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Volumn 241, Issue 1, 1996, Pages 178-185

Differential expression of superoxide dismutases containing Ni and Fe/Zn in Streptomyces coelicolor

Author keywords

Iron zinc; Metal effect; Nickel; Streptomyces coelicolor; Superoxide dismutase

Indexed keywords

IRON; METALLOPROTEIN; NICKEL; SUPEROXIDE DISMUTASE; ZINC;

EID: 0029849183     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0178t.x     Document Type: Article
Times cited : (139)

References (46)
  • 1
    • 0025219013 scopus 로고
    • Characterization of superoxide dismutases purified from either anaerobically maintained or aerated Bacteroides gingivallis
    • Amano, A., Shizukuishi, S., Tamagawa, H., Iwakura, K., Tsunasawa, S. & Tsunemitsu, A. (1990) Characterization of superoxide dismutases purified from either anaerobically maintained or aerated Bacteroides gingivallis, J. Bacteriol. 172, 1457-1463.
    • (1990) J. Bacteriol. , vol.172 , pp. 1457-1463
    • Amano, A.1    Shizukuishi, S.2    Tamagawa, H.3    Iwakura, K.4    Tsunasawa, S.5    Tsunemitsu, A.6
  • 2
    • 3042590839 scopus 로고
    • Nickel in proteins and enzymes
    • Sigel, H., ed. Marcel Dekker, New York
    • Andrews, R. K., Blakeley, R. L. & Zerner, B. (1988) Nickel in proteins and enzymes, in Metal ions in biological systems (Sigel, H., ed.) vol. 23, pp. 165-284, Marcel Dekker, New York.
    • (1988) Metal Ions in Biological Systems , vol.23 , pp. 165-284
    • Andrews, R.K.1    Blakeley, R.L.2    Zerner, B.3
  • 4
    • 0023109533 scopus 로고
    • The primary structure of iron-superoxide dismutase from Photobacterim leiognathi
    • Barra, D., Schininà, M. E., Bannister, W. H., Bannister, J. V. & Bossa, F. (1987) The primary structure of iron-superoxide dismutase from Photobacterim leiognathi, J. Biol. Chem. 262, 1001-1009.
    • (1987) J. Biol. Chem. , vol.262 , pp. 1001-1009
    • Barra, D.1    Schininà, M.E.2    Bannister, W.H.3    Bannister, J.V.4    Bossa, F.5
  • 5
    • 0020685136 scopus 로고
    • Purification and properties of a unique superoxide dismutase from Nocardia asteroides
    • Beaman, B. L., Scates, S. M., Moring, S. E., Deem, R. & Misra, H. P. (1983) Purification and properties of a unique superoxide dismutase from Nocardia asteroides, J. Biol. Chem. 258, 91-96.
    • (1983) J. Biol. Chem. , vol.258 , pp. 91-96
    • Beaman, B.L.1    Scates, S.M.2    Moring, S.E.3    Deem, R.4    Misra, H.P.5
  • 6
    • 0015153416 scopus 로고
    • Superoxide dismutase: Improved assays and an assay applicable to acrylamide gels
    • Beauchamp, C. & Fridovich, I. (1971) Superoxide dismutase: Improved assays and an assay applicable to acrylamide gels, Anal. Biochem. 44, 276-287.
    • (1971) Anal. Biochem. , vol.44 , pp. 276-287
    • Beauchamp, C.1    Fridovich, I.2
  • 7
    • 0028032403 scopus 로고
    • Escherichia coli expresses a copper-and zinc-containing superoxide dismutase
    • Benov, L. T. & Fridovich, I. (1994) Escherichia coli expresses a copper-and zinc-containing superoxide dismutase, J. Biol. Chem. 269, 25 310-25 314.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25310-25314
    • Benov, L.T.1    Fridovich, I.2
  • 8
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein using the principle of protein dye-binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein using the principle of protein dye-binding, Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 9
    • 0019132225 scopus 로고
    • Superoxide dismutase from Bacillus stearothermophilus: Complete amino acid sequence of a manganese enzyme
    • Brock, C. J. & Walker, J. E. (1980) Superoxide dismutase from Bacillus stearothermophilus: Complete amino acid sequence of a manganese enzyme, Biochemistry 19, 2873-2882.
