002) Interaction between the bacterial iron response regulator and ferrochelatase mediates genetic control of heme biosynthesis. Mol Cell 9:155-162
    • (2002) Mol Cell , vol.9 , pp. 155-162
    • Qi, Z.1    O'Brian, M.R.2
  • 87
    • 29144438143 scopus 로고    scopus 로고
    • Listeria monocytogenes perR mutants display a small-colony phenotype, increased sensitivity to hydrogen peroxide, and significantly reduced murine virulence
    • Rea R, Hill C, Gahan CG (2005) Listeria monocytogenes perR mutants display a small-colony phenotype, increased sensitivity to hydrogen peroxide, and significantly reduced murine virulence. Appl Environ Microbiol 71:8314-8322
    • (2005) Appl Environ Microbiol , vol.71 , pp. 8314-8322
    • Rea, R.1    Hill, C.2    Gahan, C.G.3
  • 88
    • 0842327149 scopus 로고    scopus 로고
    • Disruption of putative regulatory loci in Listeria monocytogenes demonstrates a significant role for fur and PerR in virulence
    • Rea RB, Gahan CG, Hill C (2004) Disruption of putative regulatory loci in Listeria monocytogenes demonstrates a significant role for Fur and PerR in virulence. Infect Immun 72:717-727
    • (2004) Infect Immun , vol.72 , pp. 717-727
    • Rea, R.B.1    Gahan, C.G.2    Hill, C.3
  • 89
    • 33746482772 scopus 로고    scopus 로고
    • The nitrosative stress response of Staphylococcus aureus is required for resistance to innate immunity
    • Richardson AR, Dunman PM, Fang FC (2006) The nitrosative stress response of Staphylococcus aureus is required for resistance to innate immunity. Mol Microbiol 61:927-939
    • (2006) Mol Microbiol , vol.61 , pp. 927-939
    • Richardson, A.R.1    Dunman, P.M.2    Fang, F.C.3
  • 90
    • 22544432327 scopus 로고    scopus 로고
    • Reconstruction of regulatory and metabolic pathways in metal-reducing delta-proteobacteria
    • Rodionov DA, Dubchak I, Arkin A, Alm E, Gelfand MS (2004) Reconstruction of regulatory and metabolic pathways in metal-reducing delta-proteobacteria. Genome Biol 5:R90
    • (2004) Genome Biol , vol.5 , pp. 90
    • Rodionov, D.A.1    Dubchak, I.2    Arkin, A.3    Alm, E.4    Gelfand, M.S.5
  • 91
    • 33744979998 scopus 로고    scopus 로고
    • Beyond the fur paradigm: Iron-controlled gene expression in rhizobia
    • Rudolph G, Hennecke H, Fischer HM (2006a) Beyond the Fur paradigm: iron-controlled gene expression in rhizobia. FEMS Microbiol Rev 30:631-648
    • (2006) FEMS Microbiol Rev , vol.30 , pp. 631-648
    • Rudolph, G.1    Hennecke, H.2    Fischer, H.M.3
  • 92
    • 30844432187 scopus 로고    scopus 로고
    • The Iron control element, acting in positive and negative control of iron-regulated Bradyrhizobium japonicum genes, is a target for the Irr protein
    • Rudolph G, Semini G, Hauser F et al (2006b) The Iron control element, acting in positive and negative control of iron-regulated Bradyrhizobium japonicum genes, is a target for the Irr protein. J Bacteriol 188:733-744
    • (2006) J Bacteriol , vol.188 , pp. 733-744
    • Rudolph, G.1    Semini, G.2    Hauser, F.3
  • 93
    • 27644580799 scopus 로고    scopus 로고
    • Understanding how cells allocate metals using metal sensors and metallochaperones
    • Tottey S, Harvie DR, Robinson NJ (2005) Understanding how cells allocate metals using metal sensors and metallochaperones. Acc Chem Res 38:775-783
    • (2005) Acc Chem Res , vol.38 , pp. 775-783
    • Tottey, S.1    Harvie, D.R.2    Robinson, N.J.3
  • 94
    • 33747081033 scopus 로고    scopus 로고
    • Crystal structure of the apo-PerR-Zn protein from Bacillus subtilis
    • Traore DAK, El Gahzouani A, Ilango S et al (2006) Crystal structure of the apo-PerR-Zn protein from Bacillus subtilis. Mol Microbiol 61:1211-1219
