메뉴 건너뛰기




Volumn 331, Issue 4, 2005, Pages 1324-1330

The unique glutathione reductase from Xanthomonas campestris: Gene expression and enzyme characterization

Author keywords

Glutathione reductase; NADPH binding motif; Organic hydroperoxide responsive promoter; Oxidative stress

Indexed keywords

ARGININE; BACTERIAL ENZYME; BETA GALACTOSIDASE; GLUTAMINE; GLUTATHIONE REDUCTASE; RECOMBINANT ENZYME; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

EID: 18844413767     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.04.050     Document Type: Article
Times cited : (12)

References (37)
  • 1
    • 0027394247 scopus 로고
    • Redox-activated expression of the cytosolic copper/zinc superoxide dismutase gene in Nicotiana
    • D. Herouart, M. Van Montagu, and D. Inze Redox-activated expression of the cytosolic copper/zinc superoxide dismutase gene in Nicotiana Proc. Natl. Acad. Sci. USA 90 1993 3012 3108
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 3012-3108
    • Herouart, D.1    Van Montagu, M.2    Inze, D.3
  • 2
    • 0030047596 scopus 로고    scopus 로고
    • Differential redox regulation by glutathione of glutathione reductase and CuZn-superoxide dismutase gene expression in Pinus sylvestris L. needles
    • G. Wingsle, and S. Karpinski Differential redox regulation by glutathione of glutathione reductase and CuZn-superoxide dismutase gene expression in Pinus sylvestris L. needles Planta 198 1996 151 157
    • (1996) Planta , vol.198 , pp. 151-157
    • Wingsle, G.1    Karpinski, S.2
  • 3
    • 0018409718 scopus 로고
    • Levels of glutathione in Escherichia coli
    • P.C. Loewen Levels of glutathione in Escherichia coli Can. J. Biochem. 57 1979 107 111
    • (1979) Can. J. Biochem. , vol.57 , pp. 107-111
    • Loewen, P.C.1
  • 5
    • 0021444159 scopus 로고
    • Repeating functional domains in the pyruvate dehydrogenase multienzyme complex of Escherichia coli
    • L.C. Packman, G. Hale, and R.N. Perham Repeating functional domains in the pyruvate dehydrogenase multienzyme complex of Escherichia coli EMBO J. 3 1984 1315 1319
    • (1984) EMBO J. , vol.3 , pp. 1315-1319
    • Packman, L.C.1    Hale, G.2    Perham, R.N.3
  • 6
    • 0020478725 scopus 로고
    • Mercuric reductase. Purification and characterization of a transposon-encoded flavoprotein containing an oxidation-reduction-active disulfide
    • B. Fox, and C.T. Walsh Mercuric reductase. Purification and characterization of a transposon-encoded flavoprotein containing an oxidation-reduction-active disulfide J. Biol. Chem. 257 1982 2498 2503
    • (1982) J. Biol. Chem. , vol.257 , pp. 2498-2503
    • Fox, B.1    Walsh, C.T.2
  • 7
    • 0023051830 scopus 로고
    • Purification and characterization of trypanothione reductase from Crithidia fasciculata, a newly discovered member of the family of disulfide-containing flavoprotein reductases
    • S.L. Shames, A.H. Fairlamb, A. Cerami, and C.T. Walsh Purification and characterization of trypanothione reductase from Crithidia fasciculata, a newly discovered member of the family of disulfide-containing flavoprotein reductases Biochemistry 25 1986 3519 3526
    • (1986) Biochemistry , vol.25 , pp. 3519-3526
    • Shames, S.L.1    Fairlamb, A.H.2    Cerami, A.3    Walsh, C.T.4
  • 8
    • 0018882304 scopus 로고
    • Pyridine nucleotide-disulfide oxidoreductases
    • A. Holmgren Pyridine nucleotide-disulfide oxidoreductases Experientia Suppl. 36 1980 149 180
    • (1980) Experientia Suppl. , vol.36 , pp. 149-180
    • Holmgren, A.1
  • 9
    • 0026235115 scopus 로고
    • New enzymes for old: Redesigning the coenzyme and substrate specificities of glutathione reductase
    • R.N. Perham, N.S. Scrutton, and A. Berry New enzymes for old: redesigning the coenzyme and substrate specificities of glutathione reductase Bioessays 13 1991 515 525