    • (1980) Biochemistry , vol.19 , pp. 2873-2882
    • Brock, C.J.1    Walker, J.E.2
  • 10
    • 0022683672 scopus 로고
    • Isolation of superoxide dismutase mutants in Escherichia coli: Is superoxide dismutase necessary for aerobic life?
    • Carlioz, A. & Touati, D. (1986) Isolation of superoxide dismutase mutants in Escherichia coli: is superoxide dismutase necessary for aerobic life? EMBO J. 5, 623-630.
    • (1986) EMBO J. , vol.5 , pp. 623-630
    • Carlioz, A.1    Touati, D.2
  • 11
    • 0345191247 scopus 로고
    • Isolation and genetic mapping of paraquat-resistant sporulating mutants of Streptomyces coelicolor
    • Chung, H.-J., Kim, H.-J., Park, U. & Roe, J.-H. (1995) Isolation and genetic mapping of paraquat-resistant sporulating mutants of Streptomyces coelicolor, J. Microbiol. 33, 215-221.
    • (1995) J. Microbiol. , vol.33 , pp. 215-221
    • Chung, H.-J.1    Kim, H.-J.2    Park, U.3    Roe, J.-H.4
  • 12
    • 0021351387 scopus 로고
    • A hybrid superoxide dismutase containing both functional iron and manganese
    • Clare, D. A., Blum, J. & Fridovich, I. (1984) A hybrid superoxide dismutase containing both functional iron and manganese, J. Biol. Chem. 259, 5932-5936.
    • (1984) J. Biol. Chem. , vol.259 , pp. 5932-5936
    • Clare, D.A.1    Blum, J.2    Fridovich, I.3
  • 13
    • 0027410196 scopus 로고
    • Interaction of six global transcription regulators in expression of manganese superoxide dismutase in Escherichia coli K-12
    • Compan, I. & Touati, D. (1993) Interaction of six global transcription regulators in expression of manganese superoxide dismutase in Escherichia coli K-12, J. Bacteriol. 175, 1687-1696.
    • (1993) J. Bacteriol. , vol.175 , pp. 1687-1696
    • Compan, I.1    Touati, D.2
  • 14
    • 0344681692 scopus 로고
    • The complete amino acid sequence of manganese-superoxide dismutase from Saccharomyces cerevisiae
    • Ditlow, C., Johanson, J. T., Martin, B. M. & Svendson, I. B. (1984) The complete amino acid sequence of manganese-superoxide dismutase from Saccharomyces cerevisiae, Carlsberg Res. Commun. 47, 87-91.
    • (1984) Carlsberg Res. Commun. , vol.47 , pp. 87-91
    • Ditlow, C.1    Johanson, J.T.2    Martin, B.M.3    Svendson, I.B.4
  • 16
    • 0017760575 scopus 로고
    • Regulation of the synthesis of superoxide dismutase in Escherichia coli
    • Hassan, H. M. & Fridovich, I. (1977) Regulation of the synthesis of superoxide dismutase in Escherichia coli, J. Biol. Chem. 252, 7667-7672.
    • (1977) J. Biol. Chem. , vol.252 , pp. 7667-7672
    • Hassan, H.M.1    Fridovich, I.2
  • 20
    • 0019834273 scopus 로고
    • Isolation and characterization of the iron-containing superoxide dismutase of Methanobacterium bryantii
    • Kirby, T. W., Lancaster, J. R. Jr & Fridovich, I. (1981) Isolation and characterization of the iron-containing superoxide dismutase of Methanobacterium bryantii, Arch. Biochem. Biophys. 210, 140-148.
    • (1981) Arch. Biochem. Biophys. , vol.210 , pp. 140-148
    • Kirby, T.W.1    Lancaster Jr., J.R.2    Fridovich, I.3
  • 21
    • 0027166927 scopus 로고
    • The induction of oxidative enzymes in Streptomyces coelicolor upon hydrogen peroxide treatment
    • Lee, J.-S., Hah, Y. C. & Roe, J.-H. (1993) The induction of oxidative enzymes in Streptomyces coelicolor upon hydrogen peroxide treatment, J. Gen. Microbiol. 139, 1013-1018.
