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Volumn 194, Issue 5, 2012, Pages 925-931

The iron-binding protein Dps2 confers peroxide stress resistance on Bacillus anthracis

Author keywords

[No Author keywords available]

Indexed keywords

DEFEROXAMINE MESYLATE; DPS2 PROTEIN; HYDROGEN PEROXIDE; IRON; IRON BINDING PROTEIN; PERR REGULATOR PROTEIN; PROTEIN DERIVATIVE; UNCLASSIFIED DRUG;

EID: 84857779377     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.06005-11     Document Type: Article
Times cited : (20)

References (42)
  • 1
    • 0027083350 scopus 로고
    • A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli
    • Almiron M, Link AJ, Furlong D, Kolter R. 1992. A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli. Genes Dev. 6:2646-2654.
    • (1992) Genes Dev. , vol.6 , pp. 2646-2654
    • Almiron, M.1    Link, A.J.2    Furlong, D.3    Kolter, R.4
  • 2
    • 65549107862 scopus 로고    scopus 로고
    • Manganese import is a key element of the OxyR response to hydrogen peroxide in Escherichia coli
    • Anjem A, Varghese S, Imlay JA. 2009. Manganese import is a key element of the OxyR response to hydrogen peroxide in Escherichia coli. Mol. Microbiol. 72:844-858.
    • (2009) Mol. Microbiol. , vol.72 , pp. 844-858
    • Anjem, A.1    Varghese, S.2    Imlay, J.A.3
  • 3
    • 0030665283 scopus 로고    scopus 로고
    • Expression of a stress-and starvation-induced dps/pexB-homologous gene is controlled by the alternative sigma factor σB in Bacillus subtilis
    • Antelmann H, et al. 1997. Expression of a stress- and starvation-induced dps/pexB-homologous gene is controlled by the alternative sigma factor σB in Bacillus subtilis. J. Bacteriol. 179:7251-7256.
    • (1997) J. Bacteriol. , vol.179 , pp. 7251-7256
    • Antelmann, H.1
  • 4
    • 0036754957 scopus 로고    scopus 로고
    • Iron acquisition by Gram-positive bacterial pathogens
    • Brown JS, Holden DW. 2002. Iron acquisition by Gram-positive bacterial pathogens. Microbes Infect. 11:1149-1156.
    • (2002) Microbes Infect. , vol.11 , pp. 1149-1156
    • Brown, J.S.1    Holden, D.W.2
  • 5
    • 0033617958 scopus 로고    scopus 로고
    • Mineralization in ferritin: an efficient means of iron storage
    • Chasteen ND, Harrison PM. 1999. Mineralization in ferritin: an efficient means of iron storage. J. Struct. Biol. 126:182-194.
    • (1999) J. Struct. Biol. , vol.126 , pp. 182-194
    • Chasteen, N.D.1    Harrison, P.M.2
  • 6
    • 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
  • 7
    • 9644300997 scopus 로고    scopus 로고
    • β-Lactamase gene expression in a penicillin-resistant Bacillus anthracis strain Antimicrob
    • Chen Y, Tenover FC, Koehler TM. 2004. β-Lactamase gene expression in a penicillin-resistant Bacillus anthracis strain Antimicrob. Agents Chemother. 48:4873-4877.
    • (2004) Agents Chemother. , vol.48 , pp. 4873-4877
    • Chen, Y.1    Tenover, F.C.2    Koehler, T.M.3
  • 8
    • 84867948203 scopus 로고    scopus 로고
    • Dps proteins, an efficient detoxification and DNA protection machinery in the bacterial response to oxidative stress
    • Chiancone E. 2008. Dps proteins, an efficient detoxification and DNA protection machinery in the bacterial response to oxidative stress. Rendiconti Lincei 19:261-270.
    • (2008) Rendiconti Lincei , vol.19 , pp. 261-270
    • Chiancone, E.1
  • 10
    • 0036223585 scopus 로고    scopus 로고
    • Bacillus subtilis functional genomics: global characterization of the stringent response by proteome and transcriptome analysis
    • Eymann C, Homuth G, Scharf C, Hecker M. 2002. Bacillus subtilis functional genomics: global characterization of the stringent response by proteome and transcriptome analysis. J. Bacteriol. 184:2500-2520.
