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Volumn 179, Issue 12, 1997, Pages 3950-3955

Characterization of transcription organization and analysis of unique expression patterns of an alkyl hydroperoxide reductase C gene (ahpC) and the peroxide regulator operon ahpF-oxyR-orfX from Xanthomonas campestris pv. phaseoli

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; CADMIUM CHLORIDE; N ETHYLMALEIMIDE; OXIDOREDUCTASE; PEROXIDE;

EID: 0030974196     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.179.12.3950-3955.1997     Document Type: Article
Times cited : (66)

References (41)
  • 1
    • 0029855070 scopus 로고    scopus 로고
    • General and oxidative stress responses in Bacillus subtilis: Cloning, expression, and mutation of the alkyl hydroperoxide reductase operon
    • Antelmann, H., S. Engelmann, R. Schmid, and M. Hecker. 1996. General and oxidative stress responses in Bacillus subtilis: cloning, expression, and mutation of the alkyl hydroperoxide reductase operon. J. Bacteriol. 178: 6571-6578.
    • (1996) J. Bacteriol. , vol.178 , pp. 6571-6578
    • Antelmann, H.1    Engelmann, S.2    Schmid, R.3    Hecker, M.4
  • 2
    • 0029144017 scopus 로고
    • A homologue to the Escherichia coli alkyl hydroperoxide reductase AhpC is induced by osmotic up shock in Staphylococcus aureus
    • Armstrong-Buisseret, L., M. B. Cole, and G. S. Stewart. 1995. A homologue to the Escherichia coli alkyl hydroperoxide reductase AhpC is induced by osmotic up shock in Staphylococcus aureus. Microbiology 141:1655-1661.
    • (1995) Microbiology , vol.141 , pp. 1655-1661
    • Armstrong-Buisseret, L.1    Cole, M.B.2    Stewart, G.S.3
  • 3
    • 0029854169 scopus 로고    scopus 로고
    • Mutation of the Bacillus subtilis alkyl hydroperoxide reductase (ahpCF) operon reveals compensatory interactions among hydrogen peroxide stress genes
    • Basat, N., L. Chen, and J. D. Helmann. 1996. Mutation of the Bacillus subtilis alkyl hydroperoxide reductase (ahpCF) operon reveals compensatory interactions among hydrogen peroxide stress genes. J. Bacteriol. 178:6579-6586.
    • (1996) J. Bacteriol. , vol.178 , pp. 6579-6586
    • Basat, N.1    Chen, L.2    Helmann, J.D.3
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0028226006 scopus 로고
    • Cloning and sequencing of thiol-specific antioxidant from mammalian brain: Alkyl hydroperoxide reductase and thiol specific antioxidant define a large family of antioxidant enzymes
    • Chae, H. Z., K. Robinson, L. B. Poole, G. Church, G. Storz, and S. G. Rhee. 1994. Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol specific antioxidant define a large family of antioxidant enzymes. Proc. Natl. Acad. Sci. USA 91:7017-7021.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7017-7021
    • Chae, H.Z.1    Robinson, K.2    Poole, L.B.3    Church, G.4    Storz, G.5    Rhee, S.G.6
  • 6
    • 0028229670 scopus 로고
    • Dimerization of thiol-specific antioxidant and the essential role of cysteine 47
    • Chae, H. Z., T. B. Uhm, and S. G. Rhee. 1994. Dimerization of thiol-specific antioxidant and the essential role of cysteine 47. Proc. Natl. Acad. Sci. USA 91:7022-7026.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7022-7026
    • Chae, H.Z.1    Uhm, T.B.2    Rhee, S.G.3
  • 7
    • 0028837261 scopus 로고
    • Unusual growth phase and oxygen tension regulation of oxidative stress protection enzymes, catalase and superoxide dismutase, in the phytopathogen Xanthomonas oryzae pv. oryzac
    • Chamnongpol, S., S. Mongkolsuk, P. Vattanaviboon, and M. Fuangthong. 1995. Unusual growth phase and oxygen tension regulation of oxidative stress protection enzymes, catalase and superoxide dismutase, in the phytopathogen Xanthomonas oryzae pv. oryzac. Appl. Environ. Microbiol. 61:393-396.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 393-396
    • Chamnongpol, S.1    Mongkolsuk, S.2    Vattanaviboon, P.3    Fuangthong, M.4
  • 8
    • 0029160467 scopus 로고
    • Atypical oxidative stress regulation of a Xanthomonas oryzae pv. oryzae monofunctional catalase
    • Chamnongpol, S., P. Vattanaviboon, S. Loprasert, and S. Mongkolsuk. 1995. Atypical oxidative stress regulation of a Xanthomonas oryzae pv. oryzae monofunctional catalase. Can. J. Microbiol. 41:541-547.
