메뉴 건너뛰기




Volumn 19, Issue 3, 2008, Pages 261-270

Dps proteins, an efficient detoxification and DNA protection machinery in the bacterial response to oxidative stress

Author keywords

DNA protection; DNA binding; Dps proteins; proteins from starred cells

Indexed keywords

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 84867948203     PISSN: 20374631     EISSN: 17200776     Source Type: Journal    
DOI: 10.1007/s12210-008-0018-4     Document Type: Article
Times cited : (14)

References (30)
  • 1
    • 0027083350 scopus 로고
    • A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli
    • 10.1101/gad.6.12b.2646
    • M. Almirón A.J. Link D. Furlong R. Kolter 1992 A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli Genes Dev 6 2646 2554 10.1101/gad.6.12b.2646
    • (1992) Genes Dev , vol.6 , pp. 2646-2554
    • Almirón, M.1    Link, A.J.2    Furlong, D.3    Kolter, R.4
  • 2
    • 0028200484 scopus 로고
    • The dps promoter is activated by OxyR during growth and by IHF and sigma S in stationary phase
    • 10.1111/j.1365-2958.1994.tb00421.x 1:CAS:528:DyaK2cXlvFOnu7g%3D
    • S. Altuvia M. Almirón G. Huisman R. Kolter G. Storz 1994 The dps promoter is activated by OxyR during growth and by IHF and sigma S in stationary phase Mol Microbiol 13 265 272 10.1111/j.1365-2958.1994.tb00421.x 1:CAS:528:DyaK2cXlvFOnu7g%3D
    • (1994) Mol Microbiol , vol.13 , pp. 265-272
    • Altuvia, S.1    Almirón, M.2    Huisman, G.3    Kolter, R.4    Storz, G.5
  • 3
    • 0030811135 scopus 로고    scopus 로고
    • Protection of DNA during oxidative stress by the nonspecific DNA-binding protein Dps
    • 1:CAS:528:DyaK2sXlsVSru70%3D
    • A. Martinez R. Kolter 1997 Protection of DNA during oxidative stress by the nonspecific DNA-binding protein Dps J Bacteriol 179 5188 5194 1:CAS:528:DyaK2sXlsVSru70%3D
    • (1997) J Bacteriol , vol.179 , pp. 5188-5194
    • Martinez, A.1    Kolter, R.2
  • 4
    • 0033168858 scopus 로고    scopus 로고
    • DNA protection by stress-induced biocrystallization
    • 10.1038/21918 1:CAS:528:DyaK1MXksFehsrk%3D
    • S.G. Wolf D. Frenkiel T. Arad S.E. Finkel R. Kolter A. Minsky 1999 DNA protection by stress-induced biocrystallization Nature 400 83 85 10.1038/21918 1:CAS:528:DyaK1MXksFehsrk%3D
    • (1999) Nature , vol.400 , pp. 83-85
    • Wolf, S.G.1    Frenkiel, D.2    Arad, T.3    Finkel, S.E.4    Kolter, R.5    Minsky, A.6
  • 5
    • 0035283138 scopus 로고    scopus 로고
    • Regulated phase transitions of bacterial chromatin: A nonenzymatic pathway for generic DNA protection
    • 10.1093/emboj/20.5.1184 1:CAS:528:DC%2BD3MXhvVemurw%3D
    • D. Frenkiel-Krispin S. Levin-Zaidman E. Shimoni S.G. Wolf E.J. Wachtel T. Arad S.E. Finkel R. Kolter A. Minsky 2001 Regulated phase transitions of bacterial chromatin: a nonenzymatic pathway for generic DNA protection EMBO J 20 1184 1191 10.1093/emboj/20.5.1184 1:CAS:528:DC%2BD3MXhvVemurw%3D