    • (2002) J. Bacteriol. , vol.184 , pp. 2500-2520
    • Eymann, C.1    Homuth, G.2    Scharf, C.3    Hecker, M.4
  • 11
    • 33750040245 scopus 로고    scopus 로고
    • Antioxidant Dps protein from the thermophilic cyanobacterium Thermosynechococcus elongatus
    • Franceschini S, Ceci P, Alaleona F, Chiancone E, Ilari A. 2006. Antioxidant Dps protein from the thermophilic cyanobacterium Thermosynechococcus elongatus. FEBS J. 273:4913-4928.
    • (2006) FEBS J. , vol.273 , pp. 4913-4928
    • Franceschini, S.1    Ceci, P.2    Alaleona, F.3    Chiancone, E.4    Ilari, A.5
  • 12
    • 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
  • 13
    • 0036968688 scopus 로고    scopus 로고
    • Iron transport: emerging roles in health and disease
    • Goswami T, Rolfs A, Hediger MA. 2002. Iron transport: emerging roles in health and disease. Biochem. Cell Biol. 80:679-689.
    • (2002) Biochem. Cell Biol. , vol.80 , pp. 679-689
    • Goswami, T.1    Rolfs, A.2    Hediger, M.A.3
  • 14
    • 75849150278 scopus 로고    scopus 로고
    • Dps-like proteins: structural and functional insights into a versatile protein family
    • Haikarainen T, Papageorgiou AC. 2010. Dps-like proteins: structural and functional insights into a versatile protein family. Cell. Mol. Life Sci. 67:341-351.
    • (2010) Cell. Mol. Life Sci. , vol.67 , pp. 341-351
    • Haikarainen, T.1    Papageorgiou, A.C.2
  • 15
    • 0842326209 scopus 로고    scopus 로고
    • The ferritin-like Dps protein is required for Salmonella enterica serovar Typhimurium oxidative stress resistance and virulence
    • Halsey TA, Vazquez-Torres A, Gravdahl DJ, Fang FC, Libby SJ. 2004. The ferritin-like Dps protein is required for Salmonella enterica serovar Typhimurium oxidative stress resistance and virulence. Infect. Immun. 72:1155-1158.
    • (2004) Infect. Immun. , vol.72 , pp. 1155-1158
    • Halsey, T.A.1    Vazquez-Torres, A.2    Gravdahl, D.J.3    Fang, F.C.4    Libby, S.J.5
  • 17
    • 0030878285 scopus 로고    scopus 로고
    • 2-enhanced non-toxin gene expression in Bacillus anthracis
    • 2-enhanced non-toxin gene expression in Bacillus anthracis. Infect. Immun. 65:3091-3099.
    • (1997) Infect. Immun. , vol.65 , pp. 3091-3099
    • Hoffmaster, A.R.1    Koehler, T.M.2
  • 18
    • 0242608621 scopus 로고    scopus 로고
    • Pathways of oxidative damage
    • Imlay JA. 2003. Pathways of oxidative damage. Annu. Rev. Microbiol. 57:395-418.
    • (2003) Annu. Rev. Microbiol. , vol.57 , pp. 395-418
    • Imlay, J.A.1
  • 19
    • 0037309086 scopus 로고    scopus 로고
    • The iron-binding protein Dps confers hydrogen peroxide stress resistance to Campylobacter jejuni
    • Ishikawa T, et al. 2003. The iron-binding protein Dps confers hydrogen peroxide stress resistance to Campylobacter jejuni. J. Bacteriol. 185:1010-1017.
    • (2003) J. Bacteriol. , vol.185 , pp. 1010-1017
    • Ishikawa, T.1
  • 20
    • 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. U. S. A. 93:13635-13640.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 13635-13640
    • Keyer, K.1    Imlay, J.A.2
  • 21
    • 0035892992 scopus 로고    scopus 로고
    • Effect of iron chelators on proliferation and iron uptake in hepatoma cells
    • Kicic A, Chua AC, Baker E. 2001. Effect of iron chelators on proliferation and iron uptake in hepatoma cells. Cancer 92:3093-3110.
    • (2001) Cancer , vol.92 , pp. 3093-3110
    • Kicic, A.1    Chua, A.C.2    Baker, E.3
  • 22
    • 0029609363 scopus 로고
    • Identification of the ferroxidase centre of Escherichia coli bacterioferritin
    • Le Brun NE, et al. 1995. Identification of the ferroxidase centre of Escherichia coli bacterioferritin. Biochem. J. 312:385-392.
    • (1995) Biochem. J. , vol.312 , pp. 385-392
    • Le Brun, N.E.1
