메뉴 건너뛰기




Volumn 19, Issue 1, 2003, Pages 29-41

Polyamines reduce paraquat-induced soxS and its regulon expression in Escherichia coli

Author keywords

Escherichia coli; Oxidative stress; Paraquat; Polyamines; sodA; soxS; zwf

Indexed keywords

GLUCOSE 6 PHOSPHATE DEHYDROGENASE; MANGANESE SUPEROXIDE DISMUTASE; PARAQUAT; POLYAMINE; PUTRESCINE; SPERMIDINE;

EID: 0037294954     PISSN: 07422091     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1022065614490     Document Type: Article
Times cited : (12)

References (36)
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976;72:248-54.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.1
  • 3
    • 0030844766 scopus 로고    scopus 로고
    • Cysteine-to-alanine replacements in the Escherichia coli SoxR protein and the role of the [2Fe-2S] centers in transcriptional activation
    • Bradley TM, Hidalgo E, Leautaud V, Ding H, Demple B. Cysteine-to-alanine replacements in the Escherichia coli SoxR protein and the role of the [2Fe-2S] centers in transcriptional activation. Nucleic Acids Res. 1997;25:1469-75.
    • (1997) Nucleic Acids Res , vol.25 , pp. 1469-1475
    • Bradley, T.M.1    Hidalgo, E.2    Leautaud, V.3    Ding, H.4    Demple, B.5
  • 4
    • 0022683672 scopus 로고
    • Isolation of superoxide dismutase mutants in Escherichia coli: Is superoxide dismutase necessary for aerobic life?
    • Carlioz A, Touati D. Isolation of superoxide dismutase mutants in Escherichia coli: is superoxide dismutase necessary for aerobic life? EMBO J. 1986;5:623-30.
    • (1986) EMBO J , vol.5 , pp. 623-630
    • Carlioz, A.1    Touati, D.2
  • 5
    • 0030574274 scopus 로고    scopus 로고
    • Redox signaling and gene control in the Escherichia coli:soxRS oxidative stress regulon - A review
    • Demple B. Redox signaling and gene control in the Escherichia coli:soxRS oxidative stress regulon - a review. Gene. 1996;179:53-7.
    • (1996) Gene , vol.179 , pp. 53-57
    • Demple, B.1
  • 6
    • 0030795788 scopus 로고    scopus 로고
    • In vivo kinetics of a redox-regulated transcriptional switch
    • Ding H, Demple B. In vivo kinetics of a redox-regulated transcriptional switch. Proc Natl Acad Sci USA. 1997;94:8445-9.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 8445-8449
    • Ding, H.1    Demple, B.2
  • 7
    • 0030448704 scopus 로고    scopus 로고
    • The redox state of the [2Fe-2S] clusters in SoxR protein regulates its activity as a transcription factor
    • Ding H, Hidalgo E, Demple B. The redox state of the [2Fe-2S] clusters in SoxR protein regulates its activity as a transcription factor. J Biol Chem. 1996;3271:33173-5.
    • (1996) J Biol Chem , vol.3271 , pp. 33173-33175
    • Ding, H.1    Hidalgo, E.2    Demple, B.3
  • 8
    • 0028908084 scopus 로고
    • Genetic definition of the Escherichia coli zwf "Soxbox," the DNA binding site for SoxS-mediated induction of glucose 6-phosphate dehydrogenase in response to superoxide
    • Fawcett WP, Wolf RE Jr. Genetic definition of the Escherichia coli zwf "Soxbox," the DNA binding site for SoxS-mediated induction of glucose 6-phosphate dehydrogenase in response to superoxide. J Bacteriol. 1995;177:1742-50.
    • (1995) J Bacteriol , vol.177 , pp. 1742-1750
    • Fawcett, W.P.1    Wolf R.E., Jr.2
  • 9
    • 0015496178 scopus 로고
    • Evidence that superoxide dismutase plays a role in protecting red blood cells against peroxidative hemolysis
    • Fee JA, Teitelbaum HD. Evidence that superoxide dismutase plays a role in protecting red blood cells against peroxidative hemolysis. Biochem Biophys Res Commun. 1972;49:150-8.