    • (2006) Mol Microbiol , vol.61 , pp. 1211-1219
    • Traore, D.A.K.1    El Gahzouani, A.2    Ilango, S.3
  • 95
    • 0032716842 scopus 로고    scopus 로고
    • Campylobacter jejuni contains two fur homologs: Characterization of iron-responsive regulation of peroxide stress defense genes by the PerR repressor
    • van Vliet AH, Baillon ML, Penn CW, Ketley JM (1999) Campylobacter jejuni contains two fur homologs: characterization of iron-responsive regulation of peroxide stress defense genes by the PerR repressor. J Bacteriol 181:6371-6376
    • (1999) J Bacteriol , vol.181 , pp. 6371-6376
    • Van Vliet, A.H.1    Baillon, M.L.2    Penn, C.W.3    Ketley, J.M.4
  • 96
    • 28844486003 scopus 로고    scopus 로고
    • The AraC-type regulator RipA represses aconitase and other iron proteins from Corynebacterium under iron limitation and is itself repressed by DtxR
    • Wennerhold J, Krug A, Bott M (2005) The AraC-type regulator RipA represses aconitase and other iron proteins from Corynebacterium under iron limitation and is itself repressed by DtxR. J Biol Chem 280:40500-40508
    • (2005) J Biol Chem , vol.280 , pp. 40500-40508
    • Wennerhold, J.1    Krug, A.2    Bott, M.3
  • 97
    • 0032581662 scopus 로고    scopus 로고
    • Structure of the metal-ion-activated diphtheria toxin repressor/tox operator complex
    • White A, Ding X, vanderSpek JC, Murphy JR, Ringe D (1998) Structure of the metal-ion-activated diphtheria toxin repressor/tox operator complex. Nature 394:502-506
    • (1998) Nature , vol.394 , pp. 502-506
    • White, A.1    Ding, X.2    Vanderspek, J.C.3    Murphy, J.R.4    Ringe, D.5
  • 98
    • 3042840984 scopus 로고    scopus 로고
    • Identification of tandem duplicate regulatory small RNAs in Pseudomonas aeruginosa involved in iron homeostasis
    • Wilderman PJ, Sowa NA, FitzGerald DJ et al (2004) Identification of tandem duplicate regulatory small RNAs in Pseudomonas aeruginosa involved in iron homeostasis. Proc Natl Acad Sci USA 101:9792-9797
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 9792-9797
    • Wilderman, P.J.1    Sowa, N.A.2    Fitzgerald, D.J.3
  • 99
    • 14844355242 scopus 로고    scopus 로고
    • Two heme binding sites are involved in the regulated degradation of the bacterial iron response regulator (Irr) protein
    • Yang J, Ishimori K, O'Brian MR (2005) Two heme binding sites are involved in the regulated degradation of the bacterial iron response regulator (Irr) protein. J Biol Chem 280:7671-7676
    • (2005) J Biol Chem , vol.280 , pp. 7671-7676
    • Yang, J.1    Ishimori, K.2    O'Brian, M.R.3
  • 100
    • 33644838945 scopus 로고    scopus 로고
    • Oxidative stress promotes degradation of the Irr protein to regulate haem biosynthesis in Bradyrhizobium japonicum
    • Yang J, Panek HR, O'Brian MR (2006a) Oxidative stress promotes degradation of the Irr protein to regulate haem biosynthesis in Bradyrhizobium japonicum. Mol Microbiol 60:209-218
    • (2006) Mol Microbiol , vol.60 , pp. 209-218
    • Yang, J.1    Panek, H.R.2    O'Brian, M.R.3
  • 101
    • 33645322140 scopus 로고    scopus 로고
    • Bradyrhizobium japonicum senses iron through the status of haem to regulate iron homeostasis and metabolism
    • Yang J, Sangwan I, Lindemann A et al (2006b) Bradyrhizobium japonicum senses iron through the status of haem to regulate iron homeostasis and metabolism. Mol Microbiol 60:427-437
    • (2006) Mol Microbiol , vol.60 , pp. 427-437
    • Yang, J.1    Sangwan, I.2    Lindemann, A.3


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