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Volumn 157, Issue 4, 2011, Pages 957-965

The soxRS response of Escherichia coli can be induced in the absence of oxidative stress and oxygen by modulation of NADPH content

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; FERREDOXIN NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE REDUCTASE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; OXYGEN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SOXRS ENZYME; UNCLASSIFIED DRUG;

EID: 79953716809     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.039461-0     Document Type: Article
Times cited : (60)

References (38)
  • 1
    • 0017397091 scopus 로고
    • Charges of nicotinamide adenine nucleotides and adenylate energy charge as regulatory parameters of the metabolism in Escherichia coli
    • Andersen, K. B. & von Meyenburg, K. (1977). Charges of nicotinamide adenine nucleotides and adenylate energy charge as regulatory parameters of the metabolism in Escherichia coli. J Biol Chem 252, 4151-4156.
    • (1977) J Biol Chem , vol.252 , pp. 4151-4156
    • Andersen, K.B.1    von Meyenburg, K.2
  • 2
    • 3242715114 scopus 로고    scopus 로고
    • Reactive oxygen species: Metabolism, oxidative stress, and signal transduction
    • doi:10.1146/annurev.arplant.55.031903.141701
    • Apel, K. & Hirt, H. (2004). Reactive oxygen species: metabolism, oxidative stress, and signal transduction. Annu Rev Plant Biol 55, 373-399. doi:10.1146/annurev.arplant.55.031903.141701.
    • (2004) Annu Rev Plant Biol , vol.55 , pp. 373-399
    • Apel, K.1    Hirt, H.2
  • 3
    • 43149105201 scopus 로고    scopus 로고
    • Rapid changes in gene expression dynamics in response to superoxide reveal soxRS-dependent and independent transcriptional networks
    • doi:10.1371/journal.pone.0001186
    • Blanchard, J. L., Wholey, W. Y., Conlon, E. M. & Pomposiello, P. J. (2007). Rapid changes in gene expression dynamics in response to superoxide reveal soxRS-dependent and independent transcriptional networks. PLoS ONE 2, e1186. doi:10.1371/journal.pone.0001186.
    • (2007) PLoS ONE , vol.2
    • Blanchard, J.L.1    Wholey, W.Y.2    Conlon, E.M.3    Pomposiello, P.J.4
  • 4
    • 34547781736 scopus 로고    scopus 로고
    • Escherichia coli malic enzymes: Two isoforms with substantial differences in kinetic properties, metabolic regulation, and structure
    • doi:10.1128/JB.00428-07
    • Bologna, F. P., Andreo, C. S. & Drincovich, M. F. (2007). Escherichia coli malic enzymes: two isoforms with substantial differences in kinetic properties, metabolic regulation, and structure. J Bacteriol 189, 5937-5946. doi:10.1128/JB.00428-07.
    • (2007) J Bacteriol , vol.189 , pp. 5937-5946
    • Bologna, F.P.1    Andreo, C.S.2    Drincovich, M.F.3
  • 5
    • 0142211218 scopus 로고    scopus 로고
    • Effects of hydrogen peroxide upon nicotinamide nucleotide metabolism in Escherichia coli: Changes in enzyme levels and nicotinamide nucleotide pools and studies of the oxidation of NAD(P)H by Fe(III)
    • doi:10.1074/jbc.M306251200
    • Brumaghim, J. L., Li, Y., Henle, E. & Linn, S. (2003). Effects of hydrogen peroxide upon nicotinamide nucleotide metabolism in Escherichia coli: changes in enzyme levels and nicotinamide nucleotide pools and studies of the oxidation of NAD(P)H by Fe(III). J Biol Chem 278, 42495-42504. doi:10.1074/jbc.M306251200.