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 1013-1018
    • Lee, J.-S.1    Hah, Y.C.2    Roe, J.-H.3
  • 22
    • 0025768952 scopus 로고
    • Effects of overproduction of superoxide dismutase on the toxicity of paraquat toward Escherichia coli
    • Liochev, S. I. & Fridovich, I. (1991) Effects of overproduction of superoxide dismutase on the toxicity of paraquat toward Escherichia coli, J. Biol. Chem. 266, 8747-8750.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8747-8750
    • Liochev, S.I.1    Fridovich, I.2
  • 23
    • 0001016169 scopus 로고
    • Nickel transport in Alcaligenes eutrophus
    • Lohmeyer, M. & Friedrich, C. G. (1987) Nickel transport in Alcaligenes eutrophus, Arch. Microbiol. 149, 130-135.
    • (1987) Arch. Microbiol. , vol.149 , pp. 130-135
    • Lohmeyer, M.1    Friedrich, C.G.2
  • 24
    • 0023030627 scopus 로고
    • A Streptococcus mutans superoxide dismutase that is active with either manganese or iron as a cofactor
    • Martin, M. E., Byers, B. R., Olson, M. O. J., Salin, M. L., Arceneaux, J. E. L. & Tolbert, C. (1986) A Streptococcus mutans superoxide dismutase that is active with either manganese or iron as a cofactor. J. Biol. Chem. 261, 9361-9367.
    • (1986) J. Biol. Chem. , vol.261 , pp. 9361-9367
    • Martin, M.E.1    Byers, B.R.2    Olson, M.O.J.3    Salin, M.L.4    Arceneaux, J.E.L.5    Tolbert, C.6
  • 25
    • 0022504269 scopus 로고
    • Fffect of the free radicalgenerating herbicide paraquat on the expression of the superoxide dismutase (Sod) genes in maize
    • Matters, G. L. & Scandalios, J. G. (1986) Fffect of the free radicalgenerating herbicide paraquat on the expression of the superoxide dismutase (Sod) genes in maize, Biochem. Biophys. Acta 882, 29-38.
    • (1986) Biochem. Biophys. Acta , vol.882 , pp. 29-38
    • Matters, G.L.1    Scandalios, J.G.2
  • 26
    • 0020356135 scopus 로고
    • Synthesis of either Fe- or Mn-superoxide dismutase with an apparently identical protein moiety by an anaerobic bacterium dependent on the metal supplied
    • Meier, B., Barra, D., Bossa, F., Calabrese, L. & Rotilio, G. (1982) Synthesis of either Fe- or Mn-superoxide dismutase with an apparently identical protein moiety by an anaerobic bacterium dependent on the metal supplied, J. Biol. Chem. 257, 13 977-13 980.
    • (1982) J. Biol. Chem. , vol.257 , pp. 13977-13980
    • Meier, B.1    Barra, D.2    Bossa, F.3    Calabrese, L.4    Rotilio, G.5
  • 27
    • 0017752904 scopus 로고
    • Superoxide dismutase and peroxidase: A positive activity stain applicable to polyacrylamide gel electropherograms
    • Misra, H. P. & Fridovich, I. (1977) Superoxide dismutase and peroxidase: A positive activity stain applicable to polyacrylamide gel electropherograms, Arch. Biochem. Biophys. 183, 511-515.
    • (1977) Arch. Biochem. Biophys. , vol.183 , pp. 511-515
    • Misra, H.P.1    Fridovich, I.2
  • 28
    • 0017849697 scopus 로고
    • Inhibition of superoxide dismutases by azide
    • Misra, H. P. & Fridovich, I. (1978) Inhibition of superoxide dismutases by azide, Arch, Biochem. Biophys. 189, 317-322.
