메뉴 건너뛰기




Volumn 239, Issue 3, 1996, Pages 655-661

Molecular cloning and characterization of a putative glutathione reductase gene, the PfGR2 gene, from Plasmodium falciparum

Author keywords

Antioxidant; Glutathione reductase; Malaria; Oxidative stress; Plasmodium falciparum

Indexed keywords

GLUTATHIONE REDUCTASE;

EID: 0029908565     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0655u.x     Document Type: Article
Times cited : (55)

References (51)
  • 1
    • 0027198723 scopus 로고
    • Low red blood cell glutathione reductase and pyridoxine phosphate oxidase activities not rolated to dietary riboflavin: Selection by malaria?
    • Anderson, B. B., Giuberti, M., Perry, G. M., Salsini, G., Casadio, I. & Vullo, C. (1993) Low red blood cell glutathione reductase and pyridoxine phosphate oxidase activities not rolated to dietary riboflavin: selection by malaria? Am. J. Clin. Nutr. 57, 666-672.
    • (1993) Am. J. Clin. Nutr. , vol.57 , pp. 666-672
    • Anderson, B.B.1    Giuberti, M.2    Perry, G.M.3    Salsini, G.4    Casadio, I.5    Vullo, C.6
  • 2
    • 0027430639 scopus 로고
    • Origin of reactive oxygen species in erythrocytes infected with Plasmodium falciparum
    • Atamna, H. & Ginsburg, H. (1993) Origin of reactive oxygen species in erythrocytes infected with Plasmodium falciparum. Parasitol. 61, 231-242.
    • (1993) Parasitol. , vol.61 , pp. 231-242
    • Atamna, H.1    Ginsburg, H.2
  • 3
    • 0028041047 scopus 로고
    • Hexose-monophosphate shunt activity in intact Plasmodium falciparum-infected erythrocytes and in free parasites
    • Atamna, H., Pascarmona, G. & Ginsburg, H. (1994) Hexose-monophosphate shunt activity in intact Plasmodium falciparum-infected erythrocytes and in free parasites. Mol. Biochem. Parasitol. 67, 79-89.
    • (1994) Mol. Biochem. Parasitol. , vol.67 , pp. 79-89
    • Atamna, H.1    Pascarmona, G.2    Ginsburg, H.3
  • 4
    • 0030034322 scopus 로고    scopus 로고
    • A glutathione reductase-like flavoenzyme of the malarial parasite Plasmodium falciparum: Structural considerations based on the DNA sequence
    • Becker, K., Müller, S., Keese, M. A., Walter, R. D. & Schirmer, R. H. (1996) A glutathione reductase-like flavoenzyme of the malarial parasite Plasmodium falciparum: structural considerations based on the DNA sequence, Biochem. Soc. Trans. 24, 67-72.
    • (1996) Biochem. Soc. Trans. , vol.24 , pp. 67-72
    • Becker, K.1    Müller, S.2    Keese, M.A.3    Walter, R.D.4    Schirmer, R.H.5
  • 5
    • 0001162149 scopus 로고
    • Erythrocyte glutathione: Function and metabolism
    • (Dolphin. D., Avramovic, O. & Poulson, R., eds) Wiley & Sons, New York
    • Beutler, E. & Dale, G. L. (1988) Erythrocyte glutathione: function and metabolism, in Coenzymes and cofactors: glutathione (Dolphin. D., Avramovic, O. & Poulson, R., eds) vol. 3. part B, pp. 291-317, Wiley & Sons, New York.
    • (1988) Coenzymes and Cofactors: Glutathione , vol.3 , Issue.PART B , pp. 291-317
    • Beutler, E.1    Dale, G.L.2
  • 7
    • 0025787080 scopus 로고
    • Redox enzyme engineering: Conversion of human glutathione reductase into a trypanothione reductase
    • Bradley, M., Bücheler, U. S. & Walsh, C. T. (1991) Redox enzyme engineering: conversion of human glutathione reductase into a trypanothione reductase, Biochemistry 30, 6124-6127.