    • (2003) J Biol Chem , vol.278 , pp. 42495-42504
    • Brumaghim, J.L.1    Li, Y.2    Henle, E.3    Linn, S.4
  • 6
    • 0037163878 scopus 로고    scopus 로고
    • Non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase is post-translationally phosphorylated in heterotrophic cells of wheat (Triticum aestivum)
    • doi:10.1016/S0014-5793(02)03455-5
    • Bustos, D. M. & Iglesias, A. A. (2002). Non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase is post-translationally phosphorylated in heterotrophic cells of wheat (Triticum aestivum). FEBS Lett 530, 169-173. doi:10.1016/S0014-5793(02)03455-5.
    • (2002) FEBS Lett , vol.530 , pp. 169-173
    • Bustos, D.M.1    Iglesias, A.A.2
  • 7
    • 0038368151 scopus 로고    scopus 로고
    • + reductase catalytic mechanism
    • doi:10.1046/j.1432-1033.2003.03566.x
    • + reductase catalytic mechanism. Eur J Biochem 270, 1900-1915. doi:10.1046/j.1432-1033.2003.03566.x.
    • (2003) Eur J Biochem , vol.270 , pp. 1900-1915
    • Carrillo, N.1    Ceccarelli, E.A.2
  • 8
    • 9744250924 scopus 로고    scopus 로고
    • Inhibition of pea ferredoxin-NADP(H) reductase by Zn-ferrocyanide
    • doi:10.1111/j.1432-1033.2004.04430.x
    • Catalano Dupuy, D. L., Rial, D. V. & Ceccarelli, E. A. (2004). Inhibition of pea ferredoxin-NADP(H) reductase by Zn-ferrocyanide. Eur J Biochem 271, 4582-4593. doi:10.1111/j.1432-1033.2004.04430.x.
    • (2004) Eur J Biochem , vol.271 , pp. 4582-4593
    • Catalano Dupuy, D.L.1    Rial, D.V.2    Ceccarelli, E.A.3
  • 9
    • 33747082622 scopus 로고    scopus 로고
    • The phenazine pyocyanin is a terminal signalling factor in the quorum sensing network of Pseudomonas aeruginosa
    • doi:10.1111/j.1365-2958.2006.05306.x
    • Dietrich, L. E. P., Price-Whelan, A., Petersen, A., Whiteley, M. & Newman, D. K. (2006). The phenazine pyocyanin is a terminal signalling factor in the quorum sensing network of Pseudomonas aeruginosa. Mol Microbiol 61, 1308-1321. doi:10.1111/j.1365-2958.2006.05306.x.
    • (2006) Mol Microbiol , vol.61 , pp. 1308-1321
    • Dietrich, L.E.P.1    Price-Whelan, A.2    Petersen, A.3    Whiteley, M.4    Newman, D.K.5
  • 10
    • 0030448704 scopus 로고    scopus 로고
    • The redox state of the [2Fe-2S] clusters in SoxR protein regulates its activity as a transcription factor
    • doi:10.1074/jbc.271. 52.33173
    • Ding, H., Hidalgo, E. & Demple, B. (1996). The redox state of the [2Fe-2S] clusters in SoxR protein regulates its activity as a transcription factor. J Biol Chem 271, 33173-33175. doi:10.1074/jbc.271. 52.33173.
    • (1996) J Biol Chem , vol.271 , pp. 33173-33175
    • Ding, H.1    Hidalgo, E.2    Demple, B.3
  • 11
    • 64049099490 scopus 로고    scopus 로고
    • Different biochemical mechanisms ensure network-wide balancing of reducing equivalents in microbial metabolism
    • doi:10.1128/JB.01523-08
    • Fuhrer, T. & Sauer, U. (2009). Different biochemical mechanisms ensure network-wide balancing of reducing equivalents in microbial metabolism. J Bacteriol 191, 2112-2121. doi:10.1128/JB.01523-08.
    • (2009) J Bacteriol , vol.191 , pp. 2112-2121
    • Fuhrer, T.1    Sauer, U.2
  • 12
    • 0028172836 scopus 로고
    • The NADPH: Sulfite reductase of Escherichia coli is a paraquat reductase
    • doi:10.1111/j.1432-1033.1994.tb20070.x
    • Gaudu, P. & Fontecave, M. (1994). The NADPH: sulfite reductase of Escherichia coli is a paraquat reductase. Eur J Biochem 226, 459-463. doi:10.1111/j.1432-1033.1994.tb20070.x.