  • 23
    • 27944471901 scopus 로고    scopus 로고
    • Formation of protein-coated iron minerals
    • Lewin A, Moore GR, Le Brun NE. 2005. Formation of protein-coated iron minerals. Dalton Trans. 22:3597-3610.
    • (2005) Dalton Trans. , vol.22 , pp. 3597-3610
    • Lewin, A.1    Moore, G.R.2    Le Brun, N.E.3
  • 25
    • 0032732998 scopus 로고    scopus 로고
    • Superoxide and iron: partners in crime
    • Liochev SI, Fridovich I. 1999. Superoxide and iron: partners in crime. IUBMB Life 48:157-161.
    • (1999) IUBMB Life , vol.48 , pp. 157-161
    • Liochev, S.I.1    Fridovich, I.2
  • 26
    • 33748878031 scopus 로고    scopus 로고
    • Paired Bacillus anthracis Dps (mini-ferritin) have different reactivities with peroxide
    • Liu X, Kim K, Leighton T, Theil EC. 2006. Paired Bacillus anthracis Dps (mini-ferritin) have different reactivities with peroxide. J. Biol. Chem. 281:27827-27835.
    • (2006) J. Biol. Chem. , vol.281 , pp. 27827-27835
    • Liu, X.1    Kim, K.2    Leighton, T.3    Theil, E.C.4
  • 27
    • 0030811135 scopus 로고    scopus 로고
    • Protection of DNA during oxidative stress by the nonspecific DNA-binding protein Dps
    • Martinez A, Kolter R. 1997. Protection of DNA during oxidative stress by the nonspecific DNA-binding protein Dps. J. Bacteriol. 179:5188-5194.
    • (1997) J. Bacteriol. , vol.179 , pp. 5188-5194
    • Martinez, A.1    Kolter, R.2
  • 28
    • 15844374760 scopus 로고    scopus 로고
    • The Dps-like protein of Listeria monocytogenes promotes stress tolerance and intracellular multiplication in macrophagelike cells
    • Olsen KN, et al. 2005. The Dps-like protein of Listeria monocytogenes promotes stress tolerance and intracellular multiplication in macrophagelike cells. Microbiology 151:925-933.
    • (2005) Microbiology , vol.151 , pp. 925-933
    • Olsen, K.N.1
  • 29
    • 0037177883 scopus 로고    scopus 로고
    • Structure of two iron-binding proteins from Bacillus anthracis
    • Papinutto E, et al. 2002. Structure of two iron-binding proteins from Bacillus anthracis. J. Biol. Chem. 277:15093-15098.
    • (2002) J. Biol. Chem. , vol.277 , pp. 15093-15098
    • Papinutto, E.1
  • 30
    • 34249791184 scopus 로고    scopus 로고
    • The global transcriptional responses of Bacillus anthracis Sterne (34F2) and a ΔsodA1 mutant to paraquat reveal metal iron homeostasis imbalances during endogenous superoxide stress
    • Passalacqua KD, Bergman NH, Lee JY, Sherman DH, Hanna P. 2007. The global transcriptional responses of Bacillus anthracis Sterne (34F2) and a ΔsodA1 mutant to paraquat reveal metal iron homeostasis imbalances during endogenous superoxide stress. J. Bacteriol. 189:3996-4013.
    • (2007) J. Bacteriol. , vol.189 , pp. 3996-4013
    • Passalacqua, K.D.1    Bergman, N.H.2    Lee, J.Y.3    Sherman, D.H.4    Hanna, P.5
  • 31
    • 79960422054 scopus 로고    scopus 로고
    • Combined proteomic and transcriptomic analysis of the response of Bacillus anthracis to oxidative stress
    • Pohl S, et al. 2011. Combined proteomic and transcriptomic analysis of the response of Bacillus anthracis to oxidative stress. Proteomics 11:3036-3055.
    • (2011) Proteomics , vol.11 , pp. 3036-3055
    • Pohl, S.1
  • 32
    • 0035424542 scopus 로고    scopus 로고
    • Immune responses to intracellular bacteria
    • Raupach B, Kaufmann SH. 2001. Immune responses to intracellular bacteria. Curr. Opin. Immunol. 13:417-428.
    • (2001) Curr. Opin. Immunol. , vol.13 , pp. 417-428
    • Raupach, B.1    Kaufmann, S.H.2
  • 33
    • 0038752613 scopus 로고    scopus 로고
    • The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria
    • Read TD, et al. 2003. The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria. Nature 423:81-86.