    • (1978) Arch, Biochem. Biophys. , vol.189 , pp. 317-322
    • Misra, H.P.1    Fridovich, I.2
  • 29
    • 0028349368 scopus 로고
    • Rapid viability loss on exposure to air in a superoxide dismutase-deficient mutant of Porphyromonas gingivalis
    • Nakayama, K. (1994) Rapid viability loss on exposure to air in a superoxide dismutase-deficient mutant of Porphyromonas gingivalis, J. Bacteriol. 176, 1939-1943.
    • (1994) J. Bacteriol. , vol.176 , pp. 1939-1943
    • Nakayama, K.1
  • 30
    • 0021924999 scopus 로고
    • Induction of superoxide dismutases in Escherichia coli B by metal chelators
    • Pugh, S. Y. R. & Fridovich, I. (1985) Induction of superoxide dismutases in Escherichia coli B by metal chelators, J. Bacteriol. 162, 196-202.
    • (1985) J. Bacteriol. , vol.162 , pp. 196-202
    • Pugh, S.Y.R.1    Fridovich, I.2
  • 31
    • 0020627128 scopus 로고
    • Positive correlation between superoxide dismutase and resistance to paraquat toxicity in the green alga Chlorella sorokiniana
    • Rabinowitch, H. D., Clare, D. A., Crapo, J. D. & Fridovich, I. (1983) Positive correlation between superoxide dismutase and resistance to paraquat toxicity in the green alga Chlorella sorokiniana, Arch. Biochem. Biophys. 225, 640-648.
    • (1983) Arch. Biochem. Biophys. , vol.225 , pp. 640-648
    • Rabinowitch, H.D.1    Clare, D.A.2    Crapo, J.D.3    Fridovich, I.4
  • 32
    • 0021111688 scopus 로고
    • Properties of purified carbon monoxide dehydrogenase from Clostridium thermoaceticum, a nickel, iron-sulfur protein
    • Ragsdale, S. W., Clark, J. E., Ljungdahl, L. G., Lundie, L. L. & Drake, H. L. (1983) Properties of purified carbon monoxide dehydrogenase from Clostridium thermoaceticum, a nickel, iron-sulfur protein. J. Biol. Chem. 258, 2364-2369.
    • (1983) J. Biol. Chem. , vol.258 , pp. 2364-2369
    • Ragsdale, S.W.1    Clark, J.E.2    Ljungdahl, L.G.3    Lundie, L.L.4    Drake, H.L.5
  • 34
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100kDa
    • Schägger, H. & von Jagow, G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100kDa, Anal. Biochem. 166, 368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 36
    • 0023654270 scopus 로고
    • Superoxide dismutase-rich bacteria: Paradoxical increase in oxidant toxicity
    • Scott, M. D., Meshnick, S. R. & Eaton, J. W. (1987) Superoxide dismutase-rich bacteria: paradoxical increase in oxidant toxicity, J. Biol. Chem. 262, 3640-3645.
    • (1987) J. Biol. Chem. , vol.262 , pp. 3640-3645
    • Scott, M.D.1    Meshnick, S.R.2    Eaton, J.W.3
  • 37
    • 0018411857 scopus 로고
    • Biosynthesis and cellular distribution of the two superoxide dismutases of Dactylium dendroides
    • Shutzman, A. R. & Kosman, D. J. (1979) Biosynthesis and cellular distribution of the two superoxide dismutases of Dactylium dendroides, J. Bacteriol. 137, 313-320.
    • (1979) J. Bacteriol. , vol.137 , pp. 313-320
    • Shutzman, A.R.1    Kosman, D.J.2
  • 38
    • 0018241823 scopus 로고
    • The amino acid sequence of mangano superoxide dismutase from Escherichia coli B
    • Steinman, H. M. (1978) The amino acid sequence of mangano superoxide dismutase from Escherichia coli B, J. Biol. Chem. 253, 8708-8720.
    • (1978) J. Biol. Chem. , vol.253 , pp. 8708-8720
    • Steinman, H.M.1
  • 39
    • 0021827654 scopus 로고
    • Bacteriocuprein superoxide dismutases in pseudomonads
    • Steinman, H. M. (1985) Bacteriocuprein superoxide dismutases in pseudomonads, J. Bacteriol. 162, 1255-1260.