    • (1994) Eur J Biochem , vol.226 , pp. 459-463
    • Gaudu, P.1    Fontecave, M.2
  • 13
    • 0034008694 scopus 로고    scopus 로고
    • Activation of SoxR by overproduction of desulfoferrodoxin: Multiple ways to induce the soxRS regulon
    • doi:10.1128/JB.182.6.1761-1763.2000
    • Gaudu, P., Dubrac, S. & Touati, D. (2000). Activation of SoxR by overproduction of desulfoferrodoxin: multiple ways to induce the soxRS regulon. J Bacteriol 182, 1761-1763. doi:10.1128/JB.182.6.1761-1763.2000.
    • (2000) J Bacteriol , vol.182 , pp. 1761-1763
    • Gaudu, P.1    Dubrac, S.2    Touati, D.3
  • 14
    • 33645542902 scopus 로고    scopus 로고
    • Glucose-6-phosphate dehydrogenase and ferredoxin-NADP(H) reductase contribute to damage repair during the soxRS response of Escherichia coli
    • doi:10.1099/mic.0.28612-0
    • Giró, M., Carrillo, N. & Krapp, A. R. (2006). Glucose-6-phosphate dehydrogenase and ferredoxin-NADP(H) reductase contribute to damage repair during the soxRS response of Escherichia coli. Microbiology 152, 1119-1128. doi:10.1099/mic.0.28612-0.
    • (2006) Microbiology , vol.152 , pp. 1119-1128
    • Giró, M.1    Carrillo, N.2    Krapp, A.R.3
  • 15
    • 41649117130 scopus 로고    scopus 로고
    • DNA binding shifts the redox potential of the transcription factor SoxR
    • doi:10.1073/pnas.0800093105
    • Gorodetsky, A. A., Dietrich, L. E., Lee, P. E., Demple, B., Newman, D. K. & Barton, J. K. (2008). DNA binding shifts the redox potential of the transcription factor SoxR. Proc Natl Acad Sci U S A 105, 3684-3689. doi:10.1073/pnas.0800093105.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 3684-3689
    • Gorodetsky, A.A.1    Dietrich, L.E.2    Lee, P.E.3    Demple, B.4    Newman, D.K.5    Barton, J.K.6
  • 16
    • 33646724707 scopus 로고    scopus 로고
    • Evidence that feedback inhibition of NAD kinase controls responses to oxidative stress
    • doi:10.1073/pnas. 0602494103
    • Grose, J. H., Joss, L., Velick, S. F. & Roth, J. R. (2006). Evidence that feedback inhibition of NAD kinase controls responses to oxidative stress. Proc Natl Acad Sci U S A 103, 7601-7606. doi:10.1073/pnas. 0602494103.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 7601-7606
    • Grose, J.H.1    Joss, L.2    Velick, S.F.3    Roth, J.R.4
  • 17
    • 31144469460 scopus 로고    scopus 로고
    • Widespread occurrence of non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase among Gram-positive bacteria
    • Iddar, A., Valverde, F., Assobhei, O., Serrano, A. & Soukri, A. (2005). Widespread occurrence of non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase among Gram-positive bacteria. Int Microbiol 8, 251-258.
    • (2005) Int Microbiol , vol.8 , pp. 251-258
    • Iddar, A.1    Valverde, F.2    Assobhei, O.3    Serrano, A.4    Soukri, A.5
  • 18
    • 50649117912 scopus 로고    scopus 로고
    • Cellular defenses against superoxide and hydrogen peroxide
    • doi:10.1146/annurev.biochem. 77.061606.161055
    • Imlay, J. A. (2008). Cellular defenses against superoxide and hydrogen peroxide. Annu Rev Biochem 77, 755-776. doi:10.1146/annurev.biochem. 77.061606.161055.