    • (1991) Biochemistry , vol.30 , pp. 6124-6127
    • Bradley, M.1    Bücheler, U.S.2    Walsh, C.T.3
  • 8
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidium thiocyanate-phenol-chloroform extraction
    • Chomezynski, P. & Sacchi, N. (1987) Single-step method of RNA isolation by acid guanidium thiocyanate-phenol-chloroform extraction, Anal. Biochem. 162, 156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomezynski, P.1    Sacchi, N.2
  • 9
    • 0028878402 scopus 로고
    • Cloning and characterisation of glutathione reductase cDNAs and identification of two genes encoding the tobacco enzyme
    • Creissen, G. P. & Mullineaux, P. M. (1995) Cloning and characterisation of glutathione reductase cDNAs and identification of two genes encoding the tobacco enzyme. Planta (Heidelb.) 197, 422-425.
    • (1995) Planta (Heidelb.) , vol.197 , pp. 422-425
    • Creissen, G.P.1    Mullineaux, P.M.2
  • 10
    • 0022335773 scopus 로고
    • Temporal relationships on macromoleculur synthesis during the asexual cycle of Plasmodium falciparum
    • de Rojas, M. F. & Wassermann, M. (1985) Temporal relationships on macromoleculur synthesis during the asexual cycle of Plasmodium falciparum. Trans. Royal Soc. Trop. Med. Hyg. 79, 792-796.
    • (1985) Trans. Royal Soc. Trop. Med. Hyg. , vol.79 , pp. 792-796
    • De Rojas, M.F.1    Wassermann, M.2
  • 11
    • 0025265852 scopus 로고
    • Rubredoxin reductase of Pseudomonas oleovorans: Structural relationship to other flavoprotein oxidoreductases based on one NAD and two FAD fingerprints
    • Eggink, G., Engel, H., Vriend, G., Terpstra, P. & Witholt, B. (1990) Rubredoxin reductase of Pseudomonas oleovorans: structural relationship to other flavoprotein oxidoreductases based on one NAD and two FAD fingerprints, J. Mol. Biol. 212, 135 142.
    • (1990) J. Mol. Biol. , vol.212 , pp. 135-142
    • Eggink, G.1    Engel, H.2    Vriend, G.3    Terpstra, P.4    Witholt, B.5
  • 12
    • 0025821928 scopus 로고
    • Structural, spectroscopic and catalytic activity studies on glutathione reductase reconstituted with FAD analogues
    • Ermler, U., Ghisla, S., Massey, V. & Schulz, G. E. (1991) Structural, spectroscopic and catalytic activity studies on glutathione reductase reconstituted with FAD analogues, Eur. J. Biochem. 199, 33-138.
    • (1991) Eur. J. Biochem. , vol.199 , pp. 33-138
    • Ermler, U.1    Ghisla, S.2    Massey, V.3    Schulz, G.E.4
  • 15
    • 0029142578 scopus 로고
    • Cloning and sequencing of human thioredoxin reductase
    • Gasdaska, P. Y., Gasdaska, J. R., Cochran, S. & Powis, G. (1995) Cloning and sequencing of human thioredoxin reductase, FEBS Lett. 373, 5-9.
    • (1995) FEBS Lett. , vol.373 , pp. 5-9
    • Gasdaska, P.Y.1    Gasdaska, J.R.2    Cochran, S.3    Powis, G.4
  • 16
    • 0024601564 scopus 로고
    • Mechanisms of flavoprotein-catalyzed reactions
    • Ghisla, S. & Massey, V. (1989) Mechanisms of flavoprotein-catalyzed reactions, Eur. J. Biochem. 181, 1-17.
    • (1989) Eur. J. Biochem. , vol.181 , pp. 1-17
    • Ghisla, S.1    Massey, V.2
  • 17
    • 0020149711 scopus 로고
    • The establishment of genomic DNA libraries for the human parasite Plasmodium falciparum and identification of individual clones by hybridization
    • Goman, M., Langsley, G., Hyde, J. E., Yankowsky, N. K., Zolg, J. W. & Scaife, J. G. (1982) The establishment of genomic DNA libraries for the human parasite Plasmodium falciparum and identification of individual clones by hybridization, Mol. Biochem. Parasitol. 5, 391-400.
