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Volumn 69, Issue 1, 2015, Pages 93-108

Transcription Factors That Defend Bacteria Against Reactive Oxygen Species

Author keywords

Hydrogen peroxide; OxyR; PerR; Reactive oxygen species; SoxR; Superoxide

Indexed keywords

COPROPORPHYRINOGEN OXIDASE; ELECTROPHILE; FERROCHELATASE; GLUTAREDOXIN; GLUTATHIONE REDUCTASE; HYDROGEN PEROXIDE; IRON; MANGANESE; OXIDOREDUCTASE; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SULFUR; SUPEROXIDE DISMUTASE; THIOREDOXIN; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR OXYR; TRANSCRIPTION FACTOR PERR; TRANSCRIPTION FACTOR SOXR; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; SUPEROXIDE;

EID: 84945246465     PISSN: 00664227     EISSN: 15453251     Source Type: Book Series    
DOI: 10.1146/annurev-micro-091014-104322     Document Type: Review
Times cited : (171)

References (121)
  • 1
    • 0023274375 scopus 로고
    • Function of micF as an antisense RNA in osmoregulatory expression of the ompF gene in Escherichia coli
    • Aiba H, Matsuyama S, Mizuno T, Mizushima S. 1987. Function of micF as an antisense RNA in osmoregulatory expression of the ompF gene in Escherichia coli. J. Bacteriol. 169: 3007-12
    • (1987) J. Bacteriol. , vol.169 , pp. 3007-3012
    • Aiba, H.1    Matsuyama, S.2    Mizuno, T.3    Mizushima, S.4
  • 2
    • 84860851659 scopus 로고    scopus 로고
    • Mononuclear iron enzymes are primary targets of hydrogen peroxide stress
    • Anjem A, Imlay JA. 2012. Mononuclear iron enzymes are primary targets of hydrogen peroxide stress. J. Biol. Chem. 287: 15544-56
    • (2012) J. Biol. Chem. , vol.287 , pp. 15544-15556
    • Anjem, A.1    Imlay, J.A.2
  • 3
    • 65549107862 scopus 로고    scopus 로고
    • Manganese import is a key element of the OxyR response to hydrogen peroxide in Escherichia coli
    • Anjem A, Varghese S, Imlay JA. 2009. Manganese import is a key element of the OxyR response to hydrogen peroxide in Escherichia coli. Mol. Microbiol. 72: 844-58
    • (2009) Mol. Microbiol. , vol.72 , pp. 844-858
    • Anjem, A.1    Varghese, S.2    Imlay, J.A.3
  • 4
    • 0032994431 scopus 로고    scopus 로고
    • Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol-disulfide status
    • Aslund F, Zheng M, Beckwith J, StorzG. 1999. Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol-disulfide status. PNAS 96: 6161-65
    • (1999) PNAS , vol.96 , pp. 6161-6165
    • Aslund, F.1    Zheng, M.2    Beckwith, J.3    Storz, G.4
  • 5
    • 34547852400 scopus 로고    scopus 로고
    • NOX family NADPH oxidases: Not just in mammals
    • Bedard K, Lardy B, Krause K-H. 2007. NOX family NADPH oxidases: not just in mammals. Biochemie 89: 1107-12
    • (2007) Biochemie , vol.89 , pp. 1107-1112
    • Bedard, K.1    Lardy, B.2    Krause, K.-H.3
  • 6
    • 43149105201 scopus 로고    scopus 로고
    • Rapid changes in gene expression dynamics in response to superoxide reveal SoxRS-dependent and-independent transcriptional networks
    • Blanchard JL, Wholely WY, Conlon EM, Pomposiello PJ. 2007. Rapid changes in gene expression dynamics in response to superoxide reveal SoxRS-dependent and-independent transcriptional networks. PLOS ONE 2: e1186
    • (2007) PLOS ONE , vol.2 , pp. e1186
    • Blanchard, J.L.1    Wholely, W.Y.2    Conlon, E.M.3    Pomposiello, P.J.4
  • 7
    • 0031850630 scopus 로고    scopus 로고
    • Bacillus subtilis contains multiple fur homologues: Identification of the iron uptake (Fur) and peroxide regulon (PerR) repressors
    • Bsat N, Herbig A, Casillas-Martinez L, Setlow P, Helmann JD. 1998. Bacillus subtilis contains multiple Fur homologues: identification of the iron uptake (Fur) and peroxide regulon (PerR) repressors. Mol. Microbiol. 29: 189-98
    • (1998) Mol. Microbiol. , vol.29 , pp. 189-198
    • Bsat, N.1    Herbig, A.2    Casillas-Martinez, L.3    Setlow, P.4    Helmann, J.D.5
  • 8
    • 0022683672 scopus 로고
    • Isolation of superoxide dismutase mutants in Escherichia coli: Is superoxide dismutase necessary for aerobic life
    • Carlioz A, Touati D. 1986. Isolation of superoxide dismutase mutants in Escherichia coli: Is superoxide dismutase necessary for aerobic life EMBO J. 5: 623-30
    • (1986) EMBO J. , vol.5 , pp. 623-630
    • Carlioz, A.1    Touati, D.2
  • 9
    • 0029152774 scopus 로고
    • Coordinate regulation of Bacillus subtilis peroxide stress genes by hydrogen peroxide and metal ions
    • Chen L, Keramati L, Helmann JD. 1995. Coordinate regulation of Bacillus subtilis peroxide stress genes by hydrogen peroxide and metal ions. PNAS 92: 8190-94
    • (1995) PNAS , vol.92 , pp. 8190-8194
    • Chen, L.1    Keramati, L.2    Helmann, J.D.3
  • 10
    • 77953809155 scopus 로고    scopus 로고
    • The multifaceted capacity of Dps proteins to combat bacterial stress conditions: Detoxification of iron and hydrogen peroxide and DNA binding
    • Chiancone E, Ceci P. 2010. The multifaceted capacity of Dps proteins to combat bacterial stress conditions: detoxification of iron and hydrogen peroxide and DNA binding. Biochim. Biophys. Acta 1800: 798-805
    • (2010) Biochim. Biophys. Acta , vol.1800 , pp. 798-805
    • Chiancone, E.1    Ceci, P.2
  • 11
    • 0035815274 scopus 로고    scopus 로고
    • Structural basis of the redox switch in the OxyR transcription factor
    • Choi H, Kim S, Mukhopadhyay P, Cho S, Woo J, et al. 2001. Structural basis of the redox switch in the OxyR transcription factor. Cell 105: 103-13
    • (2001) Cell , vol.105 , pp. 103-113
    • Choi, H.1    Kim, S.2    Mukhopadhyay, P.3    Cho, S.4    Woo, J.5
  • 12
    • 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