    • (2008) Annu Rev Biochem , vol.77 , pp. 755-776
    • Imlay, J.A.1
  • 19
    • 0033021117 scopus 로고    scopus 로고
    • Isolation of reductase for SoxR that governs an oxidative response regulon from Escherichia coli
    • doi:10.1016/S0014-5793(99)00565-7
    • Kobayashi, K. & Tagawa, S. (1999). Isolation of reductase for SoxR that governs an oxidative response regulon from Escherichia coli. FEBS Lett 451, 227-230. doi:10.1016/S0014-5793(99)00565-7.
    • (1999) FEBS Lett , vol.451 , pp. 227-230
    • Kobayashi, K.1    Tagawa, S.2
  • 20
    • 0038540118 scopus 로고    scopus 로고
    • A reducing system of the superoxide sensor SoxR in Escherichia coli
    • doi:10.1093/emboj/cdg252
    • Koo, M. S., Lee, J. H., Rah, S. Y., Yeo, W. S., Lee, J. W., Lee, K. L., Koh, Y. S., Kang, S. O. & Roe, J. H. (2003). A reducing system of the superoxide sensor SoxR in Escherichia coli. EMBO J 22, 2614-2622. doi:10.1093/emboj/cdg252.
    • (2003) EMBO J , vol.22 , pp. 2614-2622
    • Koo, M.S.1    Lee, J.H.2    Rah, S.Y.3    Yeo, W.S.4    Lee, J.W.5    Lee, K.L.6    Koh, Y.S.7    Kang, S.O.8    Roe, J.H.9
  • 21
    • 0036175587 scopus 로고    scopus 로고
    • The flavoenzyme ferredoxin (flavodoxin)-NADP(H) reductase modulates NADP(H) homeostasis during the soxRS response of Escherichia coli
    • doi:10. 1128/JB.184.5.1474-1480.2002
    • Krapp, A. R., Rodríguez, R. E., Poli, H. O., Paladini, D. H., Palatnik, J. F. & Carrillo, N. (2002). The flavoenzyme ferredoxin (flavodoxin)-NADP(H) reductase modulates NADP(H) homeostasis during the soxRS response of Escherichia coli. J Bacteriol 184, 1474-1480. doi:10. 1128/JB.184.5.1474-1480.2002.
    • (2002) J Bacteriol , vol.184 , pp. 1474-1480
    • Krapp, A.R.1    Rodríguez, R.E.2    Poli, H.O.3    Paladini, D.H.4    Palatnik, J.F.5    Carrillo, N.6
  • 22
    • 0026778382 scopus 로고
    • Fumarase C, the stable fumarase of Escherichia coli, is controlled by the soxRS regulon
    • doi:10.1073/pnas.89.13.5892
    • Liochev, S. I. & Fridovich, I. (1992). Fumarase C, the stable fumarase of Escherichia coli, is controlled by the soxRS regulon. Proc Natl Acad Sci U S A 89, 5892-5896. doi:10.1073/pnas.89.13.5892.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 5892-5896
    • Liochev, S.I.1    Fridovich, I.2
  • 23
    • 0028140477 scopus 로고
    • NADPH: Ferredoxin oxidoreductase acts as a paraquat diaphorase and is a member of the soxRS regulon
    • doi:10.1073/pnas.91.4.1328
    • Liochev, S. I., Hausladen, A., Beyer, W. F., Jr & Fridovich, I. (1994). NADPH: ferredoxin oxidoreductase acts as a paraquat diaphorase and is a member of the soxRS regulon. Proc Natl Acad Sci U S A 91, 1328-1331. doi:10.1073/pnas.91.4.1328.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 1328-1331
    • Liochev, S.I.1    Hausladen, A.2    Beyer Jr., W.F.3    Fridovich, I.4
  • 24
    • 0034461245 scopus 로고    scopus 로고
    • Hydrogen peroxide activates the soxRS regulon in vivo
    • doi:10. 1128/JB.182.23.6842-6844.2000
    • Manchado, M., Michán, C. & Pueyo, C. (2000). Hydrogen peroxide activates the soxRS regulon in vivo. J Bacteriol 182, 6842-6844. doi:10. 1128/JB.182.23.6842-6844.2000.
