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Volumn 28, Issue 5, 2009, Pages 479-487

Expression of a glutathione reductase from Brassica rapa subsp. pekinensis enhanced cellular redox homeostasis by modulating antioxidant proteins in Escherichia coli

Author keywords

Antioxidant enzymes; Brassica rapa subsp. pekinensis; Escherichia coli; Glutathione reductase; Stress tolerance

Indexed keywords

CATALASE; GLUCOSE 6 PHOSPHATE DEHYDROGENASE; GLUTATHIONE PEROXIDASE; GLUTATHIONE REDUCTASE; SUPEROXIDE DISMUTASE;

EID: 72949122801     PISSN: 10168478     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10059-009-0168-y     Document Type: Article
Times cited : (21)

References (40)
  • 2
    • 0036023036 scopus 로고    scopus 로고
    • Disrupting Escherichia coli: A comparison of methods
    • L. Benov J. Al-Ibraheem 2002 Disrupting Escherichia coli: a comparison of methods J. Biochem. Mol. Biol. 35 428 431
    • (2002) J. Biochem. Mol. Biol. , vol.35 , pp. 428-431
    • Benov, L.1    Al-Ibraheem, J.2
  • 4
    • 0026724643 scopus 로고
    • Generating compatible translation initiation regions for heterologous gene expression in Escherichia coli by exhaustive periShine-Dalgarno mutagenesis. Human glutathione reductase cDNA as a model
    • U.S. Bucheler D. Werner R.H. Schirmer 1992 Generating compatible translation initiation regions for heterologous gene expression in Escherichia coli by exhaustive periShine-Dalgarno mutagenesis. Human glutathione reductase cDNA as a model Nucleic Acids Res. 20 3127 3133
    • (1992) Nucleic Acids Res. , vol.20 , pp. 3127-3133
    • Bucheler, U.S.1    Werner, D.2    Schirmer, R.H.3
  • 5
    • 0033767925 scopus 로고    scopus 로고
    • Roles of the glutathione- and thioredoxin-dependent reduction systems in the Escherichia coli and Saccharomyces cerevisiae responses to oxidative stress
    • O. Carmel-Harel G. Storz 2000 Roles of the glutathione- and thioredoxin-dependent reduction systems in the Escherichia coli and Saccharomyces cerevisiae responses to oxidative stress Annu. Rev. Microbiol. 54 439 461
    • (2000) Annu. Rev. Microbiol. , vol.54 , pp. 439-461
    • Carmel-Harel, O.1    Storz, G.2
  • 8
    • 0027411681 scopus 로고
    • Posttranscriptional repression of Escherichia coli OmpF protein in response to redox stress: Positive control of the micF antisense RNA by the soxRS locus
    • J.H. Chou J.T. Greenberg B. Demple 1993 Posttranscriptional repression of Escherichia coli OmpF protein in response to redox stress: positive control of the micF antisense RNA by the soxRS locus J. Bacteriol. 175 1026 1031
    • (1993) J. Bacteriol. , vol.175 , pp. 1026-1031
    • Chou, J.H.1    Greenberg, J.T.2    Demple, B.3
  • 9
    • 0028960573 scopus 로고
    • Isolation, characterization and overexpression of the yeast gene, GLR1, encoding glutathione reductase
    • L.P. Collinson I.W. Dawes 1995 Isolation, characterization and overexpression of the yeast gene, GLR1, encoding glutathione reductase Gene 156 123 127
    • (1995) Gene , vol.156 , pp. 123-127
    • Collinson, L.P.1    Dawes, I.W.2
  • 10
    • 0028878402 scopus 로고
    • Cloning and characterisation of glutathione reductase cDNAs and identification of two genes encoding the tobacco enzyme