    • (1972) Biochem Biophys Res Commun , vol.49 , pp. 150-158
    • Fee, J.A.1    Teitelbaum, H.D.2
  • 10
    • 0034020742 scopus 로고    scopus 로고
    • Flavodoxin mutants of Escherichia coli K-12
    • Gaudu P, Weiss B. Flavodoxin mutants of Escherichia coli K-12. J Bacteriol. 2000;182:1788-93.
    • (2000) J Bacteriol , vol.182 , pp. 1788-1793
    • Gaudu, P.1    Weiss, B.2
  • 11
    • 0029790760 scopus 로고    scopus 로고
    • SoxR, a [2Fe-2S] transcription factor, is active only in its oxidized form
    • Gaudu P, Weiss B. SoxR, a [2Fe-2S] transcription factor, is active only in its oxidized form. Proc Natl Acad Sci USA. 1996;93:10094-8.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 10094-10098
    • Gaudu, P.1    Weiss, B.2
  • 12
    • 0031938051 scopus 로고    scopus 로고
    • Balance between endogenous superoxide stress and antioxidant defenses
    • Gort AS, Imlay JA. Balance between endogenous superoxide stress and antioxidant defenses. J Bacteriol. 1998;180:1402-10.
    • (1998) J Bacteriol , vol.180 , pp. 1402-1410
    • Gort, A.S.1    Imlay, J.A.2
  • 13
    • 0025078495 scopus 로고
    • Positive control of a global antioxidant defense regulon activated by superoxide-generating agents in Escherichia coli
    • Greenberg JT, Monach P, Chou JH, Josephy PD, Demple B. Positive control of a global antioxidant defense regulon activated by superoxide-generating agents in Escherichia coli. Proc Natl Acad Sci USA. 1990;87:6181-5.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 6181-6185
    • Greenberg, J.T.1    Monach, P.2    Chou, J.H.3    Josephy, P.D.4    Demple, B.5
  • 15
    • 0018633031 scopus 로고
    • Mutants of Escherichia coli that do not contain 1,4-diaminobutane (putrescine) or spermidine
    • Hafner EW, Tabor CW, Tabor H. Mutants of Escherichia coli that do not contain 1,4-diaminobutane (putrescine) or spermidine. J Biol Chem. 1979;254:12419-26.
    • (1979) J Biol Chem , vol.254 , pp. 12419-12426
    • Hafner, E.W.1    Tabor, C.W.2    Tabor, H.3
  • 16
    • 0030991281 scopus 로고    scopus 로고
    • High-performance liquid chromatographic determination of biogenic amines in fish implicated in food poisoning
    • Hwang D-F, Chang S-H, Shiua C-Y, Chai T-J. High-performance liquid chromatographic determination of biogenic amines in fish implicated in food poisoning. J Chrom. 1997;693:23-9.
    • (1997) J Chrom , vol.693 , pp. 23-29
    • Hwang, D.-F.1    Chang, S.-H.2    Shiua, C.-Y.3    Chai, T.-J.4
  • 17
    • 0034685624 scopus 로고    scopus 로고
    • Polyamines: Mysterious modulators of cellular functions
    • Igarashi K, Kashiwagi K. Polyamines: mysterious modulators of cellular functions. Biochem Biophys Res Commun. 2000;271:559-64.
    • (2000) Biochem Biophys Res Commun , vol.271 , pp. 559-564
    • Igarashi, K.1    Kashiwagi, K.2
  • 18
    • 0033944773 scopus 로고    scopus 로고
    • SOS induction of the recA gene by UV-, gamma- irradiation and mitomycin C is mediated by polyamines in Escherichia coli K-12
    • Kim IG, Oh TJ. SOS induction of the recA gene by UV-, gamma- irradiation and mitomycin C is mediated by polyamines in Escherichia coli K-12. Toxicol Lett. 2000;116:143-9.
    • (2000) Toxicol Lett , vol.116 , pp. 143-149
    • Kim, I.G.1    Oh, T.J.2
  • 19
    • 0033515449 scopus 로고    scopus 로고
    • Induction of the soxRS regulon of Escherichia coli by superoxide
    • Liochev SI, Benov L, Touati D, Fridovich I. Induction of the soxRS regulon of Escherichia coli by superoxide. J Biol Chem. 1999;274:9479-81.
    • (1999) J Biol Chem , vol.274 , pp. 9479-9481
    • Liochev, S.I.1    Benov, L.2    Touati, D.3    Fridovich, I.4