    • Chou JH, Greenberg JT, Demple B. 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: 1026-31
    • (1993) J. Bacteriol. , vol.175 , pp. 1026-1031
    • Chou, J.H.1    Greenberg, J.T.2    Demple, B.3
  • 13
    • 50649098819 scopus 로고    scopus 로고
    • Redox-active antibiotics control gene expression and community behavior in divergent bacteria
    • Dietrich LE, Teal TK, Price-Whelan A, Newman DK. 2008. Redox-active antibiotics control gene expression and community behavior in divergent bacteria. Science 321: 1203-6
    • (2008) Science , vol.321 , pp. 1203-1206
    • Dietrich, L.E.1    Teal, T.K.2    Price-Whelan, A.3    Newman, D.K.4
  • 14
    • 33747082622 scopus 로고    scopus 로고
    • The phenazine pyocyanin is a terminal signalling factor in the quorum sensing network of Pseudomonas aeruginosa
    • Dietrich LEP, Price-Whelan A, Petersen A, Whiteley M, Newman DK. 2006. The phenazine pyocyanin is a terminal signalling factor in the quorum sensing network of Pseudomonas aeruginosa. Mol. Microbiol. 61: 1308-21
    • (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
  • 15
    • 0030795788 scopus 로고    scopus 로고
    • In vivo kinetics of a redox-regulated transcriptional switch
    • Ding H, Demple B. 1997. In vivo kinetics of a redox-regulated transcriptional switch. PNAS 94: 8445-49
    • (1997) PNAS , vol.94 , pp. 8445-8449
    • Ding, H.1    Demple, B.2
  • 16
    • 84878675814 scopus 로고    scopus 로고
    • Methionine oxidation activates a transcription factor in response to oxidative stress
    • Drazic A, MiuraH, Peschek J, Le Y, Bach NC, et al. 2013. Methionine oxidation activates a transcription factor in response to oxidative stress. PNAS 110: 9493-98
    • (2013) PNAS , vol.110 , pp. 9493-9498
    • Drazic, A.1    Miura, H.2    Peschek, J.3    Le, Y.4    Bach, N.C.5
  • 17
    • 84868603203 scopus 로고    scopus 로고
    • Peroxide-sensing transcriptional regulators in bacteria
    • Dubbs JM, Mongkolsuk S. 2012. Peroxide-sensing transcriptional regulators in bacteria. J. Bacteriol. 194: 5495-503
    • (2012) J. Bacteriol. , vol.194 , pp. 5495-5503
    • Dubbs, J.M.1    Mongkolsuk, S.2
  • 19
    • 84896735652 scopus 로고    scopus 로고
    • The fur (ferric uptake regulator) superfamily: Diversity and versatility of key transcriptional regulators
    • Fillat MF. 2014. The FUR (ferric uptake regulator) superfamily: diversity and versatility of key transcriptional regulators. Arch. Biochem. Biophys. 546: 41-52
    • (2014) Arch. Biochem. Biophys. , vol.546 , pp. 41-52
    • Fillat, M.F.1
  • 20
    • 0027491617 scopus 로고
    • The inactivation of Fe-S cluster containing hydro-lyases by superoxide
    • Flint DH, Tuminello JF, Emptage MH. 1993. The inactivation of Fe-S cluster containing hydro-lyases by superoxide. J. Biol. Chem. 268: 22369-76
    • (1993) J. Biol. Chem. , vol.268 , pp. 22369-22376
    • Flint, D.H.1    Tuminello, J.F.2    Emptage, M.H.3
  • 21
    • 84867426269 scopus 로고    scopus 로고
    • Direct oxidation of the [2Fe-2S] cluster in SoxR protein by superoxide: Distinct differential sensitivity to superoxide-mediated signal transduction
    • Fujikawa M, Kobayashi K, Kozawa T. 2012. Direct oxidation of the [2Fe-2S] cluster in SoxR protein by superoxide: distinct differential sensitivity to superoxide-mediated signal transduction. J. Biol. Chem. 287: 35702-8
    • (2012) J. Biol. Chem. , vol.287 , pp. 35702-35708
    • Fujikawa, M.1    Kobayashi, K.2    Kozawa, T.3
  • 22
    • 84906079585 scopus 로고    scopus 로고
    • Mechanistic studies on formation of the dinitrosyl iron complex of the [2Fe-2S] cluster of SoxR protein
    • Fujikawa M, Kobayashi K, Kozawa T. 2014. Mechanistic studies on formation of the dinitrosyl iron complex of the [2Fe-2S] cluster of SoxR protein. J. Biochem. 156: 163-72
    • (2014) J. Biochem. , vol.156 , pp. 163-172
    • Fujikawa, M.1    Kobayashi, K.2    Kozawa, T.3
  • 23
    • 84944454953 scopus 로고    scopus 로고
    • Redox-dependent DNA distortion in a SoxR proteinpromoter complex studied using fluorescent probes
    • Fujikawa M, Kobayashi K, Kozawa T. 2015. Redox-dependent DNA distortion in a SoxR proteinpromoter complex studied using fluorescent probes. J. Biochem. 157: 389-97
    • (2015) J. Biochem. , vol.157 , pp. 389-397
    • Fujikawa, M.1    Kobayashi, K.2    Kozawa, T.3
  • 24
    • 0026045587 scopus 로고
    • Superoxide sensitivity of the Escherichia coli aconitase
    • Gardner PR, Fridovich I. 1991. Superoxide sensitivity of the Escherichia coli aconitase. J. Biol. Chem. 266: 19328-33
    • (1991) J. Biol. Chem. , vol.266 , pp. 19328-19333
    • Gardner, P.R.1    Fridovich, I.2
  • 25
    • 0034008694 scopus 로고    scopus 로고
    • Activation of SoxR by overproduction of desulfoferrodoxin: Multiple ways to induce the soxRS regulon
    • Gaudu P, Dubrac S, Touati D. 2000. Activation of SoxR by overproduction of desulfoferrodoxin: multiple ways to induce the soxRS regulon. J. Bacteriol. 182: 1761-63
    • (2000) J. Bacteriol. , vol.182 , pp. 1761-1763
    • Gaudu, P.1    Dubrac, S.2    Touati, D.3
  • 26
    • 0031048106 scopus 로고    scopus 로고
    • Regulation of the soxRS oxidative stress regulon
    • Gaudu P, Moon N, Weiss B. 1997. Regulation of the soxRS oxidative stress regulon. J. Biol. Chem. 272: 5082-86
    • (1997) J. Biol. Chem. , vol.272 , pp. 5082-5086
    • Gaudu, P.1    Moon, N.2    Weiss, B.3
  • 27
    • 0022870573 scopus 로고
    • The respiratory burst oxidase of human neutrophils: Further studies of the purified enzyme
    • Glass GA, DeLisle DM, DeTogni P, Gabig TG, Magee BH, et al. 1986. The respiratory burst oxidase of human neutrophils: further studies of the purified enzyme. J. Biol. Chem. 261: 13247-51