    • (1991) Bioessays , vol.13 , pp. 515-525
    • Perham, R.N.1    Scrutton, N.S.2    Berry, A.3
  • 10
    • 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, and D.A. Rouch Molecular characterization of the gor gene encoding glutathione reductase from Pseudomonas aeruginosa: determinants of substrate specificity among pyridine nucleotide-disulphide oxidoreductases Mol. Microbiol. 5 1991 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
  • 11
    • 0011985493 scopus 로고
    • CAB International Tucson, Arizona
    • S.H. Ou Bacterial disease 1987 CAB International Tucson, Arizona
    • (1987) Bacterial Disease
    • Ou, S.H.1
  • 12
    • 0031899593 scopus 로고    scopus 로고
    • Identification and characterization of a new organic hydroperoxide resistance (ohr) gene with a novel pattern of oxidative stress regulation from Xanthomonas campestris pv. phaseoli
    • S. Mongkolsuk, W. Praituan, S. Loprasert, M. Fuangthong, and S. Chamnongpol Identification and characterization of a new organic hydroperoxide resistance (ohr) gene with a novel pattern of oxidative stress regulation from Xanthomonas campestris pv. phaseoli J. Bacteriol. 180 1998 2636 2643
    • (1998) J. Bacteriol. , vol.180 , pp. 2636-2643
    • Mongkolsuk, S.1    Praituan, W.2    Loprasert, S.3    Fuangthong, M.4    Chamnongpol, S.5
  • 15
    • 0025195680 scopus 로고
    • Mini-Tn5 transposon derivatives for insertion mutagenesis, promoter probing, and chromosomal insertion of cloned DNA in gram-negative eubacteria
    • V. de Lorenzo, M. Herrero, U. Jakubzik, and K.N. Timmis Mini-Tn5 transposon derivatives for insertion mutagenesis, promoter probing, and chromosomal insertion of cloned DNA in gram-negative eubacteria J. Bacteriol. 172 1990 6568 6572
    • (1990) J. Bacteriol. , vol.172 , pp. 6568-6572
    • De Lorenzo, V.1    Herrero, M.2    Jakubzik, U.3    Timmis, K.N.4
  • 16
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 17
    • 0014690791 scopus 로고
    • The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis
    • K. Weber, and M. Osborn The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis J. Biol. Chem. 244 1969 4406 4412
    • (1969) J. Biol. Chem. , vol.244 , pp. 4406-4412
    • Weber, K.1    Osborn, M.2
  • 18
    • 0024199997 scopus 로고
    • Assay of glutathione reductase in crude tissue homogenates using 5,5′-dithiobis(2-nitrobenzoic acid)
    • I.K. Smith, T.L. Vierheller, and C.A. Thorne Assay of glutathione reductase in crude tissue homogenates using 5,5′-dithiobis(2-nitrobenzoic acid) Anal. Biochem. 175 1988 408 413
    • (1988) Anal. Biochem. , vol.175 , pp. 408-413
    • Smith, I.K.1    Vierheller, T.L.2    Thorne, C.A.3
  • 19
    • 0036032183 scopus 로고    scopus 로고
    • OhrR, a transcription repressor that senses and responds to changes in organic peroxide levels in Xanthomonas campestris pv. phaseoli
    • W. Panmanee, P. Vattanaviboon, W. Eiamphungporn, W. Whangsuk, R. Sallabhan, and S. Mongkolsuk OhrR, a transcription repressor that senses and responds to changes in organic peroxide levels in Xanthomonas campestris pv. phaseoli Mol. Microbiol. 45 2002 1647 1654
    • (2002) Mol. Microbiol. , vol.45 , pp. 1647-1654
    • Panmanee, W.1    Vattanaviboon, P.2    Eiamphungporn, W.3    Whangsuk, W.4    Sallabhan, R.5    Mongkolsuk, S.6
  • 20
    • 0013805993 scopus 로고
    • Comparison of beta-galactosidases from normal (i-o+z+) and operator constitutive (i-ocz+) strains of E. coli
    • E. Steers Jr., G.R. Craven, and C.B. Anfinsen Comparison of beta-galactosidases from normal (i-o+z+) and operator constitutive (i-ocz+) strains of E. coli Proc. Natl. Acad. Sci. USA 54 1965 1174 1181
    • (1965) Proc. Natl. Acad. Sci. USA , vol.54 , pp. 1174-1181