    • (2001) EMBO J , vol.20 , pp. 1184-1191
    • Frenkiel-Krispin, D.1    Levin-Zaidman, S.2    Shimoni, E.3    Wolf, S.G.4    Wachtel, E.J.5    Arad, T.6    Finkel, S.E.7    Kolter, R.8    Minsky, A.9
  • 6
    • 27944471901 scopus 로고    scopus 로고
    • Formation of protein-coated iron minerals
    • 10.1039/b506071k 1:CAS:528:DC%2BD2MXhtFGrtLnI
    • A. Lewin G.R. Moore N.E. Le Brun 2005 Formation of protein-coated iron minerals Dalton Trans 22 3597 3610 10.1039/b506071k 1:CAS:528:DC%2BD2MXhtFGrtLnI
    • (2005) Dalton Trans , vol.22 , pp. 3597-3610
    • Lewin, A.1    Moore, G.R.2    Le Brun, N.E.3
  • 7
    • 0016722499 scopus 로고
    • Structure of horse-spleen apoferritin at 6 Angstrom resolution
    • 10.1038/255653a0 1:CAS:528:DyaE2MXlt1Oks7s%3D
    • R.J. Hoare P.M. Harrison T.G. Hoy 1975 Structure of horse-spleen apoferritin at 6 Angstrom resolution Nature 255 653 654 10.1038/255653a0 1:CAS:528:DyaE2MXlt1Oks7s%3D
    • (1975) Nature , vol.255 , pp. 653-654
    • Hoare, R.J.1    Harrison, P.M.2    Hoy, T.G.3
  • 9
    • 0024576031 scopus 로고
    • Identification of the iron entry channels in apoferritin. Chemical modification and spectroscopic studies
    • 10.1021/bi00427a052 1:CAS:528:DyaL1MXjsFGiuw%3D%3D
    • S. Stefanini A. Desideri P. Vecchini T. Drakenberg E. Chiancone 1989 Identification of the iron entry channels in apoferritin. Chemical modification and spectroscopic studies Biochemistry 28 378 382 10.1021/bi00427a052 1:CAS:528:DyaL1MXjsFGiuw%3D%3D
    • (1989) Biochemistry , vol.28 , pp. 378-382
    • Stefanini, S.1    Desideri, A.2    Vecchini, P.3    Drakenberg, T.4    Chiancone, E.5
  • 10
    • 0031808808 scopus 로고    scopus 로고
    • Calculated electrostatic gradients in recombinant human H-chain ferritin
    • 1:CAS:528:DyaK1cXivFKktL4%3D 10.1002/pro.5560070502
    • T. Douglas D.R. Ripoll 1998 Calculated electrostatic gradients in recombinant human H-chain ferritin Protein Sci 7 1083 1091 1:CAS:528: DyaK1cXivFKktL4%3D 10.1002/pro.5560070502
    • (1998) Protein Sci , vol.7 , pp. 1083-1091
    • Douglas, T.1    Ripoll, D.R.2
  • 11
    • 0031032646 scopus 로고    scopus 로고
    • A novel non-heme iron-binding ferritin related to the DNA-binding proteins of the Dps family in Listeria innocua
    • 10.1074/jbc.272.6.3259 1:CAS:528:DyaK2sXhtFemtL4%3D
    • M. Bozzi G. Mignogna S. Stefanini D. Barra C. Longhi P. Valenti E. Chiancone 1997 A novel non-heme iron-binding ferritin related to the DNA-binding proteins of the Dps family in Listeria innocua J Biol Chem 272 3259 3265 10.1074/jbc.272.6.3259 1:CAS:528:DyaK2sXhtFemtL4%3D
    • (1997) J Biol Chem , vol.272 , pp. 3259-3265
    • Bozzi, M.1    Mignogna, G.2    Stefanini, S.3    Barra, D.4    Longhi, C.5    Valenti, P.6    Chiancone, E.7
  • 12
    • 0033986734 scopus 로고    scopus 로고