    • (2000) J Bacteriol , vol.182 , pp. 6842-6844
    • Manchado, M.1    Michán, C.2    Pueyo, C.3
  • 25
    • 0023787932 scopus 로고
    • pACYC184-derived cloning vectors containing the multiple cloning site and lacZa reporter gene of pUC8/9 and pUC18/19 plasmids
    • doi:10.1016/0378-1119(88)90608-7
    • Martínez, E., Bartolomé, B. & de la Cruz, F. (1988). pACYC184-derived cloning vectors containing the multiple cloning site and lacZa reporter gene of pUC8/9 and pUC18/19 plasmids. Gene 68, 159-162. doi:10.1016/0378-1119(88)90608-7.
    • (1988) Gene , vol.68 , pp. 159-162
    • Martínez, E.1    Bartolomé, B.2    de la Cruz, F.3
  • 27
    • 0026784249 scopus 로고
    • Two-stage control of an oxidative stress regulon: The Escherichia coli SoxR protein triggers redox-inducible expression of the soxS regulatory gene
    • Nunoshiba, T., Hidalgo, E., Amábile Cuevas, C. F. & Demple, B. (1992). Two-stage control of an oxidative stress regulon: the Escherichia coli SoxR protein triggers redox-inducible expression of the soxS regulatory gene. J Bacteriol 174, 6054-6060.
    • (1992) J Bacteriol , vol.174 , pp. 6054-6060
    • Nunoshiba, T.1    Hidalgo, E.2    Amábile Cuevas, C.F.3    Demple, B.4
  • 28
    • 0027440247 scopus 로고
    • Activation by nitric oxide of an oxidativestress response that defends Escherichia coli against activated macrophages
    • doi:10.1073/ pnas.90.21.9993
    • Nunoshiba, T., deRojas-Walker, T., Wishnok, J. S., Tannenbaum, S. R. & Demple, B. (1993). Activation by nitric oxide of an oxidativestress response that defends Escherichia coli against activated macrophages. Proc Natl Acad Sci U S A 90, 9993-9997. doi:10.1073/ pnas.90.21.9993.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 9993-9997
    • Nunoshiba, T.1    deRojas-Walker, T.2    Wishnok, J.S.3    Tannenbaum, S.R.4    Demple, B.5
  • 29
    • 0036134759 scopus 로고    scopus 로고
    • Regulation of the nfsA gene in Escherichia coli by SoxS
    • doi:10.1128/JB.184.1.51-58.2002
    • Paterson, E. S., Boucher, S. E. & Lambert, I. B. (2002). Regulation of the nfsA gene in Escherichia coli by SoxS. J Bacteriol 184, 51-58. doi:10.1128/JB.184.1.51-58.2002.
    • (2002) J Bacteriol , vol.184 , pp. 51-58
    • Paterson, E.S.1    Boucher, S.E.2    Lambert, I.B.3
  • 30
    • 0034977251 scopus 로고    scopus 로고
    • Genome-wide transcriptional profiling of the Escherichia coli responses to superoxide stress and sodium salicylate
    • doi:10. 1128/JB.183.13.3890-3902.2001
    • Pomposiello, P. J., Bennik, M. H. & Demple, B. (2001). Genome-wide transcriptional profiling of the Escherichia coli responses to superoxide stress and sodium salicylate. J Bacteriol 183, 3890-3902. doi:10. 1128/JB.183.13.3890-3902.2001.