    • (1995) Can. J. Microbiol. , vol.41 , pp. 541-547
    • Chamnongpol, S.1    Vattanaviboon, P.2    Loprasert, S.3    Mongkolsuk, S.4
  • 9
    • 0029152774 scopus 로고
    • Coordinate regulation of Bacillus subtilis peroxide stress genes by hydrogen peroxide and metal ions
    • Chen, L., L. Keramati, and J. D. Helmann. 1995. Coordinate regulation of Bacillus subtilis peroxide stress genes by hydrogen peroxide and metal ions. Proc. Natl. Acad. Sci. USA 92:8190-8194.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8190-8194
    • Chen, L.1    Keramati, L.2    Helmann, J.D.3
  • 10
    • 0021930684 scopus 로고
    • Positive control of a regulon for a defense against oxidative stress and some heat shock proteins in Salmonella typhimurium
    • Christman, M. F., R. W. Morgan, F. S. Jacobson, and B. N. Ames. 1985. Positive control of a regulon for a defense against oxidative stress and some heat shock proteins in Salmonella typhimurium. Cell 41:753-762.
    • (1985) Cell , vol.41 , pp. 753-762
    • Christman, M.F.1    Morgan, R.W.2    Jacobson, F.S.3    Ames, B.N.4
  • 11
    • 0026335852 scopus 로고
    • Regulation of bacterial oxidative stress genes
    • Demple, B. 1991. Regulation of bacterial oxidative stress genes. Annu. Rev. Genet. 25:315-337.
    • (1991) Annu. Rev. Genet. , vol.25 , pp. 315-337
    • Demple, B.1
  • 12
    • 0028882958 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis is a natural mutant with an inactivated oxidative-stress regulatory gene: Implications for sensitivity to isoniazid
    • Deretic, V., W. Philipp, S. Dhandayuthapani, M. H. Mudd, R. Curcic, T. Garbe, B. Heym, L. E. Via, and S. T. Cole. 1996. Mycobacterium tuberculosis is a natural mutant with an inactivated oxidative-stress regulatory gene: implications for sensitivity to isoniazid. Mol. Microbiol. 17:889-900.
    • (1996) Mol. Microbiol. , vol.17 , pp. 889-900
    • Deretic, V.1    Philipp, W.2    Dhandayuthapani, S.3    Mudd, M.H.4    Curcic, R.5    Garbe, T.6    Heym, B.7    Via, L.E.8    Cole, S.T.9
  • 13
    • 0029888258 scopus 로고    scopus 로고
    • Oxidative stress response and its role in sensitivity to isoniazid in mycobacteria: Characterization and inducibility of ahpC by peroxides in Mycobacterium smegmatis and lack of expression in M. aurum and M. tuberculosis
    • Dhandayuthapani, S., Y. Zhang, M. H. Mudd, and V. Deretic. 1996. Oxidative stress response and its role in sensitivity to isoniazid in mycobacteria: characterization and inducibility of ahpC by peroxides in Mycobacterium smegmatis and lack of expression in M. aurum and M. tuberculosis. J. Bacteriol. 178:3641-3649.
    • (1996) J. Bacteriol. , vol.178 , pp. 3641-3649
    • Dhandayuthapani, S.1    Zhang, Y.2    Mudd, M.H.3    Deretic, V.4
  • 14
    • 0025786078 scopus 로고
    • Oxidative stress responses in Escherichia coli and Salmonella typhimurium
    • Farr, S. B., and T. Kogoma. 1991. Oxidative stress responses in Escherichia coli and Salmonella typhimurium. Microbiol. Rev. 55:561-585.