    • (1986) J. Biol. Chem. , vol.261 , pp. 13247-13251
    • Glass, G.A.1    DeLisle, D.M.2    DeTogni, P.3    Gabig, T.G.4    Magee, B.H.5
  • 29
    • 0031938051 scopus 로고    scopus 로고
    • Balance between endogenous superoxide stress and antioxidant defenses
    • Gort AS, Imlay JA. 1998. Balance between endogenous superoxide stress and antioxidant defenses. J. Bacteriol. 180: 1402-10
    • (1998) J. Bacteriol. , vol.180 , pp. 1402-1410
    • Gort, A.S.1    Imlay, J.A.2
  • 30
    • 0038419597 scopus 로고    scopus 로고
    • The YggX protein of Salmonella enterica is involved in Fe(II) trafficking and minimizes the DNA damage caused by hydroxyl radicals: Residue CYS-7 is essential for YggX function
    • Gralnick JA, Downs DM. 2003. The YggX protein of Salmonella enterica is involved in Fe(II) trafficking and minimizes the DNA damage caused by hydroxyl radicals: Residue CYS-7 is essential for YggX function. J. Biol. Chem. 278: 20708-15
    • (2003) J. Biol. Chem. , vol.278 , pp. 20708-20715
    • Gralnick, J.A.1    Downs, D.M.2
  • 32
    • 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. 1990. Positive control of a global antioxidant defense regulon activated by superoxide-generating agents in Escherichia coli. PNAS 87: 6181-85
    • (1990) PNAS , vol.87 , pp. 6181-6185
    • Greenberg, J.T.1    Monach, P.2    Chou, J.H.3    Josephy, P.D.4    Demple, B.5
  • 33
    • 1642524483 scopus 로고    scopus 로고
    • Proteolytic degradation of Escherichia coli transcription activators Sox and MarA as the mechanism for reversing the induction of the superoxide (SoxRS) and multiple antibiotic resistance (Mar) regulons
    • GriffithKL, Shah IM, WolfREJr. 2004. Proteolytic degradation of Escherichia coli transcription activators Sox and MarA as the mechanism for reversing the induction of the superoxide (SoxRS) and multiple antibiotic resistance (Mar) regulons. Mol. Microbiol. 51: 1801-16
    • (2004) Mol. Microbiol. , vol.51 , pp. 1801-1816
    • Griffith, K.L.1    Shah, I.M.2    Wolf, R.E.3
  • 34
    • 79951789722 scopus 로고    scopus 로고
    • The SoxRS response of Escherichia coli is directly activated by redox-cycling drugs rather than by superoxide
    • Gu M, Imlay JA. 2011. The SoxRS response of Escherichia coli is directly activated by redox-cycling drugs rather than by superoxide. Mol. Microbiol. 79: 1136-50
    • (2011) Mol. Microbiol. , vol.79 , pp. 1136-1150
    • Gu, M.1    Imlay, J.A.2
  • 35
    • 84879501095 scopus 로고    scopus 로고
    • Superoxide poisons mononuclear iron enzymes by causing mismetallation
    • Gu M, Imlay JA. 2013. Superoxide poisons mononuclear iron enzymes by causing mismetallation. Mol. Microbiol. 89: 123-34
    • (2013) Mol. Microbiol. , vol.89 , pp. 123-134
    • Gu, M.1    Imlay, J.A.2
  • 36
    • 0017760575 scopus 로고
    • Regulation of the synthesis of superoxide dismutase in Escherichia coli: Induction by methyl viologen
    • Hassan HM, Fridovich I. 1977. Regulation of the synthesis of superoxide dismutase in Escherichia coli: induction by methyl viologen. J. Biol. Chem. 252: 7667-72
    • (1977) J. Biol. Chem. , vol.252 , pp. 7667-7672
    • Hassan, H.M.1    Fridovich, I.2
  • 37
    • 0018220069 scopus 로고
    • Superoxide radical and the oxygen enhancement of the toxicity of paraquat in Escherichia coli
    • HassanHM, Fridovich I. 1978. Superoxide radical and the oxygen enhancement of the toxicity of paraquat in Escherichia coli. J. Biol. Chem. 253: 8143-48
    • (1978) J. Biol. Chem. , vol.253 , pp. 8143-8148
    • Hassan, H.M.1    Fridovich, I.2
  • 38
    • 84907833692 scopus 로고    scopus 로고
    • Specificity of metal sensing: Iron and manganese homeostasis in Bacillus subtilis
    • Helmann JD. 2014. Specificity of metal sensing: iron and manganese homeostasis in Bacillus subtilis. J. Biol. Chem. 289: 28112-20
    • (2014) J. Biol. Chem. , vol.289 , pp. 28112-28120
    • Helmann, J.D.1
  • 39
    • 73649129891 scopus 로고    scopus 로고
    • Themajor catalase gene (katA) of Pseudomonas aeruginosa PA14 is under both positive and negative control of the global transactivator OxyR in response to hydrogen peroxide
    • Heo YJ, Chung IY, ChoWJ, Lee BY, Kim JH, et al. 2010. Themajor catalase gene (katA) of Pseudomonas aeruginosa PA14 is under both positive and negative control of the global transactivator OxyR in response to hydrogen peroxide. J. Bacteriol. 192: 381-90
    • (2010) J. Bacteriol. , vol.192 , pp. 381-390
    • Heo, Y.J.1    Chung, I.Y.2    Cho, W.J.3    Lee, B.Y.4    Kim, J.H.5
  • 40
    • 55349123270 scopus 로고    scopus 로고
    • OxyR tightly regulates catalase expression in Neisseria meningitidis through both repression and activation mechanisms
    • Ieva R, RoncaratiD, MetruccioMM, Seib KL, ScarlatoV, Delany I. 2008. OxyR tightly regulates catalase expression in Neisseria meningitidis through both repression and activation mechanisms. Mol. Microbiol. 70: 1152-65
    • (2008) Mol. Microbiol. , vol.70 , pp. 1152-1165
    • Ieva, R.1    Roncarati, D.2    Metruccio, M.M.3    Seib, K.L.4    Scarlato, V.5    Delany, I.6
  • 41
    • 84879422944 scopus 로고    scopus 로고
    • The molecular mechanisms and physiological consequences of oxidative stress: Lessons from a model bacterium
    • Imlay JA. 2013. The molecular mechanisms and physiological consequences of oxidative stress: lessons from a model bacterium. Nat. Rev. Microbiol. 11: 443-54
    • (2013) Nat. Rev. Microbiol. , vol.11 , pp. 443-454
    • Imlay, J.A.1
  • 42
    • 0023905646 scopus 로고
    • Toxic DNA damage by hydrogen peroxide through the Fenton reaction in vivo and in vitro
