메뉴 건너뛰기




Volumn 106, Issue 1, 2000, Pages 121-129

Molecular cloning, expression analysis and iron metal cofactor characterisation of a superoxide dismutase from Toxoplasma gondii

Author keywords

Gene cloning; Iron superoxide dismutase; Protein expression; Toxoplasma gondii

Indexed keywords

IRON; METAL; SUPEROXIDE DISMUTASE;

EID: 0343048402     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0166-6851(99)00211-X     Document Type: Article
Times cited : (33)

References (35)
  • 1
    • 0026494366 scopus 로고
    • Microbial strategies to prevent oxygen-dependent killing by phagocytes
    • Haas A., Goebel W. Microbial strategies to prevent oxygen-dependent killing by phagocytes. Free Rad Res Commun. 16:1991;137-157.
    • (1991) Free Rad Res Commun , vol.16 , pp. 137-157
    • Haas, A.1    Goebel, W.2
  • 2
    • 0031029702 scopus 로고    scopus 로고
    • Role of oxydants in microbial pathophysiology
    • Miller R.A., Britigan B.E. Role of oxydants in microbial pathophysiology. Clin Microbiol Rev. 10:1997;1-18.
    • (1997) Clin Microbiol Rev , vol.10 , pp. 1-18
    • Miller, R.A.1    Britigan, B.E.2
  • 3
    • 0022480378 scopus 로고
    • Superoxide dismutases
    • Fridovich I. Superoxide dismutases. Adv Enzymol. 58:1986;62-97.
    • (1986) Adv Enzymol , vol.58 , pp. 62-97
    • Fridovich, I.1
  • 4
    • 0024330563 scopus 로고
    • Microbial superoxide dismutases
    • Hassan H.M. Microbial superoxide dismutases. Adv in Genet. 26:1989;65-97.
    • (1989) Adv in Genet , vol.26 , pp. 65-97
    • Hassan, H.M.1
  • 5
    • 0000583813 scopus 로고    scopus 로고
    • Superoxide dismutases in bacteria and pathogen protists
    • Cold Spring Harbor Laboratory Press
    • Touati D. Superoxide dismutases in bacteria and pathogen protists. Oxidative Stress and Molecular Biology of Antioxidant Defenses. 1997;447-482 Cold Spring Harbor Laboratory Press.
    • (1997) Oxidative Stress and Molecular Biology of Antioxidant Defenses , pp. 447-482
    • Touati, D.1
  • 6
    • 0022426858 scopus 로고
    • Purification and characterization of an iron containing superoxide dismutase from eukaryote
    • Duke M.V., Salin M.L. Purification and characterization of an iron containing superoxide dismutase from eukaryote. Arch Biochem Biophys. 243:1985;305-314.
    • (1985) Arch Biochem Biophys , vol.243 , pp. 305-314
    • Duke, M.V.1    Salin, M.L.2
  • 7
    • 0028236403 scopus 로고
    • Genetic, enzymatic, and pathogenic studies of the iron superoxide dismutase of Campylobacter jejuni
    • Pesci E.C., Cottle D.L., Pickett C.L. Genetic, enzymatic, and pathogenic studies of the iron superoxide dismutase of Campylobacter jejuni. Infect Immun. 62:1994;2687-2694.
    • (1994) Infect Immun , vol.62 , pp. 2687-2694
    • Pesci, E.C.1    Cottle, D.L.2    Pickett, C.L.3
  • 8
    • 0030900746 scopus 로고    scopus 로고
    • Protection against murine listeriosis by an attenuated recombinant Salmonella typhimurium vaccine strain that secretes the naturally somatic antigen superoxide dismutase
    • Hess J., Dietrich G., Gentschev I., Miko D., Goebel W., Kaufmann S.H.E. Protection against murine listeriosis by an attenuated recombinant Salmonella typhimurium vaccine strain that secretes the naturally somatic antigen superoxide dismutase. Infect Immun. 65:1997;1286-1292.
    • (1997) Infect Immun , vol.65 , pp. 1286-1292