    • (2003) Nature , vol.423 , pp. 81-86
    • Read, T.D.1
  • 34
    • 77956235777 scopus 로고    scopus 로고
    • Human transferrin confers serum resistance against Bacillus anthracis
    • Rooijakkers SH, et al. 2010. Human transferrin confers serum resistance against Bacillus anthracis. J. Biol. Chem. 285:27609-27613.
    • (2010) J. Biol. Chem. , vol.285 , pp. 27609-27613
    • Rooijakkers, S.H.1
  • 35
    • 33646571157 scopus 로고    scopus 로고
    • Bacillus anthracis multiplication, persistence, and genetic exchange in the rhizosphere of grass plants
    • Saile E, Koehler TM. 2006. Bacillus anthracis multiplication, persistence, and genetic exchange in the rhizosphere of grass plants. Appl. Environ. Microbiol. 72:3168-3174.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 3168-3174
    • Saile, E.1    Koehler, T.M.2
  • 36
    • 0034193362 scopus 로고    scopus 로고
    • The neutrophil-activating protein (HP-NAP) of Helicobacter pylori is a protective antigen and a major virulence factor
    • Satin B, et al. 2000. The neutrophil-activating protein (HP-NAP) of Helicobacter pylori is a protective antigen and a major virulence factor. J. Exp. Med. 191:1467-1476.
    • (2000) J. Exp. Med. , vol.191 , pp. 1467-1476
    • Satin, B.1
  • 37
    • 78650118379 scopus 로고    scopus 로고
    • 2 substrates in reactivity of the diiron catalytic centers
    • 2 substrates in reactivity of the diiron catalytic centers. Biochemistry 49:10516-10525.
    • (2010) Biochemistry , vol.49 , pp. 10516-10525
    • Schwartz, J.K.1
  • 38
    • 17144402211 scopus 로고    scopus 로고
    • The so-called Listeria innocua ferritin is a Dps protein, iron incorporation, detoxification, and DNA protection properties
    • Su M, Cavallo S, Stefanini S, Chiancone E, Chasteen ND. 2005. The so-called Listeria innocua ferritin is a Dps protein, iron incorporation, detoxification, and DNA protection properties. Biochemistry 44:5572-5578.
    • (2005) Biochemistry , vol.44 , pp. 5572-5578
    • Su, M.1    Cavallo, S.2    Stefanini, S.3    Chiancone, E.4    Chasteen, N.D.5
  • 39
    • 51949087233 scopus 로고    scopus 로고
    • An iron-binding protein, Dpr, decreases hydrogen peroxide stress and protects Streptococcus pyogenes against multiple stresses
    • Tsou CC, et al. 2008. An iron-binding protein, Dpr, decreases hydrogen peroxide stress and protects Streptococcus pyogenes against multiple stresses. Infect. Immun. 76:4038-4045.
    • (2008) Infect. Immun. , vol.76 , pp. 4038-4045
    • Tsou, C.C.1
  • 40
    • 84857721565 scopus 로고    scopus 로고
    • Cellular iron distribution in Bacillus anthracis
    • Tu WY, et al. 2012. Cellular iron distribution in Bacillus anthracis. J. Bacteriol. 194:932-940.
    • (2012) J. Bacteriol. , vol.194 , pp. 932-940
    • Tu, W.Y.1
  • 41
    • 33845511105 scopus 로고    scopus 로고
    • Dual roles of Helicobacter pylori NapA in inducing and combating oxidative stress
    • Wang G, Hong Y, Olczak A, Maier SE, Maier RJ. 2006. Dual roles of Helicobacter pylori NapA in inducing and combating oxidative stress. Infect. Immun. 74:6839-6846.
    • (2006) Infect. Immun. , vol.74 , pp. 6839-6846
    • Wang, G.1    Hong, Y.2    Olczak, A.3    Maier, S.E.4    Maier, R.J.5
  • 42
    • 0037008743 scopus 로고    scopus 로고
    • Iron and hydrogen peroxide detoxification properties of DNA-binding protein from starved cells. A ferritin-like DNA-binding protein of Escherichia coli
    • Zhao G, et al. 2002. Iron and hydrogen peroxide detoxification properties of DNA-binding protein from starved cells. A ferritin-like DNA-binding protein of Escherichia coli. J. Biol. Chem. 277:27689-27696.
    • (2002) J. Biol. Chem. , vol.277 , pp. 27689-27696
    • Zhao, G.1


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