    • (1982) Mol. Biochem. Parasitol. , vol.5 , pp. 391-400
    • Goman, M.1    Langsley, G.2    Hyde, J.E.3    Yankowsky, N.K.4    Zolg, J.W.5    Scaife, J.G.6
  • 18
    • 8944229725 scopus 로고
    • Molecular and biochemical characterization of a Plasmodium falciparum cyclophilin containing a cleavable signal sequence
    • Hirtzlin, J., Färber, P. M., Franklin, R. M. & Bell, A. (1995) Molecular and biochemical characterization of a Plasmodium falciparum cyclophilin containing a cleavable signal sequence, Mol. Biochem. Parasitol. 10, 269-285.
    • (1995) Mol. Biochem. Parasitol. , vol.10 , pp. 269-285
    • Hirtzlin, J.1    Färber, P.M.2    Franklin, R.M.3    Bell, A.4
  • 19
    • 0017881332 scopus 로고
    • The α-helix dipole and the properties of proteins
    • Hol, W. G. J., van Duijnen, P. T. & Berendsen, H. J. C. (1978) The α-helix dipole and the properties of proteins, Nature 273, 443-446.
    • (1978) Nature , vol.273 , pp. 443-446
    • Hol, W.G.J.1    Van Duijnen, P.T.2    Berendsen, H.J.C.3
  • 20
    • 0025203611 scopus 로고
    • Oxidative stress and the redox status of malaria-infected erythrocytes
    • Hunt, N. H. & Stocker, R. (1990) Oxidative stress and the redox status of malaria-infected erythrocytes, Blood Cells 16, 499-526.
    • (1990) Blood Cells , vol.16 , pp. 499-526
    • Hunt, N.H.1    Stocker, R.2
  • 21
    • 0021330134 scopus 로고
    • Characterisation and translation studies of messenger RNA from the human malarial parasite Plasmodium falciparum and construction of a cDNA library
    • Hyde, J. E., Goman, M., Hall, R., Osland, A., Hope, I. A., Langsley, G. W., Zolg, J. W. & Scaife, J. G. (1984) Characterisation and translation studies of messenger RNA from the human malarial parasite Plasmodium falciparum and construction of a cDNA library, Mol. Biochem. Parasitol. 10, 269-285.
    • (1984) Mol. Biochem. Parasitol. , vol.10 , pp. 269-285
    • Hyde, J.E.1    Goman, M.2    Hall, R.3    Osland, A.4    Hope, I.A.5    Langsley, G.W.6    Zolg, J.W.7    Scaife, J.G.8
  • 22
    • 0016245986 scopus 로고
    • Glutathione reductase in the sea urchin egg
    • Ii, I. & Sakai, H. (1974) Glutathione reductase in the sea urchin egg, Biochim. Biophys. Acta 350, 151-161.
    • (1974) Biochim. Biophys. Acta , vol.350 , pp. 151-161
    • Ii, I.1    Sakai, H.2
  • 23
    • 0021326434 scopus 로고
    • Synthesis of DNA during the asexual cycle of Plasmodium falciparum in culture
    • Inselburg, J. & Banyal, H. S. (1984) Synthesis of DNA during the asexual cycle of Plasmodium falciparum in culture, Mol. Biochem. Parasitol. 10, 269-285.
    • (1984) Mol. Biochem. Parasitol. , vol.10 , pp. 269-285
    • Inselburg, J.1    Banyal, H.S.2
  • 24
    • 0025373637 scopus 로고
    • Role of the charged groups of glutathi one disulfide in the catalysis of glutathione reductase: Crystallographic and kinetic studies with synthetic analogues
    • Janes, W. & Schulz, G. E. (1990) Role of the charged groups of glutathi one disulfide in the catalysis of glutathione reductase: crystallographic and kinetic studies with synthetic analogues, Biochemistry 29, 4022-4030.