    • Steers Jr., E.1    Craven, G.R.2    Anfinsen, C.B.3
  • 21
    • 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, and B. Mannervik Cloning, sequencing, and regulation of the glutathione reductase gene from the cyanobacterium Anabaena PCC 7120 J. Biol. Chem. 270 1995 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
  • 22
    • 0030752690 scopus 로고    scopus 로고
    • Isolation, expression, and regulation of the pgr1 gene encoding glutathione reductase absolutely required for the growth of Schizosaccharomyces pombe
    • J. Lee, I.W. Dawes, and J.H. Roe Isolation, expression, and regulation of the pgr1 gene encoding glutathione reductase absolutely required for the growth of Schizosaccharomyces pombe J. Biol. Chem. 272 1997 23042 23049
    • (1997) J. Biol. Chem. , vol.272 , pp. 23042-23049
    • Lee, J.1    Dawes, I.W.2    Roe, J.H.3
  • 23
    • 0032943524 scopus 로고    scopus 로고
    • In vivo transcription of the Escherichia coli oxyR regulon as a function of growth phase and in response to oxidative stress
    • C. Michan, M. Manchado, G. Dorado, and C. Pueyo In vivo transcription of the Escherichia coli oxyR regulon as a function of growth phase and in response to oxidative stress J. Bacteriol. 181 1999 2564 2759
    • (1999) J. Bacteriol. , vol.181 , pp. 2564-2759
    • Michan, C.1    Manchado, M.2    Dorado, G.3    Pueyo, C.4
  • 24
    • 0031859324 scopus 로고    scopus 로고
    • Construction and physiological analysis of a Xanthomonas mutant to examine the role of the oxyR gene in oxidant-induced protection against peroxide killing
    • S. Mongkolsuk, R. Sukchawalit, S. Loprasert, W. Praituan, and A. Upaichit Construction and physiological analysis of a Xanthomonas mutant to examine the role of the oxyR gene in oxidant-induced protection against peroxide killing J. Bacteriol. 180 1998 3988 3991
    • (1998) J. Bacteriol. , vol.180 , pp. 3988-3991
    • Mongkolsuk, S.1    Sukchawalit, R.2    Loprasert, S.3    Praituan, W.4    Upaichit, A.5
  • 25
    • 0034047382 scopus 로고    scopus 로고
    • Mutations in oxyR resulting in peroxide resistance in Xanthomonas campestris
    • S. Mongkolsuk, W. Whangsuk, M. Fuangthong, and S. Loprasert Mutations in oxyR resulting in peroxide resistance in Xanthomonas campestris J. Bacteriol. 182 2000 3846 3849
    • (2000) J. Bacteriol. , vol.182 , pp. 3846-3849
    • Mongkolsuk, S.1    Whangsuk, W.2    Fuangthong, M.3    Loprasert, S.4
  • 26
    • 4944219920 scopus 로고    scopus 로고
    • The glutathione-glutaredoxin system in Rhodobacter capsulatus: Part of a complex regulatory network controlling defense against oxidative stress
    • K. Li, S. Hein, W. Zou, and G. Klug The glutathione-glutaredoxin system in Rhodobacter capsulatus: part of a complex regulatory network controlling defense against oxidative stress J. Bacteriol. 186 2004 6800 6808
    • (2004) J. Bacteriol. , vol.186 , pp. 6800-6808
    • Li, K.1    Hein, S.2    Zou, W.3    Klug, G.4
  • 27
    • 0002752725 scopus 로고    scopus 로고
    • Glutathione reductase: Regulation and role in oxidative stress
    • J. Scandalios Cold Spring Harbor Laboratory Press New York
    • P.M. Mullineaux, and G.P. Creissen Glutathione reductase: regulation and role in oxidative stress J. Scandalios Oxidative stress and the molecular biology of antioxidant defenses 1997 Cold Spring Harbor Laboratory Press New York 667 713
    • (1997) Oxidative Stress and the Molecular Biology of Antioxidant Defenses , pp. 667-713
    • Mullineaux, P.M.1    Creissen, G.P.2
  • 28
    • 0027490876 scopus 로고
    • Purification and characterization of glutathione reductase from Chlamydomonas reinhardtii