    • (1991) Microbiol. Rev. , vol.55 , pp. 561-585
    • Farr, S.B.1    Kogoma, T.2
  • 15
    • 0029018721 scopus 로고
    • Metabolic sources of hydrogen peroxide in aerobically growing Escherichia coli
    • Gonzalez-Flecha, B., and B. D. Demple. 1995. Metabolic sources of hydrogen peroxide in aerobically growing Escherichia coli. J. Biol. Chem. 270:13681-13687.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13681-13687
    • Gonzalez-Flecha, B.1    Demple, B.D.2
  • 16
    • 0024343602 scopus 로고
    • A global response induced in Escherichia coli by redox-cycling agents overlaps with that induced by peroxide stress
    • Greenberg, J. T., and B. Demple. 1989. A global response induced in Escherichia coli by redox-cycling agents overlaps with that induced by peroxide stress. J. Bacteriol. 171:3933-3939.
    • (1989) J. Bacteriol. , vol.171 , pp. 3933-3939
    • Greenberg, J.T.1    Demple, B.2
  • 17
    • 0018666716 scopus 로고
    • Intracellular production of superoxide radical and of hydrogen peroxide by redox active compounds
    • Hassan, H. M., and I. Fridovich. 1979. Intracellular production of superoxide radical and of hydrogen peroxide by redox active compounds. Arch. Biochem. Biophys. 196:385-395.
    • (1979) Arch. Biochem. Biophys. , vol.196 , pp. 385-395
    • Hassan, H.M.1    Fridovich, I.2
  • 19
    • 0024599904 scopus 로고
    • An alkyl hydroperoxide reductase involved in the defense of DNA against oxidative damage: Purification and properties
    • Jacobson, F. S., R. W. Morgan, M. F. Christman, and B. N. Ames. 1989. An alkyl hydroperoxide reductase involved in the defense of DNA against oxidative damage: purification and properties. J. Biol. Chem. 264:1488-1496.
    • (1989) J. Biol. Chem. , vol.264 , pp. 1488-1496
    • Jacobson, F.S.1    Morgan, R.W.2    Christman, M.F.3    Ames, B.N.4
  • 20
    • 0028930138 scopus 로고
    • Mutation analysis of the redox-sensitive transcriptional regulator OxyR: Regions important for DNA binding and multimerization
    • Kullik, I., J. Stevens, M. B. Toledano, and G. Storz. 1995. Mutation analysis of the redox-sensitive transcriptional regulator OxyR: regions important for DNA binding and multimerization. J. Bacteriol. 177:1285-1291.
    • (1995) J. Bacteriol. , vol.177 , pp. 1285-1291
    • Kullik, I.1    Stevens, J.2    Toledano, M.B.3    Storz, G.4
  • 21
    • 0028965108 scopus 로고
    • Mutation analysis of the redox-sensitive transcriptional regulator OxyR: Regions important for oxidation and transcriptional activation
    • Kullik, I., M. B. Toledano, L. A. Tartaglia, and G. Storz. 1995. Mutation analysis of the redox-sensitive transcriptional regulator OxyR: regions important for oxidation and transcriptional activation. J. Bacteriol. 177:1275-1284.
    • (1995) J. Bacteriol. , vol.177 , pp. 1275-1284
    • Kullik, I.1    Toledano, M.B.2    Tartaglia, L.A.3    Storz, G.4
  • 22
    • 0028171293 scopus 로고
    • 2, from oxidative burst orchestrates the plant hypersensitive disease resistance response
    • 2, from oxidative burst orchestrates the plant hypersensitive disease resistance response. Cell 79:583-593.