  • 20
    • 0343776197 scopus 로고    scopus 로고
    • Role of reactive oxygen species in apoptosis: Implications for cancer therapy
    • Matés JM, Sánchez-Jiménes FM. Role of reactive oxygen species in apoptosis: implications for cancer therapy. Int J Biochem Cell Biol. 2000;32:157-70.
    • (2000) Int J Biochem Cell Biol , vol.32 , pp. 157-170
    • Matés, J.M.1    Sánchez-Jiménes, F.M.2
  • 21
    • 0003785155 scopus 로고
    • Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Miller JH. Experiments in molecular genetics. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press; 1972.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 22
    • 0029831354 scopus 로고    scopus 로고
    • Overlaps and parallels in the regulation of intrinsic multiple-antibiotic resistance in Escherichia coli
    • Miller PF, Sulavik MC. Overlaps and parallels in the regulation of intrinsic multiple-antibiotic resistance in Escherichia coli. Mol Microbiol. 1996;21:441-8.
    • (1996) Mol Microbiol , vol.21 , pp. 441-448
    • Miller, P.F.1    Sulavik, M.C.2
  • 23
    • 0025305215 scopus 로고
    • Paraquat toxicity is increased in Escherichia coli defective in the synthesis of polyamines
    • Minton KW, Tabor H, Tabor CW. Paraquat toxicity is increased in Escherichia coli defective in the synthesis of polyamines. Proc Natl Acad Sci USA. 1990;87:2851-5.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 2851-2855
    • Minton, K.W.1    Tabor, H.2    Tabor, C.W.3
  • 24
    • 0029339931 scopus 로고
    • soxRS gene increased the level of organic solvent tolerance in Escherichia coli
    • Nakajima H, Kobayashi M, Negishi T, Aono R. soxRS gene increased the level of organic solvent tolerance in Escherichia coli. Biosci Biotechnol Biochem. 1995;59:1323-5.
    • (1995) Biosci Biotechnol Biochem , vol.59 , pp. 1323-1325
    • Nakajima, H.1    Kobayashi, M.2    Negishi, T.3    Aono, R.4
  • 25
    • 0027440247 scopus 로고
    • Activation by nitric oxide of an oxidative-stress response that defends Escherichia coli against activated macrophages
    • Nunoshiba T, deRojas-Walker T, Wishnok JS, Tannenbaum SR, Demple B. Activation by nitric oxide of an oxidative-stress response that defends Escherichia coli against activated macrophages. Proc Natl Acad Sci USA. 1993;90:9993-7.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 9993-9997
    • Nunoshiba, T.1    DeRojas-Walker, T.2    Wishnok, J.S.3    Tannenbaum, S.R.4    Demple, B.5
  • 26
    • 0033503192 scopus 로고    scopus 로고
    • The SOS induction of umu'-lacZ fusion gene by oxidative damage is influenced by polyamines in Escherichia coli
    • Oh TJ, Kim IG. The SOS induction of umu'-lacZ fusion gene by oxidative damage is influenced by polyamines in Escherichia coli. Cell Biol Toxicol. 1999;15:291-7.
    • (1999) Cell Biol Toxicol , vol.15 , pp. 291-297
    • Oh, T.J.1    Kim, I.G.2
  • 27
    • 0024547664 scopus 로고
    • Null mutation of copper/zinc superoxide dismutase in Drosophila confers hypersensitivity to paraquat and reduced longevity
    • Phillips JP, Campbell SD, Michaud D, Charbonneau M, Hilliker AJ. Null mutation of copper/zinc superoxide dismutase in Drosophila confers hypersensitivity to paraquat and reduced longevity. Proc Natl Acad Sci USA. 1989;86:2761-5.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 2761-2765
    • Phillips, J.P.1    Campbell, S.D.2    Michaud, D.3    Charbonneau, M.4    Hilliker, A.J.5
  • 28
    • 0035283587 scopus 로고    scopus 로고
    • Redox-operated genetic switches: The SoxR and OxyR transcription factors