    • The dodecameric ferritin from Listeria innocua contains a novel intersubunit iron-binding site
    • 10.1038/71236 1:CAS:528:DC%2BD3cXlsF2ktw%3D%3D
    • A. Ilari S. Stefanini E. Chiancone D. Tsernoglou 2000 The dodecameric ferritin from Listeria innocua contains a novel intersubunit iron-binding site Nat Struct Biol 7 38 43 10.1038/71236 1:CAS:528:DC%2BD3cXlsF2ktw%3D%3D
    • (2000) Nat Struct Biol , vol.7 , pp. 38-43
    • Ilari, A.1    Stefanini, S.2    Chiancone, E.3    Tsernoglou, D.4
  • 13
    • 0037177883 scopus 로고    scopus 로고
    • Structure of two iron-binding proteins from Bacillus anthracis
    • 10.1074/jbc.M112378200 1:CAS:528:DC%2BD38XjslSgtL0%3D
    • E. Papinutto W.G. Dundon N. Pitulis R. Battistutta C. Montecucco G. Zanotti 2002 Structure of two iron-binding proteins from Bacillus anthracis J Biol Chem 277 15093 15098 10.1074/jbc.M112378200 1:CAS:528:DC%2BD38XjslSgtL0%3D
    • (2002) J Biol Chem , vol.277 , pp. 15093-15098
    • Papinutto, E.1    Dundon, W.G.2    Pitulis, N.3    Battistutta, R.4    Montecucco, C.5    Zanotti, G.6
  • 14
    • 4644286770 scopus 로고    scopus 로고
    • Iron-oxo clusters biomineralizing on protein surfaces: Structural analysis of Halobacterium salinarum DpsA in its low-and high-iron states
    • 10.1073/pnas.0401821101 1:CAS:528:DC%2BD2cXotVygtL4%3D
    • K. Zeth S. Offermann L.O. Essen D. Oesterhelt 2004 Iron-oxo clusters biomineralizing on protein surfaces: structural analysis of Halobacterium salinarum DpsA in its low-and high-iron states Proc Natl Acad Sci USA 101 13780 13785 10.1073/pnas.0401821101 1:CAS:528:DC%2BD2cXotVygtL4%3D
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 13780-13785
    • Zeth, K.1    Offermann, S.2    Essen, L.O.3    Oesterhelt, D.4
  • 15
    • 33745909152 scopus 로고    scopus 로고
    • Crystal structure of Dps-1, a functionally distinct Dps protein from Deinococcus radiodurans
    • 10.1016/j.jmb.2006.06.010 1:CAS:528:DC%2BD28XntFSgtLg%3D
    • S.G. Kim G. Bhattacharyya A. Grove Y.H. Lee 2006 Crystal structure of Dps-1, a functionally distinct Dps protein from Deinococcus radiodurans J Mol Biol 361 105 14 10.1016/j.jmb.2006.06.010 1:CAS:528:DC%2BD28XntFSgtLg%3D
    • (2006) J Mol Biol , vol.361 , pp. 105-114
    • Kim, S.G.1    Bhattacharyya, G.2    Grove, A.3    Lee, Y.H.4
  • 16
    • 33748372577 scopus 로고    scopus 로고
    • The crystal structure of Deinococcus radiodurans Dps protein (DR2263) reveals the presence of a novel metal centre in the N terminus
    • 10.1007/s00775-006-0142-5 1:CAS:528:DC%2BD28XptVWrtrk%3D
    • C.V. Romão E.P. Mitchell S. McSweeney 2006 The crystal structure of Deinococcus radiodurans Dps protein (DR2263) reveals the presence of a novel metal centre in the N terminus J Biol Inorg Chem 11 891 902 10.1007/s00775-006- 0142-5 1:CAS:528:DC%2BD28XptVWrtrk%3D
    • (2006) J Biol Inorg Chem , vol.11 , pp. 891-902
