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Volumn 300, Issue 4, 2010, Pages 259-264

Oxidative stress and metal ions regulate a ferritin-like gene, dpr, in Streptococcus pyogenes

Author keywords

Dpr in Group A streptococcus; Oxidative stress; PerR regulator

Indexed keywords

FERRIC UPTAKE REGULATOR; FERRITIN; HYDROGEN PEROXIDE; IRON; IRON BINDING PROTEIN; METAL ION; NICKEL; PROTEIN DPR; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG; ZINC;

EID: 77950369167     PISSN: 14384221     EISSN: 16180607     Source Type: Journal    
DOI: 10.1016/j.ijmm.2009.09.002     Document Type: Article
Times cited : (27)

References (41)
  • 2
    • 0027083350 scopus 로고
    • A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli
    • Almiron M., Link A.J., Furlong D., and Kolter R. A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli. Genes Dev. 6 (1992) 2646-2654
    • (1992) Genes Dev. , vol.6 , pp. 2646-2654
    • Almiron, M.1    Link, A.J.2    Furlong, D.3    Kolter, R.4
  • 3
    • 0028200484 scopus 로고
    • The dps promoter is activated by OxyR during growth and by IHF and sigma S in stationary phase
    • Altuvia S., Almiron M., Huisman G., Kolter R., and Storz G. The dps promoter is activated by OxyR during growth and by IHF and sigma S in stationary phase. Mol. Microbiol. 13 (1994) 265-272
    • (1994) Mol. Microbiol. , vol.13 , pp. 265-272
    • Altuvia, S.1    Almiron, M.2    Huisman, G.3    Kolter, R.4    Storz, G.5
  • 4
    • 0030665283 scopus 로고    scopus 로고
    • Expression of a stress- and starvation-induced dps/pexB-homologous gene is controlled by the alternative sigma factor sigma B in Bacillus subtilis
    • Antelmann H., Engelmann S., Schmid R., Sorokin A., Lapidus A., and Hecker M. Expression of a stress- and starvation-induced dps/pexB-homologous gene is controlled by the alternative sigma factor sigma B in Bacillus subtilis. J. Bacteriol. 179 (1997) 7251-7256
    • (1997) J. Bacteriol. , vol.179 , pp. 7251-7256
    • Antelmann, H.1    Engelmann, S.2    Schmid, R.3    Sorokin, A.4    Lapidus, A.5    Hecker, M.6
  • 5
    • 0141482029 scopus 로고    scopus 로고
    • Borrelia oxidative stress response regulator, BosR: a distinctive Zn-dependent transcriptional activator
    • Boylan J.A., Posey J.E., and Gherardini F.C. Borrelia oxidative stress response regulator, BosR: a distinctive Zn-dependent transcriptional activator. Proc. Natl. Acad. Sci. USA 100 (2003) 11684-11689
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 11684-11689
    • Boylan, J.A.1    Posey, J.E.2    Gherardini, F.C.3
  • 6
    • 0034975764 scopus 로고    scopus 로고
    • Iron uptake mechanisms and their regulation in pathogenic bacteria
    • Braun V. Iron uptake mechanisms and their regulation in pathogenic bacteria. Int. J. Med. Microbiol. 291 (2001) 67-79
    • (2001) Int. J. Med. Microbiol. , vol.291 , pp. 67-79
    • Braun, V.1
  • 7
    • 12344298832 scopus 로고    scopus 로고
    • The PerR regulon in peroxide resistance and virulence of Streptococcus pyogenes
    • Brenot A., King K.Y., and Caparon M.G. The PerR regulon in peroxide resistance and virulence of Streptococcus pyogenes. Mol. Microbiol. 55 (2005) 221-234
    • (2005) Mol. Microbiol. , vol.55 , pp. 221-234
    • Brenot, A.1    King, K.Y.2    Caparon, M.G.3
  • 8
    • 0027218065 scopus 로고
    • Metalloregulation in Bacillus subtilis: isolation and characterization of two genes differentially repressed by metal ions
    • Chen L., James L.P., and Helmann J.D. Metalloregulation in Bacillus subtilis: isolation and characterization of two genes differentially repressed by metal ions. J. Bacteriol. 175 (1993) 5428-5437