    • G.P. Creissen P.M. Mullineaux 1995 Cloning and characterisation of glutathione reductase cDNAs and identification of two genes encoding the tobacco enzyme Planta 197 422 425
    • (1995) Planta , vol.197 , pp. 422-425
    • Creissen, G.P.1    Mullineaux, P.M.2
  • 11
    • 66949180061 scopus 로고    scopus 로고
    • Cloning and molecular characterization of fructose-1,6-bisphosphate aldolase gene regulated by high-salinity and drought in Sesuvium portulacastrum
    • W. Fan Z. Zhang Y. Zhang 2009 Cloning and molecular characterization of fructose-1,6-bisphosphate aldolase gene regulated by high-salinity and drought in Sesuvium portulacastrum Plant Cell Rep. 28 975 984
    • (2009) Plant Cell Rep. , vol.28 , pp. 975-984
    • Fan, W.1    Zhang, Z.2    Zhang, Y.3
  • 12
    • 0022446871 scopus 로고
    • Glutathione reductase from Escherichia coli: Cloning and sequence analysis of the gene and relationship to other flavoprotein disulfide oxidoreductases
    • S. Greer R.N. Perham 1986 Glutathione reductase from Escherichia coli: cloning and sequence analysis of the gene and relationship to other flavoprotein disulfide oxidoreductases Biochemistry 25 2736 2742
    • (1986) Biochemistry , vol.25 , pp. 2736-2742
    • Greer, S.1    Perham, R.N.2
  • 13
    • 52049083735 scopus 로고    scopus 로고
    • Multiple stressor-induced proteome responses of Escherichia coli BL21(DE3)
    • K.Y. Han J.S. Park H.S. Seo K.Y. Ahn J. Lee 2008 Multiple stressor-induced proteome responses of Escherichia coli BL21(DE3) J. Proteome Res. 7 1891 1903
    • (2008) J. Proteome Res. , vol.7 , pp. 1891-1903
    • Han, K.Y.1    Park, J.S.2    Seo, H.S.3    Ahn, K.Y.4    Lee, J.5
  • 14
    • 34548297779 scopus 로고    scopus 로고
    • Physiological response and protein expression under acid stress of Escherichia coli O157:H7 TWC01 isolated from Taiwan
    • Y.J. Huang T.Y. Tsai T.M. Pan 2007 Physiological response and protein expression under acid stress of Escherichia coli O157:H7 TWC01 isolated from Taiwan J. Agric. Food Chem. 55 7182 7191
    • (2007) J. Agric. Food Chem. , vol.55 , pp. 7182-7191
    • Huang, Y.J.1    Tsai, T.Y.2    Pan, T.M.3
  • 15
    • 0026632930 scopus 로고
    • Ferrous ion oxidation in the presence of xylenol orange for detection of lipid hydroperoxide in low density lipoprotein
    • Z.Y. Jiang J.V. Hunt S.P. Wolff 1992 Ferrous ion oxidation in the presence of xylenol orange for detection of lipid hydroperoxide in low density lipoprotein Anal. Biochem. 202 384 389
    • (1992) Anal. Biochem. , vol.202 , pp. 384-389
    • Jiang, Z.Y.1    Hunt, J.V.2    Wolff, S.P.3
  • 16
    • 0029092651 scopus 로고
    • Cloning, sequencing, and regulation of the glutathione reductase gene from the cyanobacterium Anabaena PCC 7120
    • F. Jiang U. Hellman G.E. Sroga B. Bergman B. Mannervik 1995 Cloning, sequencing, and regulation of the glutathione reductase gene from the cyanobacterium Anabaena PCC 7120 J. Biol. Chem. 270 22882 22889
    • (1995) J. Biol. Chem. , vol.270 , pp. 22882-22889
    • Jiang, F.1    Hellman, U.2    Sroga, G.E.3    Bergman, B.4    Mannervik, B.5
  • 17
    • 0027144316 scopus 로고
    • Primary structure and properties of glutathione reductase from Arabidopsis thaliana
