메뉴 건너뛰기




Volumn 32, Issue 19, 2004, Pages 5935-5944

DNA condensation and self-aggregation of Escherichia coli Dps are coupled phenomena related to the properties of the N-terminus

Author keywords

[No Author keywords available]

Indexed keywords

DNA BINDING PROTEIN; ESCHERICHIA COLI PROTEIN; LYSINE; OLIGOMER;

EID: 10244243805     PISSN: 03051048     EISSN: None     Source Type: Journal    
DOI: 10.1093/nar/gkh915     Document Type: Article
Times cited : (159)

References (26)
  • 1
    • 0027083350 scopus 로고
    • A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli
    • Almiron,M., Link,A.J., Deirdre,F. 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    Deirdre, F.3    Kolter, R.4
  • 2
    • 0032716841 scopus 로고    scopus 로고
    • Growth phase-dependent variation in protein composition of the Escherichia coli nucleoid
    • Azam,T.A., Iwata,A., Nishimura,A., Ueda,S. and Ishihama,A. (1999) Growth phase-dependent variation in protein composition of the Escherichia coli nucleoid. J. Bacteriol., 181, 6361-6370.
    • (1999) J. Bacteriol. , vol.181 , pp. 6361-6370
    • Azam, T.A.1    Iwata, A.2    Nishimura, A.3    Ueda, S.4    Ishihama, A.5
  • 3
    • 3042660143 scopus 로고    scopus 로고
    • Fundamental structural units of the Escherichia coli nucleoid revealed by atomic force microscopy
    • Kim,J., Yoshimura,S.H., Hizume,K., Ohniwa,R,L., Ishihama,A. and Takeyasu,K. (2004) Fundamental structural units of the Escherichia coli nucleoid revealed by atomic force microscopy. Nucleic Acids Res., 32, 1982-1992.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1982-1992
    • Kim, J.1    Yoshimura, S.H.2    Hizume, K.3    Ohniwa, R.L.4    Ishihama, A.5    Takeyasu, K.6
  • 4
    • 0030811135 scopus 로고    scopus 로고
    • Protection of DNA during oxidative stress by the nonspecific DNA-binding protein Dps
    • Martinez,A. and 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
  • 5
    • 3042662444 scopus 로고    scopus 로고
    • Dps protects cells against multiple stresses during stationary phase
    • Nair,S. and Finkel,S.E. (2004) Dps protects cells against multiple stresses during stationary phase. J. Bacteriol., 186 4192-4198.
    • (2004) J. Bacteriol. , vol.186 , pp. 4192-4198
    • Nair, S.1    Finkel, S.E.2
  • 6
    • 0033823598 scopus 로고    scopus 로고
    • Contribution of dps to acid stress tolerance and oxidative stress tolerance in Escherichia coli O157:H7
    • Choi,S.H., Baumler,D.J. and Kaspar,C.W. (2000) Contribution of dps to acid stress tolerance and oxidative stress tolerance in Escherichia coli O157:H7. Appl. Environ. Microbiol., 66, 3911-3916.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 3911-3916
    • Choi, S.H.1    Baumler, D.J.2    Kaspar, C.W.3
  • 8
  • 10
    • 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
  • 13
    • 0037805747 scopus 로고    scopus 로고
    • The Dps 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
    • 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 cleavage: x-ray crystal structure, iron binding, and hydroxyl-radical scavenging properties. 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
  • 14
    • 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. Nature Struct. Biol., 7, 38-43.
    • (2000) Nature Struct. Biol. , vol.7 , pp. 38-43
    • Ilari, A.1    Stefanini, S.2    Chiancone, E.3    Tsernoglou, D.4
  • 15
    • 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., Ceci,P., Ilari,A., Giangiacomo,L., Laue,T.M., Chiancone,E. and Chasteen,N.D. (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    Ceci, P.2    Ilari, A.3    Giangiacomo, L.4    Laue, T.M.5    Chiancone, E.6    Chasteen, N.D.7
  • 16
    • 0037020069 scopus 로고    scopus 로고