    • (1993) J. Bacteriol. , vol.175 , pp. 5428-5437
    • Chen, L.1    James, L.P.2    Helmann, J.D.3
  • 9
    • 0029152774 scopus 로고
    • Coordinate regulation of Bacillus subtilis peroxide stress genes by hydrogen peroxide and metal ions
    • Chen L., Keramati L., and Helmann J.D. Coordinate regulation of Bacillus subtilis peroxide stress genes by hydrogen peroxide and metal ions. Proc. Natl. Acad. Sci. USA 92 (1995) 8190-8194
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8190-8194
    • Chen, L.1    Keramati, L.2    Helmann, J.D.3
  • 10
    • 55149094071 scopus 로고    scopus 로고
    • The transcriptional terminator sequences downstream of the covR gene terminate covR/S operon transcription to generate covR monocistronic transcripts in Streptococcus pyogenes
    • Chiang-Ni C., Tsou C.C., Lin Y.S., Chuang W.J., Lin M.T., Liu C.C., and Wu J.J. The transcriptional terminator sequences downstream of the covR gene terminate covR/S operon transcription to generate covR monocistronic transcripts in Streptococcus pyogenes. Gene 427 (2008) 99-103
    • (2008) Gene , vol.427 , pp. 99-103
    • Chiang-Ni, C.1    Tsou, C.C.2    Lin, Y.S.3    Chuang, W.J.4    Lin, M.T.5    Liu, C.C.6    Wu, J.J.7
  • 11
    • 0038434128 scopus 로고    scopus 로고
    • NapA protects Helicobacter pylori from oxidative stress damage, and its production is influenced by the ferric uptake regulator
    • Cooksley C., Jenks P.J., Green A., Cockayne A., Logan R.P., and Hardie K.R. NapA protects Helicobacter pylori from oxidative stress damage, and its production is influenced by the ferric uptake regulator. J. Med. Microbiol. 52 (2003) 461-469
    • (2003) J. Med. Microbiol. , vol.52 , pp. 461-469
    • Cooksley, C.1    Jenks, P.J.2    Green, A.3    Cockayne, A.4    Logan, R.P.5    Hardie, K.R.6
  • 12
    • 2942511333 scopus 로고    scopus 로고
    • CovS inactivates CovR and is required for growth under conditions of general stress in Streptococcus pyogenes
    • Dalton T.L., and Scott J.R. CovS inactivates CovR and is required for growth under conditions of general stress in Streptococcus pyogenes. J. Bacteriol. 186 (2004) 3928-3937
    • (2004) J. Bacteriol. , vol.186 , pp. 3928-3937
    • Dalton, T.L.1    Scott, J.R.2
  • 13
    • 0029846868 scopus 로고    scopus 로고
    • Acquisition of iron from host proteins by the group A streptococcus
    • Eichenbaum Z., Muller E., Morse S.A., and Scott J.R. Acquisition of iron from host proteins by the group A streptococcus. Infect. Immun. 64 (1996) 5428-5429
    • (1996) Infect. Immun. , vol.64 , pp. 5428-5429
    • Eichenbaum, Z.1    Muller, E.2    Morse, S.A.3    Scott, J.R.4
  • 14
    • 40649086144 scopus 로고    scopus 로고
    • Transcription of the Listeria monocytogenes fri gene is growth-phase dependent and is repressed directly by Fur, the ferric uptake regulator
    • Fiorini F., Stefanini S., Valenti P., Chiancone E., and De Biase D. Transcription of the Listeria monocytogenes fri gene is growth-phase dependent and is repressed directly by Fur, the ferric uptake regulator. Gene 410 (2008) 113-121
    • (2008) Gene , vol.410 , pp. 113-121
    • Fiorini, F.1    Stefanini, S.2    Valenti, P.3    Chiancone, E.4    De Biase, D.5
  • 15
    • 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 A.F., Bsat N., and Helmann J.D. Regulation of the Bacillus subtilis fur and perR genes by PerR: not all members of the PerR regulon are peroxide inducible. J. Bacteriol. 184 (2002) 3276-3286
    • (2002) J. Bacteriol. , vol.184 , pp. 3276-3286
    • Fuangthong, M.1    Herbig, A.F.2    Bsat, N.3    Helmann, J.D.4
