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Volumn 57, Issue 4, 2005, Pages 1101-1112

The crystal structures of Lactococcus lactis MG1363 Dps proteins reveal the presence of an N-terminal helix that is required for DNA binding

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CATION; DPS PROTEIN; EDETIC ACID; GLUTAMIC ACID; LYSINE; PROTEIN SUBUNIT; UNCLASSIFIED DRUG;

EID: 23744485146     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2005.04757.x     Document Type: Article
Times cited : (58)

References (46)
  • 1
    • 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. (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
    • 0027967593 scopus 로고
    • A graph-theoretic approach to the identification of 3-dimensional patterns of amino-acid side-chains in protein structures
    • Artymiuk, P.J., Poirette, A.R., Grindley, H.M., Rice, D.W., and Willet, P. (1994) A graph-theoretic approach to the identification of 3-dimensional patterns of amino-acid side-chains in protein structures. J Mol Biol 243: 327-344.
    • (1994) J Mol Biol , vol.243 , pp. 327-344
    • Artymiuk, P.J.1    Poirette, A.R.2    Grindley, H.M.3    Rice, D.W.4    Willet, P.5
  • 3
    • 0032731196 scopus 로고    scopus 로고
    • Twelve species of the nucleoid-associated protein from Escherichia coli
    • Azam, A.A., and Ishihama, A. (1999) Twelve species of the nucleoid-associated protein from Escherichia coli. J Biol Chem 274: 33105-33113.
    • (1999) J Biol Chem , vol.274 , pp. 33105-33113
    • Azam, A.A.1    Ishihama, A.2
  • 4
    • 0028103275 scopus 로고
    • The CCP4 suite - Programs for protein crystallography
    • Bailey, S. (1994) The CCP4 suite - programs for protein crystallography. Acta Crystallogr D50: 760-763.
    • (1994) Acta Crystallogr , vol.D50 , pp. 760-763
    • Bailey, S.1
  • 5
    • 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
    • Bozzi, M., Mignogna, G., Stefanini, S., Barra, D., Longhi, C., Valenti, P., and Chiancone, E. (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.
    • (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
  • 6
    • 0038219647 scopus 로고    scopus 로고
    • Ferritins, iron uptake and storage from the bacterioferritin viewpoint
    • Carrondo, M.A. (2003) Ferritins, iron uptake and storage from the bacterioferritin viewpoint. EMBO J 22: 1959-1968.
    • (2003) EMBO J , vol.22 , pp. 1959-1968
    • Carrondo, M.A.1
  • 7
    • 0037805747 scopus 로고    scopus 로고
    • The Dps protein of Agrobacterium tumefaciens does not bind to DNA but protects it toward oxidative damage
    • Ceci, P., Ilari, A., Falvo, E., and Chiancone, E. (2003) The Dps protein of Agrobacterium tumefaciens does not bind to DNA but protects it toward oxidative damage. J Biol Chem 278: 20319-20326.
    • (2003) J Biol Chem , vol.278 , pp. 20319-20326
    • Ceci, P.1    Ilari, A.2    Falvo, E.3    Chiancone, E.4
  • 8
    • 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
    • Ceci, P., Cellai, S., Falvo, E., Rivetti, C., Rossi, G.L., and Chiancone, E. (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.
    • (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
  • 9
    • 0033617958 scopus 로고    scopus 로고
    • Mineralization in ferritin: An efficient means of iron storage
    • Chasteen, N.D., and Harrison, P.M. (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
  • 10
    • 0028861959 scopus 로고
    • Bacillus subtilis MrgA is a Dps (PexB) homologue: Evidence for metalloregulation of an oxidative-stress gene
    • Chen, L., and Helmann, J.D. (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
  • 13
    • 0035283138 scopus 로고    scopus 로고
    • Regulated phase transitions of bacterial chromatin: A non-enzymatic pathway for generic DNA protection
    • Frenkiel-Krispin, D., Levin-Zaidman, S., Shimoni, E., Wolf, S.G., Wachtel, E.J., Arad, T., et al. (2001) Regulated phase transitions of bacterial chromatin: a non-enzymatic pathway for generic DNA protection. EMBO J 20:1184-1191.