    • Imlay JA, Chin SM, Linn S. 1988. Toxic DNA damage by hydrogen peroxide through the Fenton reaction in vivo and in vitro. Science 240: 640-42
    • (1988) Science , vol.240 , pp. 640-642
    • Imlay, J.A.1    Chin, S.M.2    Linn, S.3
  • 43
    • 1642498276 scopus 로고    scopus 로고
    • Cytotoxic action of juglone and plumbagin: A mechanistic study using HaCaT keratinocytes
    • Inbaraj JJ, Chignell CF. 2004. Cytotoxic action of juglone and plumbagin: A mechanistic study using HaCaT keratinocytes. Chem. Res. Toxicol. 17: 55-62
    • (2004) Chem. Res. Toxicol. , vol.17 , pp. 55-62
    • Inbaraj, J.J.1    Chignell, C.F.2
  • 44
    • 0024599904 scopus 로고
    • An alkyl hydroperoxide reductase from Salmonella typhimurium involved in the defense of DNA against oxidative damage: Purification and properties
    • Jacobson FS, Morgan RW, Christman MF, Ames BN. 1989. An alkyl hydroperoxide reductase from Salmonella typhimurium involved in the defense of DNA against oxidative damage: Purification and properties. J. Biol. Chem. 264: 1488-96
    • (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
  • 45
    • 67649419186 scopus 로고    scopus 로고
    • Structural characterization of the active form of PerR: Insights into the metal-induced activation of PerR and fur proteins for DNA binding
    • Jacquamet L, Traore DA, Ferrer JL, Proux O, Testemale D, et al. 2009. Structural characterization of the active form of PerR: insights into the metal-induced activation of PerR and Fur proteins for DNA binding. Mol. Microbiol. 73: 20-31
    • (2009) Mol. Microbiol. , vol.73 , pp. 20-31
    • Jacquamet, L.1    Traore, D.A.2    Ferrer, J.L.3    Proux, O.4    Testemale, D.5
  • 46
    • 33847753939 scopus 로고    scopus 로고
    • Micromolar intracellular hydrogen peroxide disrupts metabolism by damaging iron-sulfur enzymes
    • Jang S, Imlay JA. 2007. Micromolar intracellular hydrogen peroxide disrupts metabolism by damaging iron-sulfur enzymes. J. Biol. Chem. 282: 929-37
    • (2007) J. Biol. Chem. , vol.282 , pp. 929-937
    • Jang, S.1    Imlay, J.A.2
  • 47
    • 78649983777 scopus 로고    scopus 로고
    • Hydrogen peroxide inactivates the Escherichia coli Isc iron-sulphur assembly system, and OxyR induces the Suf system to compensate
    • Jang S, Imlay JA. 2010. Hydrogen peroxide inactivates the Escherichia coli Isc iron-sulphur assembly system, and OxyR induces the Suf system to compensate. Mol. Microbiol. 78: 1448-67
    • (2010) Mol. Microbiol. , vol.78 , pp. 1448-1467
    • Jang, S.1    Imlay, J.A.2
  • 48
    • 84929430296 scopus 로고    scopus 로고
    • Structural details of OxyR peroxide-sensing mechanism
    • Jo I, Chung I-Y, Bae H-W, Kim J-S, Song S, et al. 2015. Structural details of OxyR peroxide-sensing mechanism. PNAS 112: 6443-48
    • (2015) PNAS , vol.112 , pp. 6443-6448
    • Jo, I.1    Chung, I.-Y.2    Bae, H.-W.3    Kim, J.-S.4    Song, S.5
  • 49
    • 77953220053 scopus 로고    scopus 로고
    • The R regulon of Streptomyces oelicolor A3(2) reveals a key role in protein quality control during disulphide stress
    • Kallifidas D, Thomas D, Doughty P, Paget MSB. 2010. The R regulon of Streptomyces oelicolor A3(2) reveals a key role in protein quality control during disulphide stress. Microbiology 156: 1661-72
    • (2010) Microbiology , vol.156 , pp. 1661-1672
    • Kallifidas, D.1    Thomas, D.2    Doughty, P.3    Paget, M.S.B.4
  • 50
    • 0036267337 scopus 로고    scopus 로고
    • Regulation of Salmonella enterica serovar Typhimurium mntH transcription by H2O2, Fe2+, andMn2+
    • Kehres DG, Janakiraman A, Slauch JM, Maguire ME. 2002. Regulation of Salmonella enterica serovar Typhimurium mntH transcription by H2O2, Fe2+, andMn2+. J. Bacteriol. 184: 3151-58
    • (2002) J. Bacteriol. , vol.184 , pp. 3151-3158
    • Kehres, D.G.1    Janakiraman, A.2    Slauch, J.M.3    Maguire, M.E.4
  • 51
    • 84905965348 scopus 로고    scopus 로고
    • Oxidative stress response in Pseudomonas putida
    • Kim J, ParkW. 2014. Oxidative stress response in Pseudomonas putida. Appl. Microbiol. Biotechnol. 98: 6933-46
    • (2014) Appl. Microbiol. Biotechnol. , vol.98 , pp. 6933-6946
    • Kim, J.1    Park, W.2
  • 52
    • 84863565065 scopus 로고    scopus 로고
    • Conservation of thiol-oxidative stress responses regulated by SigR orthologues in actinomycetes
    • Kim M-S, Dufour YS, Yoo JS, Cho Y-B, Park J-H, et al. 2012. Conservation of thiol-oxidative stress responses regulated by SigR orthologues in actinomycetes. Mol. Microbiol. 85: 326-44
    • (2012) Mol. Microbiol. , vol.85 , pp. 326-344
    • Kim, M.-S.1    Dufour, Y.S.2    Yoo, J.S.3    Cho, Y.-B.4    Park, J.-H.5
  • 53
    • 84906937468 scopus 로고    scopus 로고
    • Distinct characteristics of OxyR2, a new OxyR-type regulator, ensuring expression of peroxiredoxin 2 detoxifying low levels of hydrogen peroxide in Vibrio vulnificus
    • Kim S, Bang Y-J, Kim D, Lim JG, Oh MH, Choi SH. 2014. Distinct characteristics of OxyR2, a new OxyR-type regulator, ensuring expression of peroxiredoxin 2 detoxifying low levels of hydrogen peroxide in Vibrio vulnificus. Mol. Microbiol. 93: 992-1009
    • (2014) Mol. Microbiol. , vol.93 , pp. 992-1009
    • Kim, S.1    Bang, Y.-J.2    Kim, D.3    Lim, J.G.4    Oh, M.H.5    Choi, S.H.6
  • 54
    • 84922464341 scopus 로고    scopus 로고
    • Binding of promoter DNA to SoxR protein decreases the reduction potential of the [2Fe-2S] cluster
    • Kobayashi K, Fujikawa M, Kozawa T. 2014. Binding of promoter DNA to SoxR protein decreases the reduction potential of the [2Fe-2S] cluster. Biochemistry 54: 334-39
    • (2014) Biochemistry , vol.54 , pp. 334-339