    • A. Kubo T. Sano H. Saji K. Tanaka N. Kondo K. Tanaka 1993 Primary structure and properties of glutathione reductase from Arabidopsis thaliana Plant Cell Physiol. 34 1259 1266
    • (1993) Plant Cell Physiol. , vol.34 , pp. 1259-1266
    • Kubo, A.1    Sano, T.2    Saji, H.3    Tanaka, K.4    Kondo, N.5    Tanaka, K.6
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli 1970 Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 0032506968 scopus 로고    scopus 로고
    • Molecular cloning and characterization of the gene encoding glutathione reductase in Brassica campestris
    • H. Lee J. Jo D. Son 1998 Molecular cloning and characterization of the gene encoding glutathione reductase in Brassica campestris Biochim. Biophys. Acta 1395 309 314
    • (1998) Biochim. Biophys. Acta , vol.1395 , pp. 309-314
    • Lee, H.1    Jo, J.2    Son, D.3
  • 20
    • 0037198112 scopus 로고    scopus 로고
    • Genomic cloning and characterization of glutathione reductase gene from Brassica campestris var. pekinensis
    • H. Lee S.H. Won B.H. Lee H.D. Park W.I. Chung J. Jo 2002 Genomic cloning and characterization of glutathione reductase gene from Brassica campestris var. pekinensis Mol. Cells 13 245 251
    • (2002) Mol. Cells , vol.13 , pp. 245-251
    • Lee, H.1    Won, S.H.2    Lee, B.H.3    Park, H.D.4    Chung, W.I.5    Jo, J.6
  • 21
    • 20444389441 scopus 로고    scopus 로고
    • Expression and oxidative stress tolerance studies of glutaredoxin from cyanobacterium Synechocystis sp. PCC 6803 in Escherichia coli
    • M. Li W. Huang Q. Yang X. Liu Q. Wu 2005 Expression and oxidative stress tolerance studies of glutaredoxin from cyanobacterium Synechocystis sp. PCC 6803 in Escherichia coli Protein Expr. Purif. 42 85 91
    • (2005) Protein Expr. Purif. , vol.42 , pp. 85-91
    • Li, M.1    Huang, W.2    Yang, Q.3    Liu, X.4    Wu, Q.5
  • 22
    • 3242688896 scopus 로고    scopus 로고
    • Zinc and cadmium specifically interfere with RNA-binding activity of human iron regulatory protein 1
    • A. Martelli J.M. Moulis 2004 Zinc and cadmium specifically interfere with RNA-binding activity of human iron regulatory protein 1 J. Inorg. Biochem. 98 1413 1420
    • (2004) J. Inorg. Biochem. , vol.98 , pp. 1413-1420
    • Martelli, A.1    Moulis, J.M.2
  • 24
    • 62649160529 scopus 로고    scopus 로고
    • AhpC (alkyl hydroperoxide reductase) from Anabaena sp. PCC 7120 protects Escherichia coli from multiple abiotic stresses
    • Y. Mishra N. Chaurasia L.C. Rai 2009 AhpC (alkyl hydroperoxide reductase) from Anabaena sp. PCC 7120 protects Escherichia coli from multiple abiotic stresses Biochem. Biophys. Res. Commun. 381 606 611
    • (2009) Biochem. Biophys. Res. Commun. , vol.381 , pp. 606-611
    • Mishra, Y.1    Chaurasia, N.2    Rai, L.C.3
  • 25
    • 0032844257 scopus 로고    scopus 로고
    • Overexpression of glutathione reductase extends survival in transgenic Drosophila melanogaster under hyperoxia but not normoxia
    • R.J. Mockett R.S. Sohal W.C. Orr 1999 Overexpression of glutathione reductase extends survival in transgenic Drosophila melanogaster under hyperoxia but not normoxia FASEB J. 13 1733 1742
    • (1999) FASEB J. , vol.13 , pp. 1733-1742
    • Mockett, R.J.1    Sohal, R.S.2    Orr, W.C.3