    • (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
  • 15
    • 0031882182 scopus 로고    scopus 로고
    • A novel regulatory switch mediated by the FNR-like protein of Lactobacillus casei
    • Gostick, D.O., Green, J., Irvine, A.S., Gasson, M.J., and Guest, J.R. (1998) A novel regulatory switch mediated by the FNR-like protein of Lactobacillus casei. Microbiology 144:705-717.
    • (1998) Microbiology , vol.144 , pp. 705-717
    • Gostick, D.O.1    Green, J.2    Irvine, A.S.3    Gasson, M.J.4    Guest, J.R.5
  • 17
    • 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. (1998) The crystal structure of Dps, a ferritin homolog that binds and protects DNA. Nat Struc Biol 5: 294-303.
    • (1998) Nat Struc 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
    • 0034982114 scopus 로고    scopus 로고
    • Functional versatility in the CRP-FNR superfamily of transcription factors: FNR and FLP
    • Green, J., Scott, C., and Guest, J.R. (2001) Functional versatility in the CRP-FNR superfamily of transcription factors: FNR and FLP. Adv Microbial Physiol 144: 1-34.
    • (2001) Adv Microbial Physiol , vol.144 , pp. 1-34
    • Green, J.1    Scott, C.2    Guest, J.R.3
  • 19
    • 0038813712 scopus 로고    scopus 로고
    • Bimodal protection of DNA by Mycobacterium smegmatis DNA binding protein from stationary phase cells
    • Gupta, S., and Chatterji, D. (2003) Bimodal protection of DNA by Mycobacterium smegmatis DNA binding protein from stationary phase cells. J Biol Chem 278: 5235-5241.
    • (2003) J Biol Chem , vol.278 , pp. 5235-5241
    • Gupta, S.1    Chatterji, D.2
  • 20
    • 0025370786 scopus 로고
    • Superoxide dismutase and Fenton chemistry. Reaction of ferric-EDTA complex and ferric-bipyridyl complex with hydrogen peroxide without the apparent formation of iron (II)
    • Gutteridge, J.M., Maidt, L., and Poyer, L. (1990) Superoxide dismutase and Fenton chemistry. Reaction of ferric-EDTA complex and ferric-bipyridyl complex with hydrogen peroxide without the apparent formation of iron (II). Biochem J 269: 169-174.
    • (1990) Biochem J , vol.269 , pp. 169-174
    • Gutteridge, J.M.1    Maidt, L.2    Poyer, L.3
  • 21
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: Molecular properties, iron storage and cellular regulation
    • Harrison, P.M., and Arosio, P. (1996) The ferritins: molecular properties, iron storage and cellular regulation. Biochim Biophys Acta 1275: 161-203.
    • (1996) Biochim Biophys Acta , vol.1275 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 22
    • 0033986734 scopus 로고    scopus 로고
    • The dodecameric ferritin from Listeria innocua contains a novel intersubunit iron-binding site
    • Ilari, A., Stefanini, S., Chiancone, E., and Tsernoglou, D. (2000) The dodecameric ferritin from Listeria innocua contains a novel intersubunit iron-binding site. Nat Struc Biol 7: 38-43.
    • (2000) Nat Struc Biol , vol.7 , pp. 38-43
    • Ilari, A.1    Stefanini, S.2    Chiancone, E.3    Tsernoglou, D.4
  • 23
    • 0037020069 scopus 로고    scopus 로고
    • Iron incorporation in E. coli Dps gives rise to a ferritin-like microcrystalline core
    • Ilari, A., Ceci, P., Ferrari, D., Rossi, G., and Chiancone, E. (2002) Iron incorporation in E. coli Dps gives rise to a ferritin-like microcrystalline core. J Biol Chem 277: 37619-37623.