    • Hess, J.1    Dietrich, G.2    Gentschev, I.3    Miko, D.4    Goebel, W.5    Kaufmann, S.H.E.6
  • 9
    • 0033056490 scopus 로고    scopus 로고
    • Characterization of the major superoxide dismutase of Staphylococcus aureus and its role in starvation survival, stress resistance, and pathogenicity
    • Clements M.O., Watson S.P., Foster S.J. Characterization of the major superoxide dismutase of Staphylococcus aureus and its role in starvation survival, stress resistance, and pathogenicity. J Bacteriol. 181:1999;3898-3903.
    • (1999) J Bacteriol , vol.181 , pp. 3898-3903
    • Clements, M.O.1    Watson, S.P.2    Foster, S.J.3
  • 10
    • 0030997726 scopus 로고    scopus 로고
    • Molecular cloning and characterization of two iron superoxide dismutase cDNAs from Trypanosoma cruzi
    • Ismail S.O., Paramchuk W., Skeiky Y.A.W., Reed S.G., Bathia A., Gedamu L. Molecular cloning and characterization of two iron superoxide dismutase cDNAs from Trypanosoma cruzi. Mol Biochem Parasitol. 86:1997;187-197.
    • (1997) Mol Biochem Parasitol , vol.86 , pp. 187-197
    • Ismail, S.O.1    Paramchuk, W.2    Skeiky, Y.A.W.3    Reed, S.G.4    Bathia, A.5    Gedamu, L.6
  • 11
    • 0031455412 scopus 로고    scopus 로고
    • Cloning, characterization and overexpression of two iron superoxide dismutase cDNAs from Leishmania chagasi: Role in pathogenesis
    • Paramchuk W., Ismail S.O., Bathia A., Gedamu L. Cloning, characterization and overexpression of two iron superoxide dismutase cDNAs from Leishmania chagasi: role in pathogenesis. Mol Biochem Parasitol. 90:1997;203-221.
    • (1997) Mol Biochem Parasitol , vol.90 , pp. 203-221
    • Paramchuk, W.1    Ismail, S.O.2    Bathia, A.3    Gedamu, L.4
  • 12
    • 0030848721 scopus 로고    scopus 로고
    • Identification of a neutrophil chemotactic factor from Tritrichomonas foetus as superoxide dismutase
    • Granger B.L., Warwood S.J., Hayai N., Hayashi H., Owhashi M. Identification of a neutrophil chemotactic factor from Tritrichomonas foetus as superoxide dismutase. Mol Biochem Parasitol. 89:1997;85-95.
    • (1997) Mol Biochem Parasitol , vol.89 , pp. 85-95
    • Granger, B.L.1    Warwood, S.J.2    Hayai, N.3    Hayashi, H.4    Owhashi, M.5
  • 13
    • 0022457433 scopus 로고
    • Superoxide dismutase and catalase in Toxoplasma gondii
    • Sibley L.D., Lawson R., Weidner E. Superoxide dismutase and catalase in Toxoplasma gondii. Mol Biochem Parasitol. 19:1986;83-87.
    • (1986) Mol Biochem Parasitol , vol.19 , pp. 83-87
    • Sibley, L.D.1    Lawson, R.2    Weidner, E.3
  • 15
    • 0027244093 scopus 로고
    • Presence of an endogenous superoxide dismutase activity in three rodent malaria species
    • Bécuwe P., Slomianny C., Camus D., Dive D. Presence of an endogenous superoxide dismutase activity in three rodent malaria species. Parasitol Res. 79:1993;349-352.
    • (1993) Parasitol Res , vol.79 , pp. 349-352
    • Bécuwe, P.1    Slomianny, C.2    Camus, D.3    Dive, D.4
  • 17
    • 84887357069 scopus 로고
    • Toxoplasmic encephalitis in children
    • Sabin A. Toxoplasmic encephalitis in children. JAMA. 116:1941;801-814.
    • (1941) JAMA , vol.116 , pp. 801-814
    • Sabin, A.1
  • 18
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucl Acids Res. 22:1994;4673-4680.
    • (1994) Nucl Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 19