    • Pomposiello PJ, Demple B. Redox-operated genetic switches: the SoxR and OxyR transcription factors. Trends Biotechnol. 2001;19:109-14.
    • (2001) Trends Biotechnol , vol.19 , pp. 109-114
    • Pomposiello, P.J.1    Demple, B.2
  • 29
    • 0034977251 scopus 로고    scopus 로고
    • Genome-wide transcriptional profiling of the Escherichia coli responses to superoxide stress and sodium salicylate
    • Pomposiello PJ, Bennik MH, Demple B. Genome-wide transcriptional profiling of the Escherichia coli responses to superoxide stress and sodium salicylate. J Bacteriol. 2001;183:3890-902.
    • (2001) J Bacteriol , vol.183 , pp. 3890-3902
    • Pomposiello, P.J.1    Bennik, M.H.2    Demple, B.3
  • 30
    • 0038957365 scopus 로고    scopus 로고
    • Transcriptional regulation of glutaredoxin and thioredoxin pathways and related enzymes in response to oxidative stress
    • Prieto-Alamo MJ, Jurado J, Gallardo-Madueno R, Monje-Casas F, Holmgren A, Pueyo C. Transcriptional regulation of glutaredoxin and thioredoxin pathways and related enzymes in response to oxidative stress. J Biol Chem. 2000;275:13398-405.
    • (2000) J Biol Chem , vol.275 , pp. 13398-13405
    • Prieto-Alamo, M.J.1    Jurado, J.2    Gallardo-Madueno, R.3    Monje-Casas, F.4    Holmgren, A.5    Pueyo, C.6
  • 32
    • 0034923283 scopus 로고    scopus 로고
    • The role of the natural polyamine putrescine in defense against oxidative stress in Escherichia coli
    • Tkachenko A, Nesterova L, Pshenichnov M. The role of the natural polyamine putrescine in defense against oxidative stress in Escherichia coli. Arch Microbiol. 2001;176:155-7.
    • (2001) Arch Microbiol , vol.176 , pp. 155-157
    • Tkachenko, A.1    Nesterova, L.2    Pshenichnov, M.3
  • 33
    • 0025369726 scopus 로고
    • soxR, a locus governing a superoxide response regulon in Escherichia coli K-12
    • Tsaneva IR, Weiss B. soxR, a locus governing a superoxide response regulon in Escherichia coli K-12. J Bacteriol. 1990;172:4197-205.
    • (1990) J Bacteriol , vol.172 , pp. 4197-4205
    • Tsaneva, I.R.1    Weiss, B.2
  • 34
    • 0025809949 scopus 로고
    • Two divergently transcribed genes, soxR and soxS, control a superoxide response regulon of Escherichia coli
    • Wu J, Weiss B. Two divergently transcribed genes, soxR and soxS, control a superoxide response regulon of Escherichia coli. J Bacteriol. 1991;173:2864-71.
    • (1991) J Bacteriol , vol.173 , pp. 2864-2871
    • Wu, J.1    Weiss, B.2
  • 35
    • 0035282733 scopus 로고    scopus 로고
    • Role of spermine in amyloid beta-peptide-associated free radical-induced neurotoxicity
    • Yatin SM, Yatin M, Varadarajan S, Ain KB, Butterfield DA. Role of spermine in amyloid beta-peptide-associated free radical-induced neurotoxicity. J Neurosci Res. 2001;63:395-401.
    • (2001) J Neurosci Res , vol.63 , pp. 395-401
    • Yatin, S.M.1    Yatin, M.2    Varadarajan, S.3    Ain, K.B.4    Butterfield, D.A.5
  • 36
    • 0035844218 scopus 로고    scopus 로고
    • Polyamine enhancement of the synthesis of adenylate cyclase at the translational level and the consequential stimulation of the synthesis of the RNA polymerase sigma 28 subunit
    • Yoshida M, Kashiwagi K, Kawai G, Ishihama A, Igarashi K. Polyamine enhancement of the synthesis of adenylate cyclase at the translational level and the consequential stimulation of the synthesis of the RNA polymerase sigma 28 subunit. J Biol Chem. 2001;276:16289-95.
    • (2001) J Biol Chem , vol.276 , pp. 16289-16295
    • Yoshida, M.1    Kashiwagi, K.2    Kawai, G.3    Ishihama, A.4    Igarashi, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.