    • (2002) J Biol Chem , vol.277 , pp. 37619-37623
    • Ilari, A.1    Ceci, P.2    Ferrari, D.3    Rossi, G.4    Chiancone, E.5
  • 24
    • 0037309086 scopus 로고    scopus 로고
    • The iron-binding protein Dps confers hydrogen peroxide resistance to Campylobacter jejuni
    • Ishikawa, T., Mizunoe, Y., Kawabata, S., Takade, A., Harada, M., Wai, S.N., and Yoshida, S. (2003) The iron-binding protein Dps confers hydrogen peroxide resistance to Campylobacter jejuni. J Bacteriol 185: 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
  • 25
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position specific scoring matrices
    • Jones, D.T. (1999) Protein secondary structure prediction based on position specific scoring matrices. J Mol Biol 292: 152-202.
    • (1999) J Mol Biol , vol.292 , pp. 152-202
    • Jones, D.T.1
  • 26
    • 1842686188 scopus 로고    scopus 로고
    • Crystal structure of Streptococcus suis dps-like peroxide resistance protein Dpr: Implications for iron incorporation
    • Kauko, A., Haataja, S., Pulliainen, A.T., Finne, J., and Papageorgiou, A.C. (2004) Crystal structure of Streptococcus suis dps-like peroxide resistance protein Dpr: Implications for iron incorporation. J Mol Biol 338: 547-558.
    • (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
  • 28
    • 0030811135 scopus 로고    scopus 로고
    • Protection of DNA during oxidative stress by the non-specific DNA binding protein Dps
    • Martinez, A., and Kolter, R. (1997) Protection of DNA during oxidative stress by the non-specific DNA binding protein Dps. J Bacteriol 179: 5188-5194.
    • (1997) J Bacteriol , vol.179 , pp. 5188-5194
    • Martinez, A.1    Kolter, R.2
  • 31
    • 0038291700 scopus 로고    scopus 로고
    • The multi-layered structure of Dps with a novel di-nuclear ferroxidase center
    • Ren, B., Tibbelin, G., Kajino, T., Asami, O., and Ladenstein, R. (2003) The multi-layered structure of Dps with a novel di-nuclear ferroxidase center. J Mol Biol 329: 467-477.
    • (2003) J Mol Biol , vol.329 , pp. 467-477
    • Ren, B.1    Tibbelin, G.2    Kajino, T.3    Asami, O.4    Ladenstein, R.5
  • 33
    • 3042582299 scopus 로고    scopus 로고
    • X-ray analysis of Mycobacterium smegmatis Dps and a comparative study involving other Dps and Dps-like molecules
    • Roy, S., Gupta, S., Das, S., Sekar, K., Chatterji, D., and Vijayan, M. (2004) X-ray analysis of Mycobacterium smegmatis Dps and a comparative study involving other Dps and Dps-like molecules. J Mol Biol 339: 1103-1113.
    • (2004) J Mol Biol , vol.339 , pp. 1103-1113
    • Roy, S.1    Gupta, S.2    Das, S.3    Sekar, K.4    Chatterji, D.5    Vijayan, M.6
  • 34
    • 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., Del Giudice, G., Della Bianca, V., Dusi, S., Laudanna, C., Tonello, F., 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    Del Giudice, G.2    Della Bianca, V.3    Dusi, S.4    Laudanna, C.5    Tonello, F.6
  • 36
    • 0034071872 scopus 로고    scopus 로고
    • Characterization of the Lactococcus lactis transcription factor FlpA and demonstration of an in vitro switch
    • Scott, C., Guest, J.R., and Green, J. (2000b) Characterization of the Lactococcus lactis transcription factor FlpA and demonstration of an in vitro switch. Mol Microbiol 35: 1383-1393.
    • (2000) Mol Microbiol , vol.35 , pp. 1383-1393
    • Scott, C.1    Guest, J.R.2    Green, J.3
  • 37
    • 0033558219 scopus 로고    scopus 로고
    • Incorporation of iron by the unusual dodecameric ferritin from Listeria innocua
    • Steffanini, S., Cavallo, S., Montagnini, B., and Chianicone, E. (1999) Incorporation of iron by the unusual dodecameric ferritin from Listeria innocua. Biochem J 338: 71-75.