    • 0028933323 scopus 로고
    • Structure-function in Escherichia coli iron superoxide dismutase: Comparisons with the manganese enzyme from Thermus thermophilus
    • Lah M.S., Dixon M.M., Pattridge K.A., Stallings W.C., Fee J.A., Ludwig M.L. Structure-function in Escherichia coli iron superoxide dismutase: comparisons with the manganese enzyme from Thermus thermophilus. Biochemistry. 34:1995;1646-1660.
    • (1995) Biochemistry , vol.34 , pp. 1646-1660
    • Lah, M.S.1    Dixon, M.M.2    Pattridge, K.A.3    Stallings, W.C.4    Fee, J.A.5    Ludwig, M.L.6
  • 20
    • 0032915435 scopus 로고    scopus 로고
    • Isolation and characterization of a substractive library enriched for developmentally regulated transcripts expressed during encystation of Toxoplasma gondii
    • Yahiaoui B., Dzierszinski F., Bernigaud A., Slomianny C., Camus D., Tomavo S. Isolation and characterization of a substractive library enriched for developmentally regulated transcripts expressed during encystation of Toxoplasma gondii. Mol Biochem Parasitol. 99:1999;223-235.
    • (1999) Mol Biochem Parasitol , vol.99 , pp. 223-235
    • Yahiaoui, B.1    Dzierszinski, F.2    Bernigaud, A.3    Slomianny, C.4    Camus, D.5    Tomavo, S.6
  • 22
    • 26444574092 scopus 로고
    • Expression using the T7 RNA polymerase/promoter system
    • F.M. et al. Ausubel. New York: Greene Publishing and Wiley-Interscience. 16.2.1-16.2.11
    • Tabor S. Expression using the T7 RNA polymerase/promoter system. Ausubel F.M. et al. Current Protocols in Molecular Biology. 1990;16 Greene Publishing and Wiley-Interscience, New York. 16.2.1-16.2.11.
    • (1990) Current Protocols in Molecular Biology , pp. 16
    • Tabor, S.1
  • 23
    • 0016272750 scopus 로고
    • Involvement of the superoxide anion radical in the autoxidation of pyrogallol and a convenient assay for superoxide dismutase
    • Marklund S., Marklund G. Involvement of the superoxide anion radical in the autoxidation of pyrogallol and a convenient assay for superoxide dismutase. Eur J Biochem. 47:1974;469-474.
    • (1974) Eur J Biochem , vol.47 , pp. 469-474
    • Marklund, S.1    Marklund, G.2
  • 24
    • 0019363396 scopus 로고
    • Organization and expression of eukaryotic split genes coding for proteins
    • Breathnach R., Chambon P. Organization and expression of eukaryotic split genes coding for proteins. Ann Rev Biochem. 50:1981;349-383.
    • (1981) Ann Rev Biochem , vol.50 , pp. 349-383
    • Breathnach, R.1    Chambon, P.2
  • 25
    • 0022552131 scopus 로고
    • Point mutations define a sequence flanking the AUG initiatior codon that modulates translation by eukaryotic ribosomes
    • Kozak M. Point mutations define a sequence flanking the AUG initiatior codon that modulates translation by eukaryotic ribosomes. Cell. 44:1986;283-292.
    • (1986) Cell , vol.44 , pp. 283-292
    • Kozak, M.1
  • 26
    • 0028211397 scopus 로고
    • Homologous recombination and gene replacement at the dihydrofolate reductase-thymidylate synthase locus in Toxoplasma gondii
    • Donald R.G.K., Roos D.S. Homologous recombination and gene replacement at the dihydrofolate reductase-thymidylate synthase locus in Toxoplasma gondii. Mol Biochem Biol. 63:1994;243-253.
    • (1994) Mol Biochem Biol , vol.63 , pp. 243-253
    • Donald, R.G.K.1    Roos, D.S.2
  • 27
    • 0028054245 scopus 로고