    • (2001) J Bacteriol , vol.183 , pp. 3890-3902
    • Pomposiello, P.J.1    Bennik, M.H.2    Demple, B.3
  • 31
    • 0027406241 scopus 로고
    • Induction of manganese-containing superoxide dismutase in anaerobic Escherichia coli by diamide and 1,10-phenanthroline: Sites of transcriptional regulation
    • doi:10.1073/ pnas.90.6.2310
    • Privalle, C. T., Kong, S. E. & Fridovich, I. (1993). Induction of manganese-containing superoxide dismutase in anaerobic Escherichia coli by diamide and 1,10-phenanthroline: sites of transcriptional regulation. Proc Natl Acad Sci U S A 90, 2310-2314. doi:10.1073/ pnas.90.6.2310.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 2310-2314
    • Privalle, C.T.1    Kong, S.E.2    Fridovich, I.3
  • 32
    • 0017390556 scopus 로고
    • A rapid, sensitive, and versatile assay for protein using Coomassie brilliant blue G250
    • doi:10.1016/0003-2697(77)90428-6
    • Sedmak, J. J. & Grossberg, S. E. (1977). A rapid, sensitive, and versatile assay for protein using Coomassie brilliant blue G250. Anal Biochem 79, 544-552. doi:10.1016/0003-2697(77)90428-6.
    • (1977) Anal Biochem , vol.79 , pp. 544-552
    • Sedmak, J.J.1    Grossberg, S.E.2
  • 33
    • 34548563918 scopus 로고    scopus 로고
    • Oxidative stress evokes a metabolic adaptation that favors increased NADPH synthesis and decreased NADH production in Pseudomonas fluorescens
    • doi:10.1128/JB.00555-07
    • Singh, R., Mailloux, R. J., Puiseux-Dao, S. & Appanna, V. D. (2007). Oxidative stress evokes a metabolic adaptation that favors increased NADPH synthesis and decreased NADH production in Pseudomonas fluorescens. J Bacteriol 189, 6665-6675. doi:10.1128/JB.00555-07.
    • (2007) J Bacteriol , vol.189 , pp. 6665-6675
    • Singh, R.1    Mailloux, R.J.2    Puiseux-Dao, S.3    Appanna, V.D.4
  • 34
    • 0000208385 scopus 로고
    • A colorimetric method for estimating the pyridine nucleotide content of small amounts of animal tissue
    • doi:10.1038/193454a0
    • Slater, T. F. & Sawyer, B. (1962). A colorimetric method for estimating the pyridine nucleotide content of small amounts of animal tissue. Nature 193, 454-456. doi:10.1038/193454a0.
    • (1962) Nature , vol.193 , pp. 454-456
    • Slater, T.F.1    Sawyer, B.2
  • 35
    • 41949137280 scopus 로고    scopus 로고
    • Crystal structure of the [2Fe-2S] oxidative-stress sensor SoxR bound to DNA
    • doi:10.1073/pnas. 0709188105
    • Watanabe, S., Kita, A., Kobayashi, K. & Miki, K. (2008). Crystal structure of the [2Fe-2S] oxidative-stress sensor SoxR bound to DNA. Proc Natl Acad Sci U S A 105, 4121-4126. doi:10.1073/pnas. 0709188105.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 4121-4126
    • Watanabe, S.1    Kita, A.2    Kobayashi, K.3    Miki, K.4
  • 36
    • 0037072770 scopus 로고    scopus 로고
    • Reduced flavins promote oxidative DNA damage in non-respiring Escherichia coli by delivering electrons to intracellular free iron
    • doi:10.1074/jbc.M203977200
    • Woodmansee, A. N. & Imlay, J. A. (2002). Reduced flavins promote oxidative DNA damage in non-respiring Escherichia coli by delivering electrons to intracellular free iron. J Biol Chem 277, 34055-34066. doi:10.1074/jbc.M203977200.
    • (2002) J Biol Chem , vol.277 , pp. 34055-34066
    • Woodmansee, A.N.1    Imlay, J.A.2
  • 37
    • 0026638855 scopus 로고
    • Two-stage induction of the soxRS (superoxide response) regulon of Escherichia coli
    • Wu, J. & Weiss, B. (1992). Two-stage induction of the soxRS (superoxide response) regulon of Escherichia coli. J Bacteriol 174, 3915-3920.
    • (1992) J Bacteriol , vol.174 , pp. 3915-3920
    • Wu, J.1    Weiss, B.2


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