    • (1990) Biochemistry , vol.29 , pp. 4022-4030
    • Janes, W.1    Schulz, G.E.2
  • 25
    • 0023644992 scopus 로고
    • Refined structure of glutathione reductase at 1.54 Å resolution
    • Karplus, P. A. & Schulz, G. E. (1987) Refined structure of glutathione reductase at 1.54 Å resolution, J. Mol. Biol. 195, 701-729.
    • (1987) J. Mol. Biol. , vol.195 , pp. 701-729
    • Karplus, P.A.1    Schulz, G.E.2
  • 26
    • 0024959343 scopus 로고
    • A crystallographic study of the glutathione binding site of glutathione reductase at 0.3-nm resolution
    • Karplus, P. A., Pai, K. F. & Schulz, G. E. (1989) A crystallographic study of the glutathione binding site of glutathione reductase at 0.3-nm resolution, Eur. J. Biochem. 178, 693-703.
    • (1989) Eur. J. Biochem. , vol.178 , pp. 693-703
    • Karplus, P.A.1    Pai, K.F.2    Schulz, G.E.3
  • 28
    • 0030025118 scopus 로고    scopus 로고
    • Glutathione reductase and glutamate dehydrogenase of Plasmodium falciparum, the causative agent of tropical malaria
    • Krauth-Siegel, R. L., Müller, J. G., Eottspeich, F. & Schirmer, R. H. (1996) Glutathione reductase and glutamate dehydrogenase of Plasmodium falciparum, the causative agent of tropical malaria, Eur. J. Biochem. 235, 345-350.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 345-350
    • Krauth-Siegel, R.L.1    Müller, J.G.2    Eottspeich, F.3    Schirmer, R.H.4
  • 29
  • 30
    • 0023712973 scopus 로고
    • Glutathione reductase directly mediates the stimulation of yeast glucose-6-phosphate dehydrogenase by GSSG
    • Llobell, A., Lopez-Ruiz, A., Peinado, J. & López-Barea, J. (1988) Glutathione reductase directly mediates the stimulation of yeast glucose-6-phosphate dehydrogenase by GSSG, Biochem. J. 249, 293-296.
    • (1988) Biochem. J. , vol.249 , pp. 293-296
    • Llobell, A.1    Lopez-Ruiz, A.2    Peinado, J.3    López-Barea, J.4
  • 31
    • 0020050314 scopus 로고
    • A catalogue of splice junction sequences
    • Mount, S. M. (1982) A catalogue of splice junction sequences, Nucleic Acids Res. 10, 459-472.
    • (1982) Nucleic Acids Res. , vol.10 , pp. 459-472
    • Mount, S.M.1
  • 32
    • 0029563798 scopus 로고
    • Plasmodium falciparum glutathione reductase exhibits sequence similarities with the human host enzyme in the core structure but differs at the ligand-hinding sites
    • Müller, S., Becker, K., Bergmann, B., Schirmer, R. H. & Walter, R. D. (1995) Plasmodium falciparum glutathione reductase exhibits sequence similarities with the human host enzyme in the core structure but differs at the ligand-hinding sites, Mol. Biochem. Parasitol. 74, 11-18.
    • (1995) Mol. Biochem. Parasitol. , vol.74 , pp. 11-18
    • Müller, S.1    Becker, K.2    Bergmann, B.3    Schirmer, R.H.4    Walter, R.D.5
  • 33
    • 0027190591 scopus 로고
    • Folding of the four domains and dimerization are impaired by the Gly446→Glu exchange in human glutathione reductase. Implications for the design of antiparasitic drugs
    • Nordhoff, A., Bücheler, U. S., Werner, D. & Schirmer, R. H. (1993) Folding of the four domains and dimerization are impaired by the Gly446→Glu exchange in human glutathione reductase. Implications for the design of antiparasitic drugs, Biochemistry 32, 4060-4066.
    • (1993) Biochemistry , vol.32 , pp. 4060-4066
    • Nordhoff, A.1    Bücheler, U.S.2    Werner, D.3    Schirmer, R.H.4
  • 34
    • 0027412924 scopus 로고
    • Metabolism and functions of glutathione in microorganisms
    • Penninckx, M. J. & Elskens, M. T. (1993) Metabolism and functions of glutathione in microorganisms, Adv. Microbiol. Physiol. 34, 240-301.