  • 16
    • 0031959912 scopus 로고    scopus 로고
    • The crystal structure of Dps, a ferritin homolog that binds and protects DNA
    • Grant R.A., Filman D.J., Finkel S.E., Kolter R., and Hogle J.M. The crystal structure of Dps, a ferritin homolog that binds and protects DNA. Nat. Struct. Biol. 5 (1998) 294-303
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 294-303
    • Grant, R.A.1    Filman, D.J.2    Finkel, S.E.3    Kolter, R.4    Hogle, J.M.5
  • 18
    • 27744530244 scopus 로고    scopus 로고
    • ABC transporter FtsABCD of Streptococcus pyogenes mediates uptake of ferric ferrichrome
    • Hanks T.S., Liu M., McClure M.J., and Lei B. ABC transporter FtsABCD of Streptococcus pyogenes mediates uptake of ferric ferrichrome. BMC Microbiol. 5 (2005) 62
    • (2005) BMC Microbiol. , vol.5 , pp. 62
    • Hanks, T.S.1    Liu, M.2    McClure, M.J.3    Lei, B.4
  • 19
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: molecular properties, iron storage function and cellular regulation
    • Harrison P.M., and Arosio P. The ferritins: molecular properties, iron storage function and cellular regulation. Biochim. Biophys. Acta 1275 (1996) 161-203
    • (1996) Biochim. Biophys. Acta , vol.1275 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 20
    • 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 A.F., and Helmann J.D. 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 (2001) 849-859
    • (2001) Mol. Microbiol. , vol.41 , pp. 849-859
    • Herbig, A.F.1    Helmann, J.D.2
  • 21
    • 0035013928 scopus 로고    scopus 로고
    • PerR controls oxidative stress resistance and iron storage proteins and is required for virulence in Staphylococcus aureus
    • Horsburgh M.J., Clements M.O., Crossley H., Ingham E., and Foster S.J. PerR controls oxidative stress resistance and iron storage proteins and is required for virulence in Staphylococcus aureus. Infect. Immun. 69 (2001) 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
  • 22
    • 0037309086 scopus 로고    scopus 로고
    • The iron-binding protein Dps confers hydrogen peroxide stress resistance to Campylobacter jejuni
    • Ishikawa T., Mizunoe Y., Kawabata S., Takade A., Harada M., Wai S.N., and Yoshida S. The iron-binding protein Dps confers hydrogen peroxide stress resistance to Campylobacter jejuni. J. Bacteriol. 185 (2003) 1010-1017
    • (2003) J. Bacteriol. , vol.185 , pp. 1010-1017
    • Ishikawa, T.1    Mizunoe, Y.2    Kawabata, S.3    Takade, A.4    Harada, M.5    Wai, S.N.6    Yoshida, S.7
  • 23
    • 0037407638 scopus 로고    scopus 로고
    • MtsABC is important for manganese and iron transport, oxidative stress resistance, and virulence of Streptococcus pyogenes
    • Janulczyk R., Ricci S., and Bjorck L. MtsABC is important for manganese and iron transport, oxidative stress resistance, and virulence of Streptococcus pyogenes. Infect. Immun. 71 (2003) 2656-2664
    • (2003) Infect. Immun. , vol.71 , pp. 2656-2664
    • Janulczyk, R.1    Ricci, S.2    Bjorck, L.3
  • 24
    • 33646125623 scopus 로고    scopus 로고
    • dps expression in Escherichia coli O157:H7 requires an extended -10 region and is affected by the cAMP receptor protein
    • Jeong K.C., Baumler D.J., and Kaspar C.W. dps expression in Escherichia coli O157:H7 requires an extended -10 region and is affected by the cAMP receptor protein. Biochim. Biophys. Acta 1759 (2006) 51-59
    • (2006) Biochim. Biophys. Acta , vol.1759 , pp. 51-59
    • Jeong, K.C.1    Baumler, D.J.2    Kaspar, C.W.3
  • 25
    • 16644402961 scopus 로고    scopus 로고
    • [The role of iron-regulated genes in microbial pathogenesis.]