    • Induction of the iron-containing superoxide dismutase in Entamoeba histolytica by a superoxide anion-generating system or by iron chelation
    • Bruchhaus I., Tannich E. Induction of the iron-containing superoxide dismutase in Entamoeba histolytica by a superoxide anion-generating system or by iron chelation. Mol Biochem Parasitol. 67:1994;281-288.
    • (1994) Mol Biochem Parasitol , vol.67 , pp. 281-288
    • Bruchhaus, I.1    Tannich, E.2
  • 28
    • 0024292275 scopus 로고
    • Crystal structure of maganese superoxide dismutase from Bacillus stearothermophilus at 2.4 A resolution
    • Parker M.W., Blake C.C.F. Crystal structure of maganese superoxide dismutase from Bacillus stearothermophilus at 2.4 A resolution. J Mol Biol. 199:1988;649-661.
    • (1988) J Mol Biol , vol.199 , pp. 649-661
    • Parker, M.W.1    Blake, C.C.F.2
  • 29
    • 0025196784 scopus 로고
    • The 2.1-A resolution of iron superoxide dismutase from Pseudomonas ovalis
    • Stoddard B.L., Howell P.L., Ringe D., Petsko G.A. The 2.1-A resolution of iron superoxide dismutase from Pseudomonas ovalis. Biochemistry. 29:1990;8885-8893.
    • (1990) Biochemistry , vol.29 , pp. 8885-8893
    • Stoddard, B.L.1    Howell, P.L.2    Ringe, D.3    Petsko, G.A.4
  • 30
    • 0025946099 scopus 로고
    • Pathogenic and nonpathogenic Entamoeba histolytica: Identification and molecular cloning of an iron-containing superoxide dismutase
    • Tannich E., Bruchhaus I., Walter R.D., Horstman R.D. Pathogenic and nonpathogenic Entamoeba histolytica: identification and molecular cloning of an iron-containing superoxide dismutase. Mol Biochem Parasitol. 49:1991;61-72.
    • (1991) Mol Biochem Parasitol , vol.49 , pp. 61-72
    • Tannich, E.1    Bruchhaus, I.2    Walter, R.D.3    Horstman, R.D.4
  • 33
    • 0033582535 scopus 로고    scopus 로고
    • Targeted reduction of nucleoside triphosphatehydrolase by antisense RNA inhibits Toxoplasma gondii proliferation
    • Nakaar V., Samuel B.U., Ngo E.O., Joiner K.A. Targeted reduction of nucleoside triphosphatehydrolase by antisense RNA inhibits Toxoplasma gondii proliferation. J Biol Chem. 274:1999;5083-5087.
    • (1999) J Biol Chem , vol.274 , pp. 5083-5087
    • Nakaar, V.1    Samuel, B.U.2    Ngo, E.O.3    Joiner, K.A.4
  • 34
    • 0025987923 scopus 로고
    • Proposal for a uniform genetic nomenclature in Toxoplasma gondii
    • Sibley L.D., Pfefferkorn E.R., Boothroyd J.C. Proposal for a uniform genetic nomenclature in Toxoplasma gondii. Parasitol Today. 7:1991;327-328.
    • (1991) Parasitol Today , vol.7 , pp. 327-328
    • Sibley, L.D.1    Pfefferkorn, E.R.2    Boothroyd, J.C.3
  • 35
    • 0002145058 scopus 로고    scopus 로고
    • Three dimensional molecular modeling, CD and Raman studies of Plasmodium falciparum iron-containing superoxide dismutase
    • P. et al. Carmona. London: Kluver
    • Alix A.J.P., Dauchez M., Berjot M., Gratepanche S., Dive D. Three dimensional molecular modeling, CD and Raman studies of Plasmodium falciparum iron-containing superoxide dismutase. Carmona P. et al. Spectroscopy of Biological Molecules: Modern Trends. 1997;51-53 Kluver, London.
    • (1997) Spectroscopy of Biological Molecules: Modern Trends , pp. 51-53
    • Alix, A.J.P.1    Dauchez, M.2    Berjot, M.3    Gratepanche, S.4    Dive, D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.