    • (1993) Adv. Microbiol. Physiol. , vol.34 , pp. 240-301
    • Penninckx, M.J.1    Elskens, M.T.2
  • 35
    • 0021099182 scopus 로고
    • The catalytic mechanism of glutathione reductase as derived from X-ray diffraction analysis of reaction intermediates
    • Pai, E. F. & Schulz, G. E. (1983) The catalytic mechanism of glutathione reductase as derived from X-ray diffraction analysis of reaction intermediates, J. Biol. Chem. 258, 1752-1757.
    • (1983) J. Biol. Chem. , vol.258 , pp. 1752-1757
    • Pai, E.F.1    Schulz, G.E.2
  • 36
    • 0024286097 scopus 로고
    • Crystallographic analysis of the binding of NADPH, NADPH fragments, and NADPH analogues to glutathione reductase
    • Pai, E. F., Karplus, P. A. & Schulz, G. E. (1988) Crystallographic analysis of the binding of NADPH, NADPH fragments, and NADPH analogues to glutathione reductase, Biochemistry 27, 4465-4475.
    • (1988) Biochemistry , vol.27 , pp. 4465-4475
    • Pai, E.F.1    Karplus, P.A.2    Schulz, G.E.3
  • 37
    • 0028356539 scopus 로고
    • Structure of the NADPH-binding motif of glutathione reductase: Efficiency determined by evolution
    • Rescigno, M. & Perham, R. N. (1994) Structure of the NADPH-binding motif of glutathione reductase: efficiency determined by evolution, Biochemistry 33, 5721-5727.
    • (1994) Biochemistry , vol.33 , pp. 5721-5727
    • Rescigno, M.1    Perham, R.N.2
  • 39
    • 0023205787 scopus 로고
    • Malarial parasite hexokinase and hexokinase-dependent glutathione reduction in the Plasmodium falciparum-infected human erythrocyte
    • Roth, E. F. Jr (1987) Malarial parasite hexokinase and hexokinase-dependent glutathione reduction in the Plasmodium falciparum-infected human erythrocyte, J. Biol. Chem. 262, 15678-15682.
    • (1987) J. Biol. Chem. , vol.262 , pp. 15678-15682
    • Roth Jr., E.F.1
  • 40
    • 0025347960 scopus 로고
    • Analysis of the sequences flanking the translational start sites of Plasmodium falciparum
    • Saul, A. & Battistutta, D. (1990) Analysis of the sequences flanking the translational start sites of Plasmodium falciparum, Mol. Biochem. Parasitol. 42, 55-62.
    • (1990) Mol. Biochem. Parasitol. , vol.42 , pp. 55-62
    • Saul, A.1    Battistutta, D.2
  • 41
    • 0001136010 scopus 로고
    • Glutathione reductase
    • (Dolphin. D., Avramovic, O. & Poulson, R., eds) Wiley & Sons, New York
    • Schirmer, R. H., Krauth-Siegel, R. L. & Schulz, G. E. (1989) Glutathione reductase, in Coenzymes and cofactors: glutathione (Dolphin. D., Avramovic, O. & Poulson, R., eds) vol. 3. part A, pp. 553-596, Wiley & Sons, New York.
    • (1989) Coenzymes and Cofactors: Glutathione , vol.3 , Issue.PART A , pp. 553-596
    • Schirmer, R.H.1    Krauth-Siegel, R.L.2    Schulz, G.E.3
  • 42
    • 33748233963 scopus 로고
    • Disulfide reductase inhibitors as chemotherapeutic agents: The design of drugs for trypanosomiasis and malaria
    • Schirmer, R. H., Müller, J. G. & Krauth-Siegel, R. L. (1995) Disulfide reductase inhibitors as chemotherapeutic agents: the design of drugs for trypanosomiasis and malaria, Angew. Chem. Int. Ed. Engl. 34, 141-154.