  • 26
    • 0024498674 scopus 로고
    • Cloning and characterization of the Escherichia coli phosphoglycerate kinase (pgk) gene
    • L.J. Nellemann F. Holm T. Atlung F.G. Hansen 1989 Cloning and characterization of the Escherichia coli phosphoglycerate kinase (pgk) gene Gene 77 185 191
    • (1989) Gene , vol.77 , pp. 185-191
    • Nellemann, L.J.1    Holm, F.2    Atlung, T.3    Hansen, F.G.4
  • 27
    • 14244268784 scopus 로고    scopus 로고
    • Genome-wide analyses of Escherichia coli gene expression responsive to the BaeSR two-component regulatory system
    • K. Nishino T. Honda A. Yamaguchi 2005 Genome-wide analyses of Escherichia coli gene expression responsive to the BaeSR two-component regulatory system J. Bacteriol. 187 1763 1772
    • (2005) J. Bacteriol. , vol.187 , pp. 1763-1772
    • Nishino, K.1    Honda, T.2    Yamaguchi, A.3
  • 28
    • 0033071047 scopus 로고    scopus 로고
    • Gene transfer of mitochondrially targeted glutathione reductase protects H441 cells from t-butyl hydroperoxide-induced oxidant stresses
    • D.J. O'Donovan J.P. Katkin T. Tamura R. Husser X. Xu C.V. Smith S.E. Welty 1999 Gene transfer of mitochondrially targeted glutathione reductase protects H441 cells from t-butyl hydroperoxide-induced oxidant stresses Am. J. Respir. Cell Mol. Biol. 20 256 263
    • (1999) Am. J. Respir. Cell Mol. Biol. , vol.20 , pp. 256-263
    • O'Donovan, D.J.1    Katkin, J.P.2    Tamura, T.3    Husser, R.4    Xu, X.5    Smith, C.V.6    Welty, S.E.7
  • 29
    • 0026081456 scopus 로고
    • Molecular characterization of the gor gene encoding glutathione reductase from Pseudomonas aeruginosa: Determinants of substrate specificity among pyridine nucleotide-disulphide oxidoreductases
    • A.C. Perry N. Ni Bhriain N.L. Brown D.A. Rouch 1991 Molecular characterization of the gor gene encoding glutathione reductase from Pseudomonas aeruginosa: determinants of substrate specificity among pyridine nucleotide-disulphide oxidoreductases Mol. Microbiol. 5 163 171
    • (1991) Mol. Microbiol. , vol.5 , pp. 163-171
    • Perry, A.C.1    Ni Bhriain, N.2    Brown, N.L.3    Rouch, D.A.4
  • 30
    • 0034525911 scopus 로고    scopus 로고
    • Overexpression of glutathion reductase in Brassica juncea: Effects on cadmium accumulation and tolerance
    • E.A. Pilon-Smits Y.L. Zhu T. Sears N. Terry 2000 Overexpression of glutathion reductase in Brassica juncea: effects on cadmium accumulation and tolerance Physiol. Plant 110 455 460
    • (2000) Physiol. Plant , vol.110 , pp. 455-460
    • Pilon-Smits, E.A.1    Zhu, Y.L.2    Sears, T.3    Terry, N.4
  • 31
    • 0035209075 scopus 로고    scopus 로고
    • Alkyl hydroperoxide reductase is the primary scavenger of endogenous hydrogen peroxide in Escherichia coli
    • L.C. Seaver J.A. Imlay 2001 Alkyl hydroperoxide reductase is the primary scavenger of endogenous hydrogen peroxide in Escherichia coli J. Bacteriol. 183 7173 7181
    • (2001) J. Bacteriol. , vol.183 , pp. 7173-7181
    • Seaver, L.C.1    Imlay, J.A.2
  • 33
    • 0033966137 scopus 로고    scopus 로고
    • The biosynthesis of erythroascorbate in Saccharomyces cerevisiae and its role as an antioxidant