    • Romão, C.V.1    Mitchell, E.P.2    McSweeney, S.3
  • 17
    • 34447622836 scopus 로고    scopus 로고
    • The crystal structure of the Dps2 from Deinococcus radiodurans reveals an unusual pore profile with a non-specific metal binding site
    • 10.1016/j.jmb.2006.11.032 1:CAS:528:DC%2BD2sXotlSjt70%3D
    • M.G. Cuypers E.P. Mitchell C.V. Romão S.M. McSweeney 2007 The crystal structure of the Dps2 from Deinococcus radiodurans reveals an unusual pore profile with a non-specific metal binding site J Mol Biol 371 787 799 10.1016/j.jmb.2006.11.032 1:CAS:528:DC%2BD2sXotlSjt70%3D
    • (2007) J Mol Biol , vol.371 , pp. 787-799
    • Cuypers, M.G.1    Mitchell, E.P.2    Romão, C.V.3    McSweeney, S.M.4
  • 18
    • 1842686188 scopus 로고    scopus 로고
    • Crystal structure of Streptococcus suis Dps-like peroxide resistance protein Dpr: Implications for iron incorporation
    • 10.1016/j.jmb.2004.03.009 1:CAS:528:DC%2BD2cXjtVegtbs%3D
    • A. Kauko S. Haataja A.T. Pulliainen J. Finne A.C. Papageorgiou 2004 Crystal structure of Streptococcus suis Dps-like peroxide resistance protein Dpr: implications for iron incorporation J Mol Biol 338 547 558 10.1016/j.jmb.2004.03.009 1:CAS:528:DC%2BD2cXjtVegtbs%3D
    • (2004) J Mol Biol , vol.338 , pp. 547-558
    • Kauko, A.1    Haataja, S.2    Pulliainen, A.T.3    Finne, J.4    Papageorgiou, A.C.5
  • 19
    • 0038291700 scopus 로고    scopus 로고
    • The multi-layered structure of Dps with a novel di-nuclear ferroxidase center
    • 10.1016/S0022-2836(03)00466-2 1:CAS:528:DC%2BD3sXktFGhsLY%3D
    • B. Ren G. Tibbelin T. Kajino O. Asami R. Ladenstein 2003 The multi-layered structure of Dps with a novel di-nuclear ferroxidase center J Mol Biol 329 467 477 10.1016/S0022-2836(03)00466-2 1:CAS:528:DC%2BD3sXktFGhsLY%3D
    • (2003) J Mol Biol , vol.329 , pp. 467-477
    • Ren, B.1    Tibbelin, G.2    Kajino, T.3    Asami, O.4    Ladenstein, R.5
  • 20
    • 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
    • 10.1074/jbc.M202094200 1:CAS:528:DC%2BD38XlvFKgsLc%3D
    • G. Zhao P. Ceci A. Ilari L. Giangiacomo T.M. Laue E. Chiancone N.D. Chasteen 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 10.1074/jbc.M202094200 1:CAS:528:DC%2BD38XlvFKgsLc%3D
    • (2002) J Biol Chem , vol.277 , pp. 27689-27696
    • Zhao, G.1    Ceci, P.2    Ilari, A.3    Giangiacomo, L.4    Laue, T.M.5    Chiancone, E.6    Chasteen, N.D.7
  • 21
    • 17144402211 scopus 로고    scopus 로고
    • The so-called Listeria innocua ferritin is a Dps protein. Iron incorporation, detoxification, and DNA protection properties
    • 10.1021/bi0472705 1:CAS:528:DC%2BD2MXisVyms78%3D
    • M. Su S. Cavallo S. Stefanini E. Chiancone N.D. Chasteen 2005 The so-called Listeria innocua ferritin is a Dps protein. Iron incorporation, detoxification, and DNA protection properties Biochemistry 44 5572 5578 10.1021/bi0472705 1:CAS:528:DC%2BD2MXisVyms78%3D