    • (1995) Angew. Chem. Int. Ed. Engl. , vol.34 , pp. 141-154
    • Schirmer, R.H.1    Müller, J.G.2    Krauth-Siegel, R.L.3
  • 43
    • 0017879559 scopus 로고
    • The structure of the flavoenzyme glutathione reductase
    • Schulz, G. E., Schirmer, R. H., Sachsenheimer, W. & Pai, E. F. (1978) The structure of the flavoenzyme glutathione reductase, Nature 273, 120-124.
    • (1978) Nature , vol.273 , pp. 120-124
    • Schulz, G.E.1    Schirmer, R.H.2    Sachsenheimer, W.3    Pai, E.F.4
  • 44
    • 0026763791 scopus 로고
    • An 88-kDa protein of Plasmodium falciparum is related to the band-3-binding domain of human erythrocytic ankyrin
    • Sütterlin, B. W., Kappes, B., Jenö, P. & Franklin, R. M. (1992) An 88-kDa protein of Plasmodium falciparum is related to the band-3-binding domain of human erythrocytic ankyrin, Eur. J. Biochem. 207, 455-461.
    • (1992) Eur. J. Biochem. , vol.207 , pp. 455-461
    • Sütterlin, B.W.1    Kappes, B.2    Jenö, P.3    Franklin, R.M.4
  • 46
    • 0017311840 scopus 로고
    • Human malaria parasites in continuous culture
    • Trager, W. & Jensen, J. B. (1976) Human malaria parasites in continuous culture, Science 193, 673-675.
    • (1976) Science , vol.193 , pp. 673-675
    • Trager, W.1    Jensen, J.B.2
  • 47
    • 0000876731 scopus 로고
    • Lipoamide dehydrogenase, glutathione reductase, thioredoxin reductase, and mercuric ion reductase - A family of flavoenzyme transhydrogenases
    • (Müller, F., ed.) CRC Press, Boca Raton, FL
    • Williams, C. H. Jr (1992) Lipoamide dehydrogenase, glutathione reductase, thioredoxin reductase, and mercuric ion reductase - A family of flavoenzyme transhydrogenases, in Chemistry and biochemistry of flavoenzymes (Müller, F., ed.) vol. 3, pp. 121-211. CRC Press, Boca Raton, FL.
    • (1992) Chemistry and Biochemistry of Flavoenzymes , vol.3 , pp. 121-211
    • Williams Jr., C.H.1
  • 48
    • 0025804898 scopus 로고
    • The sequence flanking translational initiation sites in protozoa
    • Yamauchi, K. (1991) The sequence flanking translational initiation sites in protozoa, Nucleic Acids Res. 19, 2715-2720.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 2715-2720
    • Yamauchi, K.1
  • 49
    • 0023853092 scopus 로고
    • Glutathione reductase inhibitors as potential antimalarial drugs
    • Zhang, Y, Hempelmann, E. & Schirmer, R. H. (1988a) Glutathione reductase inhibitors as potential antimalarial drugs, Biochem. Pharmacol. 37, 855-860.
    • (1988) Biochem. Pharmacol. , vol.37 , pp. 855-860
    • Zhang, Y.1    Hempelmann, E.2    Schirmer, R.H.3
  • 50
    • 0023831311 scopus 로고
    • Glutathione reductase-deficient erythrocytes as host cells of malarial parasites
    • Zhang, Y., König, I. & Schirmer, R. H. (1988b) Glutathione reductase-deficient erythrocytes as host cells of malarial parasites, Biochem. Pharmacol. 37, 861-865.
    • (1988) Biochem. Pharmacol. , vol.37 , pp. 861-865
    • Zhang, Y.1    König, I.2    Schirmer, R.H.3
  • 51
    • 0026638161 scopus 로고
    • Molecular cloning, stage-specific expression and cellular distribution of a putative protein kinase from Plasmodium falciparum
    • Zhao, Y., Kappes, B., Yang, J. & Franklin, R. M. (1992) Molecular cloning, stage-specific expression and cellular distribution of a putative protein kinase from Plasmodium falciparum, Eur. J. Biochem. 207, 305-313.
    • (1992) Eur. J. Biochem. , vol.207 , pp. 305-313
    • Zhao, Y.1    Kappes, B.2    Yang, J.3    Franklin, R.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.