    • C.M. Spickett N. Smirnoff A.R. Pitt 2000 The biosynthesis of erythroascorbate in Saccharomyces cerevisiae and its role as an antioxidant Free Radic Biol Med 28 183 192
    • (2000) Free Radic Biol Med , vol.28 , pp. 183-192
    • Spickett, C.M.1    Smirnoff, N.2    Pitt, A.R.3
  • 34
    • 0033789250 scopus 로고    scopus 로고
    • Characterisation of pea cytosolic glutathione reductase expressed in transgenic tobacco
    • R.G. Stevens G.P. Creissen P.M. Mullineaux 2000 Characterisation of pea cytosolic glutathione reductase expressed in transgenic tobacco Planta 211 537 545
    • (2000) Planta , vol.211 , pp. 537-545
    • Stevens, R.G.1    Creissen, G.P.2    Mullineaux, P.M.3
  • 35
    • 0034668921 scopus 로고    scopus 로고
    • Role of glutathione in heat-shock-induced cell death of Saccharomyces cerevisiae
    • K. Sugiyama A. Kawamura S. Izawa Y. Inoue 2000 Role of glutathione in heat-shock-induced cell death of Saccharomyces cerevisiae Biochem. J. 352 71 78
    • (2000) Biochem. J. , vol.352 , pp. 71-78
    • Sugiyama, K.1    Kawamura, A.2    Izawa, S.3    Inoue, Y.4
  • 36
    • 0032579371 scopus 로고    scopus 로고
    • Identification of the major oxidatively damaged proteins in Escherichia coli cells exposed to oxidative stress
    • J. Tamarit E. Cabiscol J. Ros 1998 Identification of the major oxidatively damaged proteins in Escherichia coli cells exposed to oxidative stress J. Biol. Chem. 273 3027 3032
    • (1998) J. Biol. Chem. , vol.273 , pp. 3027-3032
    • Tamarit, J.1    Cabiscol, E.2    Ros, J.3
  • 37
    • 1642547105 scopus 로고    scopus 로고
    • Regulation of redox homeostasis in the yeast Saccharomyces cerevisiae
    • G.L. Wheeler C.M. Grant 2004 Regulation of redox homeostasis in the yeast Saccharomyces cerevisiae Physiol. Plant 120 12 20
    • (2004) Physiol. Plant , vol.120 , pp. 12-20
    • Wheeler, G.L.1    Grant, C.M.2
  • 38
    • 0347622754 scopus 로고    scopus 로고
    • PHdependent catabolic protein expression during anaerobic growth of Escherichia coli K-12
    • E. Yohannes D.M. Barnhart J.L. Slonczewski 2004 pHdependent catabolic protein expression during anaerobic growth of Escherichia coli K-12 J. Bacteriol. 186 192 199
    • (2004) J. Bacteriol. , vol.186 , pp. 192-199
    • Yohannes, E.1    Barnhart, D.M.2    Slonczewski, J.L.3
  • 39
    • 10444288624 scopus 로고    scopus 로고
    • Overexpression of a eukaryotic glutathione reductase gene from Brassica campestris improved resistance to oxidative stress in Escherichia coli
    • H.S. Yoon I.A. Lee H. Lee B.H. Lee J. Jo 2005 Overexpression of a eukaryotic glutathione reductase gene from Brassica campestris improved resistance to oxidative stress in Escherichia coli Biochem. Biophys. Res. Commun. 326 618 623
    • (2005) Biochem. Biophys. Res. Commun. , vol.326 , pp. 618-623
    • Yoon, H.S.1    Lee, I.A.2    Lee, H.3    Lee, B.H.4    Jo, J.5
  • 40
    • 34548717039 scopus 로고    scopus 로고
    • Crystal structure of glutathione reductase Glr1 from the yeast Saccharomyces cerevisiae
    • J. Yu C.Z. Zhou 2007 Crystal structure of glutathione reductase Glr1 from the yeast Saccharomyces cerevisiae Proteins 68 972 979
    • (2007) Proteins , vol.68 , pp. 972-979
    • Yu, J.1    Zhou, C.Z.2


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