    • T. Takeda, T. Isikawa, S. Shigeoka, O. Hirayama, and T. Mitsunaga Purification and characterization of glutathione reductase from Chlamydomonas reinhardtii J. Gen. Microbiol. 139 1993 2233 2238
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 2233-2238
    • Takeda, T.1    Isikawa, T.2    Shigeoka, S.3    Hirayama, O.4    Mitsunaga, T.5
  • 29
    • 0017165455 scopus 로고
    • Glutathione reductase from human erythrocytes. Catalytic properties and aggregation
    • D.J. Worthington, and M.A. Rosemeyer Glutathione reductase from human erythrocytes. Catalytic properties and aggregation Eur. J. Biochem. 67 1976 231 238
    • (1976) Eur. J. Biochem. , vol.67 , pp. 231-238
    • Worthington, D.J.1    Rosemeyer, M.A.2
  • 30
    • 0025019734 scopus 로고
    • Redesign of the coenzyme specificity of a dehydrogenase by protein engineering
    • N.S. Scrutton, A. Berry, and R.N. Perham Redesign of the coenzyme specificity of a dehydrogenase by protein engineering Nature 343 1990 38 43
    • (1990) Nature , vol.343 , pp. 38-43
    • Scrutton, N.S.1    Berry, A.2    Perham, R.N.3
  • 31
    • 0016526806 scopus 로고
    • Purification and properties of the glutathione reductase of Chromatium vinosum
    • Y.C. Chung, and R.E. Hurlbert Purification and properties of the glutathione reductase of Chromatium vinosum J. Bacteriol. 123 1975 203 211
    • (1975) J. Bacteriol. , vol.123 , pp. 203-211
    • Chung, Y.C.1    Hurlbert, R.E.2
  • 32
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • J.D. Thompson, D.G. Higgins, and T.J. Gibson CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Nucleic Acids Res. 22 1994 4673 4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 33
    • 0033587499 scopus 로고    scopus 로고
    • Probing the kinetic mechanism and coenzyme specificity of glutathione reductase from the cyanobacterium Anabaena PCC 7120 by redesign of the pyridine-nucleotide-binding site
    • U.H. Danielson, F. Jiang, L.O. Hansson, and B. Mannervik Probing the kinetic mechanism and coenzyme specificity of glutathione reductase from the cyanobacterium Anabaena PCC 7120 by redesign of the pyridine-nucleotide-binding site Biochemistry 38 1999 9254 9263
    • (1999) Biochemistry , vol.38 , pp. 9254-9263
    • Danielson, U.H.1    Jiang, F.2    Hansson, L.O.3    Mannervik, B.4
  • 34
    • 0033083420 scopus 로고    scopus 로고
    • Optimized heterologous expression of glutathione reductase from Cyanobacterium anabaena PCC 7120 and characterization of the recombinant protein
    • F. Jiang, and B. Mannervik Optimized heterologous expression of glutathione reductase from Cyanobacterium anabaena PCC 7120 and characterization of the recombinant protein Protein Expr. Purif. 15 1999 92 98
    • (1999) Protein Expr. Purif. , vol.15 , pp. 92-98
    • Jiang, F.1    Mannervik, B.2
  • 36
    • 0036047508 scopus 로고    scopus 로고
    • Regulation of inducible peroxide stress responses
    • S. Mongkolsuk, and J.D. Helmann Regulation of inducible peroxide stress responses Mol. Microbiol. 45 2002 9 15
    • (2002) Mol. Microbiol. , vol.45 , pp. 9-15
    • Mongkolsuk, S.1    Helmann, J.D.2
  • 37
    • 0034944405 scopus 로고    scopus 로고
    • Complex regulation of the organic hydroperoxide resistance gene (ohr) from Xanthomonas involves OhrR, a novel organic peroxide-inducible negative regulator, and posttranscriptional modifications
    • R. Sukchawalit, S. Loprasert, S. Atichartpongkul, and S. Mongkolsuk Complex regulation of the organic hydroperoxide resistance gene (ohr) from Xanthomonas involves OhrR, a novel organic peroxide-inducible negative regulator, and posttranscriptional modifications J. Bacteriol. 183 2001 4405 4412
    • (2001) J. Bacteriol. , vol.183 , pp. 4405-4412
    • Sukchawalit, R.1    Loprasert, S.2    Atichartpongkul, S.3    Mongkolsuk, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.