    • (1994) Cell , vol.79 , pp. 583-593
    • Levine, A.1    Tenhaken, R.2    Dixon, R.3    Lamb, C.4
  • 23
    • 0031038988 scopus 로고    scopus 로고
    • Identification of a penicillin-binding protein 3 homolog, PBP3x, in Pseudomonas aeruginosa: Gene cloning and growth phase-dependent expression
    • Liao, X., and R. E. W. Hancock. 1997. Identification of a penicillin-binding protein 3 homolog, PBP3x, in Pseudomonas aeruginosa: gene cloning and growth phase-dependent expression. J. Bacteriol. 179:1490-1496.
    • (1997) J. Bacteriol. , vol.179 , pp. 1490-1496
    • Liao, X.1    Hancock, R.E.W.2
  • 24
    • 0031008472 scopus 로고    scopus 로고
    • Isolation and analysis of the Xanthomonas alkyl hydroperoxide reductase gene and the peroxide sensor regulator genes ahpC and ahpF-oxyR-orfX
    • Loprasert, S., S. Atichartpongkun, W. Whangsuk, and S. Mongkolsuk. 1997. Isolation and analysis of the Xanthomonas alkyl hydroperoxide reductase gene and the peroxide sensor regulator genes ahpC and ahpF-oxyR-orfX. J. Bacteriol. 179:3944-3949.
    • (1997) J. Bacteriol. , vol.179 , pp. 3944-3949
    • Loprasert, S.1    Atichartpongkun, S.2    Whangsuk, W.3    Mongkolsuk, S.4
  • 25
    • 0030574264 scopus 로고    scopus 로고
    • Regulation of oxidative stress protective enzymes, catalase and superoxide dismutase in Xanthomonas - A review
    • Loprasert, S., P. Vattanaviboon, W. Praituan, S. Chamnongpol, and S. Mongkolsuk. 1996. Regulation of oxidative stress protective enzymes, catalase and superoxide dismutase in Xanthomonas - a review. Gene 179:33-37.
    • (1996) Gene , vol.179 , pp. 33-37
    • Loprasert, S.1    Vattanaviboon, P.2    Praituan, W.3    Chamnongpol, S.4    Mongkolsuk, S.5
  • 27
    • 85036444184 scopus 로고    scopus 로고
    • Unpublished observations
    • Mongkolsuk, S. Unpublished observations.
    • Mongkolsuk, S.1
  • 29
    • 0031028846 scopus 로고    scopus 로고
    • Induced adaptive and cross protection responses against oxidative stress killing in a bacterial phytopathogen, Xanthomonas oryzae pv. oryzae
    • Mongkolsuk, S., P. Vattanaviboon, and W. Praituan. 1997. Induced adaptive and cross protection responses against oxidative stress killing in a bacterial phytopathogen, Xanthomonas oryzae pv. oryzae. FEMS Microbiol. Lett. 146: 217-222.
    • (1997) FEMS Microbiol. Lett. , vol.146 , pp. 217-222
    • Mongkolsuk, S.1    Vattanaviboon, P.2    Praituan, W.3
  • 30
    • 0004080812 scopus 로고
    • CAB International, Tucson, Ariz.
    • Ou, S. H. (ed.). 1987. Rice diseases, p. 66-96. CAB International, Tucson, Ariz.
    • (1987) Rice Diseases , pp. 66-96
    • Ou, S.H.1
  • 31
    • 0030066091 scopus 로고    scopus 로고
    • Flavin-dependent alkyl hydroperoxide reductase from Salmonella typhimurium. 2. Cysteine disulphides involved in catalysis of peroxide reduction
    • Poole, L. B. 1996. Flavin-dependent alkyl hydroperoxide reductase from Salmonella typhimurium. 2. Cysteine disulphides involved in catalysis of peroxide reduction. Biochemistry 35:65-75.
    • (1996) Biochemistry , vol.35 , pp. 65-75
    • Poole, L.B.1
  • 32
    • 0030032612 scopus 로고    scopus 로고
    • Flavin-dependent alkyl hydroperoxide reductase from Salmonella typhimurium. 1. Purification and enzymatic activities of over expressed AhpF and AhpC proteins
    • Poole, L. B., and H. R. Ellis. 1996. Flavin-dependent alkyl hydroperoxide reductase from Salmonella typhimurium. 1. Purification and enzymatic activities of over expressed AhpF and AhpC proteins. Biochemistry 35:56-64.