    • Kozyrev D.P., and Vasinova N.A. [The role of iron-regulated genes in microbial pathogenesis.]. Tsitologiia 46 (2004) 465-473
    • (2004) Tsitologiia , vol.46 , pp. 465-473
    • Kozyrev, D.P.1    Vasinova, N.A.2
  • 26
    • 0031870998 scopus 로고    scopus 로고
    • Role of streptococcal pyrogenic exotoxin B in the mouse model of group A streptococcal infection
    • Kuo C.F., Wu J.J., Lin K.Y., Tsai P.J., Lee S.C., Jin Y.T., Lei H.Y., and Lin Y.S. Role of streptococcal pyrogenic exotoxin B in the mouse model of group A streptococcal infection. Infect. Immun. 66 (1998) 3931-3935
    • (1998) Infect. Immun. , vol.66 , pp. 3931-3935
    • Kuo, C.F.1    Wu, J.J.2    Lin, K.Y.3    Tsai, P.J.4    Lee, S.C.5    Jin, Y.T.6    Lei, H.Y.7    Lin, Y.S.8
  • 27
    • 33645037891 scopus 로고    scopus 로고
    • 2 by metal-catalysed histidine oxidation
    • 2 by metal-catalysed histidine oxidation. Nature 440 (2006) 363-367
    • (2006) Nature , vol.440 , pp. 363-367
    • Lee, J.W.1    Helmann, J.D.2
  • 28
    • 34248669001 scopus 로고    scopus 로고
    • Functional specialization within the Fur family of metalloregulators
    • Lee J.W., and Helmann J.D. Functional specialization within the Fur family of metalloregulators. Biometals 20 (2007) 485-499
    • (2007) Biometals , vol.20 , pp. 485-499
    • Lee, J.W.1    Helmann, J.D.2
  • 29
    • 23344441114 scopus 로고    scopus 로고
    • Heme transfer from streptococcal cell surface protein Shp to HtsA of transporter HtsABC
    • Liu M., and Lei B. Heme transfer from streptococcal cell surface protein Shp to HtsA of transporter HtsABC. Infect. Immun. 73 (2005) 5086-5092
    • (2005) Infect. Immun. , vol.73 , pp. 5086-5092
    • Liu, M.1    Lei, B.2
  • 31
    • 0036047508 scopus 로고    scopus 로고
    • Regulation of inducible peroxide stress responses
    • Mongkolsuk S., and Helmann J.D. Regulation of inducible peroxide stress responses. Mol. Microbiol. 45 (2002) 9-15
    • (2002) Mol. Microbiol. , vol.45 , pp. 9-15
    • Mongkolsuk, S.1    Helmann, J.D.2
  • 32
    • 27744500176 scopus 로고    scopus 로고
    • The streptococcal iron uptake (Siu) transporter is required for iron uptake and virulence in a zebrafish infection model
    • Montanez G.E., Neely M.N., and Eichenbaum Z. The streptococcal iron uptake (Siu) transporter is required for iron uptake and virulence in a zebrafish infection model. Microbiology (Reading, England) 151 (2005) 3749-3757
    • (2005) Microbiology (Reading, England) , vol.151 , pp. 3749-3757
    • Montanez, G.E.1    Neely, M.N.2    Eichenbaum, Z.3
  • 33
    • 0030956641 scopus 로고    scopus 로고
    • Cell wall anchoring of the Streptococcus pyogenes M6 protein in various lactic acid bacteria
    • Piard J.C., Hautefort I., Fischetti V.A., Ehrlich S.D., Fons M., and Gruss A. Cell wall anchoring of the Streptococcus pyogenes M6 protein in various lactic acid bacteria. J. Bacteriol. 179 (1997) 3068-3072