    • Kobayashi, K.1    Fujikawa, M.2    Kozawa, T.3
  • 55
    • 0033021117 scopus 로고    scopus 로고
    • Isolation of reductase for SoxR that governs an oxidative response regulon from Escherichia coli
    • KobayashiK, Tagawa S. 1999. Isolation of reductase for SoxR that governs an oxidative response regulon from Escherichia coli. FEBS Lett. 451: 227-30
    • (1999) FEBS Lett. , vol.451 , pp. 227-230
    • Kobayashi, K.1    Tagawa, S.2
  • 56
    • 0038540118 scopus 로고    scopus 로고
    • A reducing system of the superoxide sensor SoxR in Escherichia coli
    • Koo MS, Lee JH, Ray SY, Yeo WS, Lee JW, et al. 2003. A reducing system of the superoxide sensor SoxR in Escherichia coli. EMBO J. 22: 2614-22
    • (2003) EMBO J. , vol.22 , pp. 2614-2622
    • Koo, M.S.1    Lee, J.H.2    Ray, S.Y.3    Yeo, W.S.4    Lee, J.W.5
  • 57
    • 0036194027 scopus 로고    scopus 로고
    • A potential role for periplasmic superoxide dismutase in blocking the penetration of external superoxide into the cytosol of phagocytosed bacteria
    • Korshunov SS, Imlay JA. 2002. A potential role for periplasmic superoxide dismutase in blocking the penetration of external superoxide into the cytosol of phagocytosed bacteria. Mol. Microbiol. 43: 95-106
    • (2002) Mol. Microbiol. , vol.43 , pp. 95-106
    • Korshunov, S.S.1    Imlay, J.A.2
  • 58
    • 79953716809 scopus 로고    scopus 로고
    • The soxRS response of Escherichia coli can be induced in the absence of oxidative stress and oxygen by modulation of NADPH content
    • Krapp AR, Humbert MV, Carrillo N. 2011. The soxRS response of Escherichia coli can be induced in the absence of oxidative stress and oxygen by modulation of NADPH content. Microbiology 157: 957-65
    • (2011) Microbiology , vol.157 , pp. 957-965
    • Krapp, A.R.1    Humbert, M.V.2    Carrillo, N.3
  • 59
    • 0036175587 scopus 로고    scopus 로고
    • The flavoenzyme ferredoxin (flavodoxin)-NADP(H) reductase modulates NADP(H) homeostasis during the soxRS response of Escherichia coli
    • Krapp AR, Rodriguez RE, Poli HU, Paladini DH, Palatnik JF, Carillo N. 2002. The flavoenzyme ferredoxin (flavodoxin)-NADP(H) reductase modulates NADP(H) homeostasis during the soxRS response of Escherichia coli. J. Bacteriol. 184: 1474-80
    • (2002) J. Bacteriol. , vol.184 , pp. 1474-1480
    • Krapp, A.R.1    Rodriguez, R.E.2    Poli, H.U.3    Paladini, D.H.4    Palatnik, J.F.5    Carillo, N.6
  • 60
    • 0023178381 scopus 로고
    • Dihydroxyisovalerate dehydratase: A superoxide-sensitive enzyme
    • Kuo CF, Mashino T, Fridovich I. 1987. dihydroxyisovalerate dehydratase: A superoxide-sensitive enzyme. J. Biol. Chem. 262: 4724-27
    • (1987) J. Biol. Chem. , vol.262 , pp. 4724-4727
    • Kuo, C.F.1    Mashino, T.2    Fridovich, I.3
  • 61
    • 16544369973 scopus 로고    scopus 로고
    • Redox regulation of OxyR requires specific disulfide bond formation involving a rapid kinetic reaction path
    • Lee C, Lee SM, Mukhopadhyay P, Kim SJ, Lee SC, et al. 2004. Redox regulation of OxyR requires specific disulfide bond formation involving a rapid kinetic reaction path. Nat. Struct. Mol. Biol. 11: 1179-85
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 1179-1185
    • Lee, C.1    Lee, S.M.2    Mukhopadhyay, P.3    Kim, S.J.4    Lee, S.C.5
  • 62
    • 67649406254 scopus 로고    scopus 로고
    • SoxRS-mediated lipopolysaccharide modification enhances resistance against multiple drugs in Escherichia coli
    • Lee JH, Lee KL, Yeo WS, Park SJ, Roe JH. 2009. SoxRS-mediated lipopolysaccharide modification enhances resistance against multiple drugs in Escherichia coli. J. Bacteriol. 191: 4441-50
    • (2009) J. Bacteriol. , vol.191 , pp. 4441-4450
    • Lee, J.H.1    Lee, K.L.2    Yeo, W.S.3    Park, S.J.4    Roe, J.H.5
  • 63
    • 33747722767 scopus 로고    scopus 로고
    • Biochemical characterization of the structural Zn2+ site in the Bacillus subtilis peroxide sensor PerR
    • Lee J-W, Helmann JD. 2006. Biochemical characterization of the structural Zn2+ site in the Bacillus subtilis peroxide sensor PerR. J. Biol. Chem. 281: 23567-78
    • (2006) J. Biol. Chem. , vol.281 , pp. 23567-23578
    • Lee, J.-W.1    Helmann, J.D.2
  • 64
    • 33645037891 scopus 로고    scopus 로고
    • The PerR transcription factor senses H2O2 by metal-catalyzed histidine oxidation
    • Lee J-W, Helmann JD. 2006. The PerR transcription factor senses H2O2 by metal-catalyzed histidine oxidation. Nature 440: 363-67
    • (2006) Nature , vol.440 , pp. 363-367
    • Lee, J.-W.1    Helmann, J.D.2
  • 66
    • 78049488541 scopus 로고    scopus 로고
    • A role of ygfZ in the Escherichia coli response to plumbagin challenge
    • Lin CN, SyuWJ, SunWS, Chen JW, Chen TH, et al. 2010. A role of ygfZ in the Escherichia coli response to plumbagin challenge. J. Biomed. Sci. 17: 84
    • (2010) J. Biomed. Sci. , vol.17 , pp. 84
    • Lin, C.N.1    Syu, W.J.2    Sun, W.S.3    Chen, J.W.4    Chen, T.H.5
  • 67
    • 0033515449 scopus 로고    scopus 로고
    • Induction of the soxRS regulon of Escherichia coli by superoxide
    • Liochev SI, Benov L, Touati D, Fridovich I. 1999. Induction of the soxRS regulon of Escherichia coli by superoxide. J. Biol. Chem. 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
  • 68
    • 0026778382 scopus 로고
    • Fumarase C, the stable fumarase of Escherichia coli, is controlled by the soxRS regulon
    • Liochev SI, Fridovich I. 1992. Fumarase C, the stable fumarase of Escherichia coli, is controlled by the soxRS regulon. PNAS 89: 5892-96
    • (1992) PNAS , vol.89 , pp. 5892-5896
    • Liochev, S.I.1    Fridovich, I.2
  • 69