    • (2005) Biochemistry , vol.44 , pp. 5572-5578
    • Su, M.1    Cavallo, S.2    Stefanini, S.3    Chiancone, E.4    Chasteen, N.D.5
  • 22
    • 33748878031 scopus 로고    scopus 로고
    • Paired Bacillus anthracis Dps (miniferritin) have different reactivities with peroxide
    • 10.1074/jbc.M601398200 1:CAS:528:DC%2BD28XpsFOrt7g%3D
    • X. Liu K. Kim T. Leighton E.C. Theil 2006 Paired Bacillus anthracis Dps (miniferritin) have different reactivities with peroxide J Biol Chem 281 27827 27835 10.1074/jbc.M601398200 1:CAS:528:DC%2BD28XpsFOrt7g%3D
    • (2006) J Biol Chem , vol.281 , pp. 27827-27835
    • Liu, X.1    Kim, K.2    Leighton, T.3    Theil, E.C.4
  • 23
    • 0037020069 scopus 로고    scopus 로고
    • Iron incorporation into Escherichia coli Dps gives rise to a ferritin-like microcrystalline core
    • 10.1074/jbc.M206186200 1:CAS:528:DC%2BD38XnsVejsb8%3D
    • A. Ilari P. Ceci D. Ferrari G.L. Rossi E. Chiancone 2002 Iron incorporation into Escherichia coli Dps gives rise to a ferritin-like microcrystalline core J Biol Chem 277 37619 37623 10.1074/jbc.M206186200 1:CAS:528:DC%2BD38XnsVejsb8%3D
    • (2002) J Biol Chem , vol.277 , pp. 37619-37623
    • Ilari, A.1    Ceci, P.2    Ferrari, D.3    Rossi, G.L.4    Chiancone, E.5
  • 24
    • 0036091613 scopus 로고    scopus 로고
    • An iron-binding protein, Dpr, from Streptococcusmutans prevents iron-dependent hydroxyl radical formation in vitro
    • 10.1128/JB.184.11.2931-2939.2002 1:CAS:528:DC%2BD38XjvVGku7Y%3D
    • Y. Yamamoto L.B. Poole R.R. Hantgan Y. Kamio 2002 An iron-binding protein, Dpr, from Streptococcusmutans prevents iron-dependent hydroxyl radical formation in vitro J Bacteriol 184 2931 2939 10.1128/JB.184.11.2931-2939.2002 1:CAS:528:DC%2BD38XjvVGku7Y%3D
    • (2002) J Bacteriol , vol.184 , pp. 2931-2939
    • Yamamoto, Y.1    Poole, L.B.2    Hantgan, R.R.3    Kamio, Y.4
  • 25
    • 17144367329 scopus 로고    scopus 로고
    • The unusual intersubunit ferroxidase center of Listeria innocua Dps is required for hydrogen peroxide detoxification but not for iron uptake. A study with site-specific mutants
    • 10.1021/bi050005e 1:CAS:528:DC%2BD2MXis1OhsLY%3D
    • A. Ilari M.C. Latella P. Ceci F. Ribacchi M. Su L. Giangiacomo S. Stefanini N.D. Chasteen E. Chiancone 2005 The unusual intersubunit ferroxidase center of Listeria innocua Dps is required for hydrogen peroxide detoxification but not for iron uptake. A study with site-specific mutants Biochemistry 44 5579 87 10.1021/bi050005e 1:CAS:528:DC%2BD2MXis1OhsLY%3D
    • (2005) Biochemistry , vol.44 , pp. 5579-5587
    • Ilari, A.1    Latella, M.C.2    Ceci, P.3    Ribacchi, F.4    Su, M.5    Giangiacomo, L.6    Stefanini, S.7    Chasteen, N.D.8    Chiancone, E.9
  • 26
    • 0031959912 scopus 로고    scopus 로고
    • The crystal structure of Dps, a ferritin homolog that binds and protects DNA