    • (1996) Biochemistry , vol.35 , pp. 56-64
    • Poole, L.B.1    Ellis, H.R.2
  • 33
    • 0025214239 scopus 로고
    • Use of saturation mutagenesis to localize probable functional domains in the NahR protein, a LysR type transcriptional activator
    • Schell, M. A., P. H. Brown, and S. Raju. 1990. Use of saturation mutagenesis to localize probable functional domains in the NahR protein, a LysR type transcriptional activator. J. Biol. Chem. 265:3844-3850.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3844-3850
    • Schell, M.A.1    Brown, P.H.2    Raju, S.3
  • 36
    • 0024604234 scopus 로고
    • An alkyl hydroperoxide reductase induced by oxidative stress in Salmonella typhimurium and Escherichia coli: Genetic characterization and cloning of ahp
    • Storz, G., F. S. Jacobson, L. A. Tartaglia, R. W. Morgan, L. A. Silveira, and B. N. Ames. 1989. An alkyl hydroperoxide reductase induced by oxidative stress in Salmonella typhimurium and Escherichia coli: genetic characterization and cloning of ahp. J. Bacteriol. 171:2049-2055.
    • (1989) J. Bacteriol. , vol.171 , pp. 2049-2055
    • Storz, G.1    Jacobson, F.S.2    Tartaglia, L.A.3    Morgan, R.W.4    Silveira, L.A.5    Ames, B.N.6
  • 37
    • 0025214474 scopus 로고
    • Transcriptional regulator of oxidative stress-inducible genes: Direct activation by oxidation
    • Storz, G., L. A. Tartaglia, and B. N. Ames. 1990. Transcriptional regulator of oxidative stress-inducible genes: direct activation by oxidation. Science 248: 189-194.
    • (1990) Science , vol.248 , pp. 189-194
    • Storz, G.1    Tartaglia, L.A.2    Ames, B.N.3
  • 38
    • 0007926680 scopus 로고
    • The generation of oxygen radicals during host plant response to infection
    • Sutherland, M. W. 1991. The generation of oxygen radicals during host plant response to infection. Physiol. Mol. Plant. Pathol. 39:79-93.
    • (1991) Physiol. Mol. Plant. Pathol. , vol.39 , pp. 79-93
    • Sutherland, M.W.1
  • 39
    • 0029034529 scopus 로고
    • Cloning of a Corynebacterium diphtheriae iron-repressible gene that shares homology with the AhpC subunit of alkyl hydroperoxide reductase of Salmonella typhimurium
    • Tai, S. S., and Y. Y. Zhu. 1995. Cloning of a Corynebacterium diphtheriae iron-repressible gene that shares homology with the AhpC subunit of alkyl hydroperoxide reductase of Salmonella typhimurium. J. Bacteriol. 177:3512-3517.
    • (1995) J. Bacteriol. , vol.177 , pp. 3512-3517
    • Tai, S.S.1    Zhu, Y.Y.2
  • 40
    • 0028807191 scopus 로고
    • Growth phase dependent resistance to oxidative stress in a phytopathogen Xanthomonas oryzae pv oryzae
    • Vattanaviboon, P., W. Praituan, and S. Mongkolsuk. 1995. Growth phase dependent resistance to oxidative stress in a phytopathogen Xanthomonas oryzae pv oryzae. Can. J. Microbiol. 41:1043-1045.
    • (1995) Can. J. Microbiol. , vol.41 , pp. 1043-1045
    • Vattanaviboon, P.1    Praituan, W.2    Mongkolsuk, S.3
  • 41
    • 0029915633 scopus 로고    scopus 로고
    • ahpC, a gene involved in isoniazid resistance of the Mycobacterium tuberculosis complex
    • Wilson, T. M., and D. M. Collins. 1996. ahpC, a gene involved in isoniazid resistance of the Mycobacterium tuberculosis complex. Mol. Microbiol. 19: 1025-1034.
    • (1996) Mol. Microbiol. , vol.19 , pp. 1025-1034
    • Wilson, T.M.1    Collins, D.M.2


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