    • 0031004571 scopus 로고    scopus 로고
    • Lucigenin luminescence as ameasure of intracellular superoxide dismutase activity in Escherichia coli
    • Liochev SI, Fridovich I. 1997. Lucigenin luminescence as ameasure of intracellular superoxide dismutase activity in Escherichia coli. PNAS 94: 2891-96
    • (1997) PNAS , vol.94 , pp. 2891-2896
    • Liochev, S.I.1    Fridovich, I.2
  • 70
    • 0033616612 scopus 로고    scopus 로고
    • Nitroreductase A is regulated as a member of the soxRS regulon of Escherichia coli
    • Liochev SI, Hausladen A, Fridovich I. 1999. Nitroreductase A is regulated as a member of the soxRS regulon of Escherichia coli. PNAS 96: 3537-39
    • (1999) PNAS , vol.96 , pp. 3537-3539
    • Liochev, S.I.1    Hausladen, A.2    Fridovich, I.3
  • 71
    • 79955542589 scopus 로고    scopus 로고
    • The YaaA protein of the Escherichia coli OxyR regulon lessens hydrogen peroxide toxicity by diminishing the amount of intracellular unincorporated iron
    • Liu Y, Bauer SC, Imlay JA. 2011. The YaaA protein of the Escherichia coli OxyR regulon lessens hydrogen peroxide toxicity by diminishing the amount of intracellular unincorporated iron. J. Bacteriol. 193: 2186-96
    • (2011) J. Bacteriol. , vol.193 , pp. 2186-2196
    • Liu, Y.1    Bauer, S.C.2    Imlay, J.A.3
  • 74
    • 0017876650 scopus 로고
    • Permeation of the erythrocyte stroma by superoxide radical
    • Lynch R, Fridovich I. 1978. Permeation of the erythrocyte stroma by superoxide radical. J. Biol. Chem. 253: 4697-99
    • (1978) J. Biol. Chem. , vol.253 , pp. 4697-4699
    • Lynch, R.1    Fridovich, I.2
  • 76
    • 84855891357 scopus 로고    scopus 로고
    • Novel roles of SoxR, a transcriptional regulator from Xanthomonas campestris, in sensing redox-cycling drugs and regulating a protective gene that have overall implications for bacterial stress physiology and virulence on a host plant
    • Mahavihakanont A, Charoenlap N, Namchaiw P, EiamphungpornW, Chattrakarn S, et al. 2012. Novel roles of SoxR, a transcriptional regulator from Xanthomonas campestris, in sensing redox-cycling drugs and regulating a protective gene that have overall implications for bacterial stress physiology and virulence on a host plant. J. Bacteriol. 194: 209-17
    • (2012) J. Bacteriol. , vol.194 , pp. 209-217
    • Mahavihakanont, A.1    Charoenlap, N.2    Namchaiw, P.3    Eiamphungporn, W.4    Chattrakarn, S.5
  • 77
    • 84929192909 scopus 로고    scopus 로고
    • The induction of two biosynthetic enzymes helps Escherichia coli sustain heme synthesis and activate catalase during hydrogen peroxide stress
    • Mancini S, Imlay JA. 2015. The induction of two biosynthetic enzymes helps Escherichia coli sustain heme synthesis and activate catalase during hydrogen peroxide stress. Mol. Microbiol. 96: 744-63
    • (2015) Mol. Microbiol. , vol.96 , pp. 744-763
    • Mancini, S.1    Imlay, J.A.2
  • 78
    • 78650887552 scopus 로고    scopus 로고
    • Promoter discrimination at class i MarA regulon promoters mediated by glutamic acid 89 of the MarA transcriptional activator of Escherichia coli
    • Martin RG, Rosner JL. 2011. Promoter discrimination at class I MarA regulon promoters mediated by glutamic acid 89 of the MarA transcriptional activator of Escherichia coli. J. Bacteriol. 193: 506-15
    • (2011) J. Bacteriol. , vol.193 , pp. 506-515
    • Martin, R.G.1    Rosner, J.L.2
  • 79
    • 0027951017 scopus 로고
    • Active oxygen species in plant defense against pathogens
    • Mehdy MC. 1994. Active oxygen species in plant defense against pathogens. Plant Physiol. 105: 467-72
    • (1994) Plant Physiol. , vol.105 , pp. 467-472
    • Mehdy, M.C.1
  • 80
    • 84902112138 scopus 로고    scopus 로고
    • Ada response-a strategy for repair of alkylated DNA in bacteria
    • Mielecki D, Grzesiuk E. 2014. Ada response-a strategy for repair of alkylated DNA in bacteria. FEMS Microbiol. Lett. 355: 1-11
    • (2014) FEMS Microbiol. Lett. , vol.355 , pp. 1-11
    • Mielecki, D.1    Grzesiuk, E.2
  • 81
    • 84884295788 scopus 로고    scopus 로고
    • Escherichia coli pyruvate: Flavodoxin oxidoreductase, YdbK-regulation of expression and biological roles in protection against oxidative stress
    • Nakayama T, Yonekura S-I, Yonei S, Zhang-Akiyama Q-M. 2013. Escherichia coli pyruvate: flavodoxin oxidoreductase, YdbK-regulation of expression and biological roles in protection against oxidative stress. Genes Genet. Syst. 88: 175-88
    • (2013) Genes Genet. Syst. , vol.88 , pp. 175-188
    • Nakayama, T.1    Yonekura, S.-I.2    Yonei, S.3    Zhang-Akiyama, Q.-M.4
  • 82
    • 84939784999 scopus 로고    scopus 로고
    • RNA-Seq analysis reveals a six-gene SoxR regulon in Streptomyces coelicolor
    • Naseer N, Shapiro JA, Chander M. 2014. RNA-Seq analysis reveals a six-gene SoxR regulon in Streptomyces coelicolor. PLOS ONE 9: e106181
    • (2014) PLOS ONE , vol.9 , pp. e106181
    • Naseer, N.1    Shapiro, J.A.2    Chander, M.3
  • 84
    • 0027440247 scopus 로고
    • Activation by nitric oxide of an oxidative stress response that defends Escherichia coli against activated macrophages
    • Nunoshiba T, Derojaswalker T, Wishnok JS, Tannenbaum SR, Demple B. 1993. Activation by nitric oxide of an oxidative stress response that defends Escherichia coli against activated macrophages. PNAS 90: 9993-97
    • (1993) PNAS , vol.90 , pp. 9993-9997
    • Nunoshiba, T.1    Derojaswalker, T.2    Wishnok, J.S.3    Tannenbaum, S.R.4    Demple, B.5
  • 85
    • 2442567822 scopus 로고    scopus 로고
    • A suf operon requirement for Fe-S cluster assembly during iron starvation in Escherichia coli