    • 10.1038/nsb0498-294 1:CAS:528:DyaK1cXitlantbk%3D
    • R.A. Grant D.J. Filman S.E. Finkel R. Kolter J.M. Hogle 1998 The crystal structure of Dps, a ferritin homolog that binds and protects DNA Nat Struct Biol 5 294 303 10.1038/nsb0498-294 1:CAS:528:DyaK1cXitlantbk%3D
    • (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
  • 27
    • 10244243805 scopus 로고    scopus 로고
    • DNA condensation and self-aggregation of Escherichia coli Dps are coupled phenomena related to the properties of the N-terminus
    • 10.1093/nar/gkh915 1:CAS:528:DC%2BD2cXhtVSqsrnI
    • P. Ceci S. Cellai E. Falvo C. Rivetti G.L. Rossi E. Chiancone 2004 DNA condensation and self-aggregation of Escherichia coli Dps are coupled phenomena related to the properties of the N-terminus Nucleic Acids Res 32 5935 5944 10.1093/nar/gkh915 1:CAS:528:DC%2BD2cXhtVSqsrnI
    • (2004) Nucleic Acids Res , vol.32 , pp. 5935-5944
    • Ceci, P.1    Cellai, S.2    Falvo, E.3    Rivetti, C.4    Rossi, G.L.5    Chiancone, E.6
  • 28
    • 0037805747 scopus 로고    scopus 로고
    • TheDps protein of Agrobacterium tumefaciens does not bind to DNA but protects it toward oxidative cleavage: X-ray crystal structure, iron binding, and hydroxyl-radical scavenging properties
    • 10.1074/jbc.M302114200 1:CAS:528:DC%2BD3sXktVejs7g%3D
    • P. Ceci A. Ilari E. Falvo E. Chiancone 2003 TheDps protein of Agrobacterium tumefaciens does not bind to DNA but protects it toward oxidative cleavage: X-ray crystal structure, iron binding, and hydroxyl-radical scavenging properties J Biol Chem 278 20319 20326 10.1074/jbc.M302114200 1:CAS:528:DC%2BD3sXktVejs7g%3D
    • (2003) J Biol Chem , vol.278 , pp. 20319-20326
    • Ceci, P.1    Ilari, A.2    Falvo, E.3    Chiancone, E.4
  • 29
    • 0038813712 scopus 로고    scopus 로고
    • Bimodal protection of DNA by Mycobacterium smegmatis DNA-binding protein from stationary phase cells
    • 10.1074/jbc.M208825200 1:CAS:528:DC%2BD3sXhtVKltbw%3D
    • S. Gupta D. Chatterji 2003 Bimodal protection of DNA by Mycobacterium smegmatis DNA-binding protein from stationary phase cells J Biol Chem 278 5235 5241 10.1074/jbc.M208825200 1:CAS:528:DC%2BD3sXhtVKltbw%3D
    • (2003) J Biol Chem , vol.278 , pp. 5235-5241
    • Gupta, S.1    Chatterji, D.2
  • 30
    • 27144476584 scopus 로고    scopus 로고
    • Reassessment of protein stability, DNA binding, and protection of Mycobacterium smegmatis Dps
    • 10.1074/jbc.M502343200 1:CAS:528:DC%2BD2MXhtVyksrbK
    • P. Ceci A. Ilari E. Falvo L. Giangiacomo E. Chiancone 2005 Reassessment of protein stability, DNA binding, and protection of Mycobacterium smegmatis Dps J Biol Chem 280 34776 34785 10.1074/jbc.M502343200 1:CAS:528:DC%2BD2MXhtVyksrbK
    • (2005) J Biol Chem , vol.280 , pp. 34776-34785
    • Ceci, P.1    Ilari, A.2    Falvo, E.3    Giangiacomo, L.4    Chiancone, E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.