    • Iron incorporation into Escherichia coli Dps gives rise to a ferritin-like microcrystalline core
    • Ilari,A., Ceci,P, Ferrari,D., Rossi,G,L. and Chiancone,E. (2002) Iron incorporation into Escherichia 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.L.4    Chiancone, E.5
  • 17
    • 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., 184, 2931-2939.
    • (2002) J. Bacteriol. , vol.184 , pp. 2931-2939
    • Yamamoto, Y.1    Poole, L.B.2    Hantgan, R.R.3    Kamio, Y.4
  • 18
  • 19
    • 0001096585 scopus 로고
    • pH homeostasis in Escherichia coli: Measurement by 31P nuclear magnetic resonance of methylphosphonate and phosphate
    • Slonczewski,J.L., Rosen,B.P., Alger,J.R. and Macnab,R.M. (1981) pH homeostasis in Escherichia coli: measurement by 31P nuclear magnetic resonance of methylphosphonate and phosphate. Proc. Natl Acad. Sci., 78, 6271-6275.
    • (1981) Proc. Natl. Acad. Sci. , vol.78 , pp. 6271-6275
    • Slonczewski, J.L.1    Rosen, B.P.2    Alger, J.R.3    Macnab, R.M.4
  • 20
    • 0035823820 scopus 로고    scopus 로고
    • Effects of pH on protein association: Modification of the proton-linkage model and experimental verification of the modified model in the case of cytochrome c and plastocyanin
    • Crnogorac,M.M., Ullmann,G.M. and Kostic,N.M. (2001) Effects of pH on protein association: modification of the proton-linkage model and experimental verification of the modified model in the case of cytochrome c and plastocyanin. J. Am. Chem. Soc., 123, 10789-10798.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 10789-10798
    • Crnogorac, M.M.1    Ullmann, G.M.2    Kostic, N.M.3
  • 22
    • 0842326209 scopus 로고    scopus 로고
    • The ferritin-like Dps protein is required for Salmonella enterica serovar Typhimurium oxidative stress resistance and virulence
    • Halsey,T.A., Vazquez-Torres,A., Gravdahl,D.J., Fang,F.C. and Libby,S.J. (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
  • 23
    • 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. (2003) NaPA protects Helicobacter pylori from oxidative stress damage, and its production is influenced by the ferric uptake regulator. J. Med. Microbiol., 6, 461-469.
    • (2003) J. Med. Microbiol. , vol.6 , pp. 461-469
    • Cooksley, C.1    Jenks, P.J.2    Green, A.3    Cockayne, A.4    Logan, R.P.5    Hardie, K.R.6
  • 24
    • 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. (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    Mizunoe, Y.2    Kawabata, S.3    Takade, A.4    Harada, M.5    Wai, S.N.6    Yoshida, S.7
  • 25
    • 0037371197 scopus 로고    scopus 로고
    • Purification, gene cloning, gene expression, and mutants of Dps from the obligate anaerobe Porphyromonas gingivalis
    • Ueshima,J., Shoji,M., Ratnayake,D.B., Abe,K., Yoshida,S., Yamamoto,K. and Nakayama,K. (2003) Purification, gene cloning, gene expression, and mutants of Dps from the obligate anaerobe Porphyromonas gingivalis. Infect. Immun., 71, 1170-1178.
    • (2003) Infect. Immun. , vol.71 , pp. 1170-1178
    • Ueshima, J.1    Shoji, M.2    Ratnayake, D.B.3    Abe, K.4    Yoshida, S.5    Yamamoto, K.6    Nakayama, K.7
  • 26
    • 0037424379 scopus 로고    scopus 로고
    • 2 resistance mediated by Streptococcal Dpr. Demonstration of the functional involvement of the putative ferroxidase center by site-directed mutagenesis in Streptococcus suis
    • 2 resistance mediated by Streptococcal Dpr. Demonstration of the functional involvement of the putative ferroxidase center by site-directed mutagenesis in Streptococcus suis. J. Biol. Chem., 278, 7996-8005.
    • (2003) J. Biol. Chem. , vol.278 , pp. 7996-8005
    • Pulliainen, A.T.1    Haataja, S.2    Kahkonen, S.3    Finne, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.