    • Outten FW, Djaman O, Storz G. 2004. A suf operon requirement for Fe-S cluster assembly during iron starvation in Escherichia coli. Mol. Microbiol. 52: 861-72
    • (2004) Mol. Microbiol. , vol.52 , pp. 861-872
    • Outten, F.W.1    Djaman, O.2    Storz, G.3
  • 86
    • 0035171384 scopus 로고    scopus 로고
    • Defining the disulphide stress response in Streptomyces coelicolor A3(2): Identification of the R regulon
    • PagetMS, Molle V, CohenG, Aharonowitz Y, Buttner MJ. 2001. Defining the disulphide stress response in Streptomyces coelicolor A3(2): identification of the R regulon. Mol. Microbiol. 42: 1007-20
    • (2001) Mol. Microbiol. , vol.42 , pp. 1007-1020
    • Paget, M.S.1    Molle, V.2    Cohen, G.3    Aharonowitz, Y.4    Buttner, M.J.5
  • 88
    • 17644408447 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa SoxR does not conform to the archetypal paradigm for SoxR-dependent regulation of the bacterial oxidative stress adaptive response
    • Palma M, Zurita J, Ferreras JA, Worgall S, Larone DH, et al. 2005. Pseudomonas aeruginosa SoxR does not conform to the archetypal paradigm for SoxR-dependent regulation of the bacterial oxidative stress adaptive response. Infect. Immun. 73: 2958-66
    • (2005) Infect. Immun. , vol.73 , pp. 2958-2966
    • Palma, M.1    Zurita, J.2    Ferreras, J.A.3    Worgall, S.4    Larone, D.H.5
  • 89
    • 84884852887 scopus 로고    scopus 로고
    • Single glutamate to aspartate mutation makes ferric uptake regulator (Fur) as sensitive toH2O2 as peroxide resistance regulator (PerR)
    • Parent A, Caux-Thang C, Signor L, Clemancey M, Sethu R, et al. 2013. Single glutamate to aspartate mutation makes ferric uptake regulator (Fur) as sensitive toH2O2 as peroxide resistance regulator (PerR). Angew. Chem. Int. Ed. 52: 10339-43
    • (2013) Angew. Chem. Int. Ed. , vol.52 , pp. 10339-10343
    • Parent, A.1    Caux-Thang, C.2    Signor, L.3    Clemancey, M.4    Sethu, R.5
  • 90
    • 0242407472 scopus 로고    scopus 로고
    • SoxRS-regulated expression and genetic analysis of the yggX gene of Escherichia coli
    • Pomposiello PJ, KoutsolioutsouA, CarrascoD, DempleB. 2003. SoxRS-regulated expression and genetic analysis of the yggX gene of Escherichia coli. J. Bacteriol. 185: 6624-32
    • (2003) J. Bacteriol. , vol.185 , pp. 6624-6632
    • Pomposiello, P.J.1    Koutsolioutsou, A.2    Carrasco, D.3    Demple, B.4
  • 91
    • 38749094500 scopus 로고    scopus 로고
    • The catalytic mechanism of peroxiredoxins
    • Poole LB. 2007. The catalytic mechanism of peroxiredoxins. Subcell. Biochem. 44: 61-81
    • (2007) Subcell. Biochem. , vol.44 , pp. 61-81
    • Poole, L.B.1
  • 92
    • 33947420458 scopus 로고    scopus 로고
    • Nitric oxide in chemostat-cultured Escherichia coli is sensed by Fnr and other global regulators: Unaltered methionine biosynthesis indicates lack of S nitrosation
    • Pullan ST, GidleyMD, Jones RA, Barrett J, StevaninTM, et al. 2007. Nitric oxide in chemostat-cultured Escherichia coli is sensed by Fnr and other global regulators: Unaltered methionine biosynthesis indicates lack of S nitrosation. J. Bacteriol. 189: 1845-55
    • (2007) J. Bacteriol. , vol.189 , pp. 1845-1855
    • Pullan, S.T.1    Gidley, M.D.2    Jones, R.A.3    Barrett, J.4    Stevanin, T.M.5
  • 93
    • 0034635333 scopus 로고    scopus 로고
    • Active and inhibited human catalase structures: Ligand and NADPH binding and catalytic mechanism
    • Putnam CD, Arvai AS, Bourne Y, Tainer JA. 2000. Active and inhibited human catalase structures: ligand and NADPH binding and catalytic mechanism. J. Mol. Biol. 296: 295-309
    • (2000) J. Mol. Biol. , vol.296 , pp. 295-309
    • Putnam, C.D.1    Arvai, A.S.2    Bourne, Y.3    Tainer, J.A.4
  • 94
    • 0035812657 scopus 로고    scopus 로고
    • Localization of Fe2+ at an RTGR sequence within a DNA duplex explains preferential cleavage by Fe2+ and H2O2
    • Rai P, Cole TD, Wemmer DE, Linn S. 2001. Localization of Fe2+ at an RTGR sequence within a DNA duplex explains preferential cleavage by Fe2+ and H2O2. J. Mol. Biol. 312: 1089-101
    • (2001) J. Mol. Biol. , vol.312 , pp. 1089-1101
    • Rai, P.1    Cole, T.D.2    Wemmer, D.E.3    Linn, S.4
  • 95
    • 0037641012 scopus 로고    scopus 로고
    • Oxygen-insensitive nitroreductasesNfsA and NfsB of Escherichia coli function under anaerobic conditions as lawsone-dependent Azo reductases
    • Rau J, Stolz A. 2003. Oxygen-insensitive nitroreductasesNfsA and NfsB of Escherichia coli function under anaerobic conditions as lawsone-dependent Azo reductases. Appl. Environ. Microbiol. 69: 3448-55
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 3448-3455
    • Rau, J.1    Stolz, A.2
  • 96
    • 84896718349 scopus 로고    scopus 로고
    • The role of thiol oxidative stress response in heat-induced protein aggregate formation during thermotolerance in Bacillus subtilis
    • Runde S, Moliere N, Heinz A, Maisonneuve E, Janczikowski A, et al. 2014. The role of thiol oxidative stress response in heat-induced protein aggregate formation during thermotolerance in Bacillus subtilis. Mol. Microbiol. 91: 1036-52
    • (2014) Mol. Microbiol. , vol.91 , pp. 1036-1052
    • Runde, S.1    Moliere, N.2    Heinz, A.3    Maisonneuve, E.4    Janczikowski, A.5
  • 97
    • 0035212036 scopus 로고    scopus 로고
    • Hydrogen peroxide fluxes and compartmentalization inside growing Escherichia coli
    • Seaver LC, Imlay JA. 2001. Hydrogen peroxide fluxes and compartmentalization inside growing Escherichia coli. J. Bacteriol. 183: 7182-89
    • (2001) J. Bacteriol. , vol.183 , pp. 7182-7189
    • Seaver, L.C.1    Imlay, J.A.2
  • 98
    • 1642293901 scopus 로고    scopus 로고