    • (1997) J. Bacteriol. , vol.179 , pp. 3068-3072
    • Piard, J.C.1    Hautefort, I.2    Fischetti, V.A.3    Ehrlich, S.D.4    Fons, M.5    Gruss, A.6
  • 34
    • 0037151781 scopus 로고    scopus 로고
    • The expression of the dodecameric ferritin in Listeria spp. is induced by iron limitation and stationary growth phase
    • Polidoro M., De Biase D., Montagnini B., Guarrera L., Cavallo S., Valenti P., Stefanini S., and Chiancone E. The expression of the dodecameric ferritin in Listeria spp. is induced by iron limitation and stationary growth phase. Gene 296 (2002) 121-128
    • (2002) Gene , vol.296 , pp. 121-128
    • Polidoro, M.1    De Biase, D.2    Montagnini, B.3    Guarrera, L.4    Cavallo, S.5    Valenti, P.6    Stefanini, S.7    Chiancone, E.8
  • 35
    • 24744440295 scopus 로고    scopus 로고
    • Expression and regulation pattern of ferritin-like DpsA in the archaeon Halobacterium salinarum
    • Reindel S., Schmidt C.L., Anemüller S., and Matzanke B.F. Expression and regulation pattern of ferritin-like DpsA in the archaeon Halobacterium salinarum. Biometals 18 (2005) 387-397
    • (2005) Biometals , vol.18 , pp. 387-397
    • Reindel, S.1    Schmidt, C.L.2    Anemüller, S.3    Matzanke, B.F.4
  • 36
    • 0034044843 scopus 로고    scopus 로고
    • Growth phase and metal-dependent regulation of the dpsA gene in Synechococcus sp. strain PCC 7942, USA
    • Sen A., Dwivedi K., Rice K.A., and Bullerjahn G.S. Growth phase and metal-dependent regulation of the dpsA gene in Synechococcus sp. strain PCC 7942, USA. Arch. Microbiol. 173 (2000) 352-357
    • (2000) Arch. Microbiol. , vol.173 , pp. 352-357
    • Sen, A.1    Dwivedi, K.2    Rice, K.A.3    Bullerjahn, G.S.4
  • 37
    • 4344700535 scopus 로고    scopus 로고
    • The physiological role of ferritin-like compounds in bacteria
    • Smith J.L. The physiological role of ferritin-like compounds in bacteria. Crit. Rev. Microbiol. 30 (2004) 173-185
    • (2004) Crit. Rev. Microbiol. , vol.30 , pp. 173-185
    • Smith, J.L.1
  • 38
    • 33748209079 scopus 로고    scopus 로고
    • Iron and bacterial virulence
    • Sritharan M. Iron and bacterial virulence. Indian J. Med. Microbiol. 24 (2006) 163-164
    • (2006) Indian J. Med. Microbiol. , vol.24 , pp. 163-164
    • Sritharan, M.1
  • 39
    • 51949087233 scopus 로고    scopus 로고
    • An iron-binding protein, Dpr, decreases hydrogen peroxide stress and protects Streptococcus pyogenes against multiple stresses
    • Tsou C.C., Chiang-Ni C., Lin Y.S., Chuang W.J., Lin M.T., Liu C.C., and Wu J.J. An iron-binding protein, Dpr, decreases hydrogen peroxide stress and protects Streptococcus pyogenes against multiple stresses. Infect. Immun. 76 (2008) 4038-4045
    • (2008) Infect. Immun. , vol.76 , pp. 4038-4045
    • Tsou, C.C.1    Chiang-Ni, C.2    Lin, Y.S.3    Chuang, W.J.4    Lin, M.T.5    Liu, C.C.6    Wu, J.J.7


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