    • (1999) Biochem J , vol.338 , pp. 71-75
    • Steffanini, S.1    Cavallo, S.2    Montagnini, B.3    Chianicone, E.4
  • 39
    • 0002463721 scopus 로고    scopus 로고
    • Oxidative stress
    • Storz, G., and Hengge-Aronis, R. (eds). Washington, DC: American Society for Microbiology Press
    • Storz, G., and Zheng, M. (2000) Oxidative stress. In Bacterial Stress Responses. Storz, G., and Hengge-Aronis, R. (eds). Washington, DC: American Society for Microbiology Press, pp. 47-59.
    • (2000) Bacterial Stress Responses , pp. 47-59
    • Storz, G.1    Zheng, M.2
  • 40
    • 0001413894 scopus 로고    scopus 로고
    • The Helicobacter pylori neutrophil-activating protein is an iron-binding protein with dodecameric structure
    • Tonello, F., Dundon, W.G., Satin, B., Molinari, M., Tognon, G., Grandi, G. et al. (1999) The Helicobacter pylori neutrophil-activating protein is an iron-binding protein with dodecameric structure. Mol Microbiol 34: 238-246.
    • (1999) Mol Microbiol , vol.34 , pp. 238-246
    • Tonello, F.1    Dundon, W.G.2    Satin, B.3    Molinari, M.4    Tognon, G.5    Grandi, G.6
  • 41
    • 0030757720 scopus 로고    scopus 로고
    • TNT refinement package
    • Tronrud, D.E. (1997) TNT refinement package. Meth Enzymol 277: 306-319.
    • (1997) Meth Enzymol , vol.277 , pp. 306-319
    • Tronrud, D.E.1
  • 43
    • 0036091613 scopus 로고    scopus 로고
    • An iron-binding protein, Dpr, from Streptococcus mutans prevents iron-dependent hydroxyl radical formation in vitro
    • Yamamoto, Y., Poole, L.B., Hantgan, R.R., and Kamio, Y. (2002) An iron-binding protein, Dpr, from Streptococcus mutans prevents iron-dependent hydroxyl radical formation in vitro. J Bacteriol 194: 2931-2939.
    • (2002) J Bacteriol , vol.194 , pp. 2931-2939
    • Yamamoto, Y.1    Poole, L.B.2    Hantgan, R.R.3    Kamio, Y.4
  • 45
    • 0037008743 scopus 로고    scopus 로고
    • Iron and hydrogen peroxide detoxification properties of DNA binding protein from starved cells
    • Zhao, G., Ceci, P., Ilari, A., Giangiacomo, L., Laua, T.M., Chiancone, E., and Chasteen, N.D. (2002) Iron and hydrogen peroxide detoxification properties of DNA binding protein from starved cells. J Biol Chem 277: 27689-27696.
    • (2002) J Biol Chem , vol.277 , pp. 27689-27696
    • Zhao, G.1    Ceci, P.2    Ilari, A.3    Giangiacomo, L.4    Laua, T.M.5    Chiancone, E.6    Chasteen, N.D.7
  • 46
    • 0034932337 scopus 로고    scopus 로고
    • DNA microarray-mediated transcriptional profiling of the Escherichia coli response to hydrogen peroxide
    • Zheng, M., Wang, X., Templeton, L.J., Smulski, D.R., Larossa, R.A., and Storz, G. (2001) DNA microarray-mediated transcriptional profiling of the Escherichia coli response to hydrogen peroxide. J Bacteriol 183: 4562-4570.
    • (2001) J Bacteriol , vol.183 , pp. 4562-4570
    • Zheng, M.1    Wang, X.2    Templeton, L.J.3    Smulski, D.R.4    Larossa, R.A.5    Storz, G.6


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