    • (1985) J. Bacteriol. , vol.162 , pp. 1255-1260
    • Steinman, H.M.1
  • 40
    • 0025339960 scopus 로고
    • Copper-zinc superoxide dismutase of Caulobacter crescentus: Cloning, sequencing and mapping of the gene and periplasmic location of the enzyme
    • Steinman, H. M. & Ely, B. (1990) Copper-zinc superoxide dismutase of Caulobacter crescentus: cloning, sequencing and mapping of the gene and periplasmic location of the enzyme. J. Bacteriol. 172, 2901-2910.
    • (1990) J. Bacteriol. , vol.172 , pp. 2901-2910
    • Steinman, H.M.1    Ely, B.2
  • 41
    • 0024415922 scopus 로고
    • Nucleotide and deduced amino acid sequence of Mycobacterium leprae
    • Thangaraj, H. S., Lamb, F. I., Davis, E. O. & Colston, M. J. (1989) Nucleotide and deduced amino acid sequence of Mycobacterium leprae, Nucleic Acids Res. 17, 8378.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 8378
    • Thangaraj, H.S.1    Lamb, F.I.2    Davis, E.O.3    Colston, M.J.4
  • 42
    • 0024021540 scopus 로고
    • Transcriptional and posttranscriptional regulation of manganese superoxide dismutase biosynthesis in Escherichia coli. studied with operon and protein fusions
    • Touati, D. (1988) Transcriptional and posttranscriptional regulation of manganese superoxide dismutase biosynthesis in Escherichia coli. studied with operon and protein fusions, J. Bacteriol. 170, 2511-2520.
    • (1988) J. Bacteriol. , vol.170 , pp. 2511-2520
    • Touati, D.1
  • 43
    • 0002554499 scopus 로고
    • Regulation and protective role of the microbial superoxide dismutases
    • Scandalios, J. G., ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor NY
    • Touati, D. (1992) Regulation and protective role of the microbial superoxide dismutases, in Molecular biology of free radical scavenging systems (Scandalios, J. G., ed.) pp. 231-261, Cold Spring Harbor Laboratory Press, Cold Spring Harbor NY.
    • (1992) Molecular Biology of Free Radical Scavenging Systems , pp. 231-261
    • Touati, D.1
  • 44
    • 0002844137 scopus 로고
    • SOD-like activity of complexes of nickel(II) ion with some biologically important peptides and their novel reactions with hydrogen peroxide
    • Ueda, J., Ozawa, T., Miyazaki, M. & Fujiwara, Y. (1993) SOD-like activity of complexes of nickel(II) ion with some biologically important peptides and their novel reactions with hydrogen peroxide, Inorg. Chim. Acta 214, 29-32.
    • (1993) Inorg. Chim. Acta , vol.214 , pp. 29-32
    • Ueda, J.1    Ozawa, T.2    Miyazaki, M.3    Fujiwara, Y.4
  • 45
    • 0039604509 scopus 로고
    • A yeast mutant lacking mitochondrial manganese-superoxide dismutase is hypersensitive to oxygen
    • van Loon, A. P. G. M., Pesold-Hurt, B. & Schatz, G. (1986) A yeast mutant lacking mitochondrial manganese-superoxide dismutase is hypersensitive to oxygen, Proc. Natl Acad. Sci. USA 83, 3820-3824.
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 3820-3824
    • Van Loon, A.P.G.M.1    Pesold-Hurt, B.2    Schatz, G.3
  • 46
    • 0029778889 scopus 로고    scopus 로고
    • A novel nickel-containing superoxide dismutase from Streptomyces spp
    • Youn, H.-D., Kim, E.-J., Roe, J.-H., Hah, Y. C. & Kang, S.-O. (1996) A novel nickel-containing superoxide dismutase from Streptomyces spp., Biochem. J. 318, 889-896.
    • (1996) Biochem. J. , vol.318 , pp. 889-896
    • Youn, H.-D.1    Kim, E.-J.2    Roe, J.-H.3    Hah, Y.C.4    Kang, S.-O.5


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