    • Hydrogen peroxide production in Streptococcus pyogenes: Involvement of lactase oxidase and coupling with aerobic utilization of lactate
    • Seki M, Iida K, Saito M, Nakayama H, Yoshida S. 2004. Hydrogen peroxide production in Streptococcus pyogenes: involvement of lactase oxidase and coupling with aerobic utilization of lactate. J. Bacteriol. 186: 2046-51
    • (2004) J. Bacteriol. , vol.186 , pp. 2046-2051
    • Seki, M.1    Iida, K.2    Saito, M.3    Nakayama, H.4    Yoshida, S.5
  • 99
    • 84860176878 scopus 로고    scopus 로고
    • Endogenous protein S-nitrosylation of E. Coli: Regulation by OxyR
    • Seth D, Hausladen A, Wang YJ, Stamler JS. 2012. Endogenous protein S-nitrosylation of E. Coli: regulation by OxyR. Science 336: 470-73
    • (2012) Science , vol.336 , pp. 470-473
    • Seth, D.1    Hausladen, A.2    Wang, Y.J.3    Stamler, J.S.4
  • 101
    • 78650114522 scopus 로고    scopus 로고
    • Activation of the SoxR regulon in Streptomyces colelicolor by the extracellular form of the pigmented antibiotic actinorhodin
    • Shin JH, Singh AK, Cheon DJ, Roe J-H. 2011. Activation of the SoxR regulon in Streptomyces colelicolor by the extracellular form of the pigmented antibiotic actinorhodin. J. Bacteriol. 193: 75-81
    • (2011) J. Bacteriol. , vol.193 , pp. 75-81
    • Shin, J.H.1    Singh, A.K.2    Cheon, D.J.3    Roe, J.-H.4
  • 103
    • 84899761386 scopus 로고    scopus 로고
    • Intracellular hydrogen peroxide and superoxide poison 3-deoxy-Darabinoheptulosonate 7-phosphate synthase, the first committed enzyme in the aromatic biosynthetic pathway of Escherichia coli
    • Sobota JM, Gu M, Imlay JA. 2014. Intracellular hydrogen peroxide and superoxide poison 3-deoxy-Darabinoheptulosonate 7-phosphate synthase, the first committed enzyme in the aromatic biosynthetic pathway of Escherichia coli. J. Bacteriol. 196: 1980-91
    • (2014) J. Bacteriol. , vol.196 , pp. 1980-1991
    • Sobota, J.M.1    Gu, M.2    Imlay, J.A.3
  • 104
    • 79953896180 scopus 로고    scopus 로고
    • Iron enzyme ribulose-5-phosphate 3-epimerase in Escherichia coli is rapidly damaged by hydrogen peroxide but can be protected by manganese
    • Sobota JM, Imlay JA. 2011. Iron enzyme ribulose-5-phosphate 3-epimerase in Escherichia coli is rapidly damaged by hydrogen peroxide but can be protected by manganese. PNAS 108: 5402-7
    • (2011) PNAS , vol.108 , pp. 5402-5407
    • Sobota, J.M.1    Imlay, J.A.2
  • 105
    • 84879993819 scopus 로고    scopus 로고
    • OxyR acts as a transcriptional repressor of hydrogen peroxideinducible antioxidant genes in Corynebacterium glutamicum R
    • Teramoto H, Inui M, Yukawa H. 2013. OxyR acts as a transcriptional repressor of hydrogen peroxideinducible antioxidant genes in Corynebacterium glutamicum R. FEBS J. 280: 3298-312
    • (2013) FEBS J. , vol.280 , pp. 3298-3312
    • Teramoto, H.1    Inui, M.2    Yukawa, H.3
  • 108
    • 0025369726 scopus 로고
    • SoxR, a locus governing a superoxide response regulon in Escherichia coli K-12
    • Tsaneva IR, Weiss B. 1990. SoxR, a locus governing a superoxide response regulon in Escherichia coli K-12. J. Bacteriol. 172: 4197-205
    • (1990) J. Bacteriol. , vol.172 , pp. 4197-4205
    • Tsaneva, I.R.1    Weiss, B.2
  • 109
    • 0022484538 scopus 로고
    • Occurrence, biochemistry, and physiology of phenazine pigment production
    • Turner JM, Messenger AJ. 1986. Occurrence, biochemistry, and physiology of phenazine pigment production. Adv. Microb. Physiol. 27: 211-75
    • (1986) Adv. Microb. Physiol. , vol.27 , pp. 211-275
    • Turner, J.M.1    Messenger, A.J.2
  • 110
    • 0037214441 scopus 로고    scopus 로고
    • Contrasting sensitivities of Escherichia coli aconitases A and B to oxidation and iron depletion
    • Varghese S, Tang Y, Imlay JA. 2003. Contrasting sensitivities of Escherichia coli aconitases A and B to oxidation and iron depletion. J. Bacteriol. 185: 221-30
    • (2003) J. Bacteriol. , vol.185 , pp. 221-230
    • Varghese, S.1    Tang, Y.2    Imlay, J.A.3
  • 111
    • 34247472147 scopus 로고    scopus 로고
    • Submicromolar hydrogen peroxide disrupts the ability of fur protein to control free-iron levels in Escherichia coli
    • Varghese S, Wu A, Park S, Imlay KRC, Imlay JA. 2007. Submicromolar hydrogen peroxide disrupts the ability of Fur protein to control free-iron levels in Escherichia coli. Mol. Microbiol. 64: 822-30
    • (2007) Mol. Microbiol. , vol.64 , pp. 822-830
    • Varghese, S.1    Wu, A.2    Park, S.3    Imlay, K.R.C.4    Imlay, J.A.5
  • 112
    • 73849089506 scopus 로고    scopus 로고
    • Endogenous phenazine antibiotics promote anaerobic survival of Pseudomonas aeruginosa via extracellular electron transfer
    • Wang Y, Kern SE, Newman DK. 2010. Endogenous phenazine antibiotics promote anaerobic survival of Pseudomonas aeruginosa via extracellular electron transfer. J. Bacteriol. 192: 365-69
    • (2010) J. Bacteriol. , vol.192 , pp. 365-369
    • Wang, Y.1    Kern, S.E.2    Newman, D.K.3
  • 113
    • 79960419185 scopus 로고    scopus 로고
    • Phenazine-1-carboxylic acid promotes bacterial biofilm development via ferrous iron acquisition
    • Wang Y, Wilks JC, Danhorn T, Ramos I, Croal L, Newman DK. 2011. Phenazine-1-carboxylic acid promotes bacterial biofilm development via ferrous iron acquisition. J. Bacteriol. 193: 3606-17
    • (2011) J. Bacteriol. , vol.193 , pp. 3606-3617
    • Wang, Y.1    Wilks, J.C.2    Danhorn, T.3    Ramos, I.4    Croal, L.5    Newman, D.K.6
  • 114
    • 41949137280 scopus 로고    scopus 로고
    • Crystal structure of the [2Fe-2S] oxidative-stress sensor SoxR bound to DNA
    • Watanabe S, Kita A, Kobayashi K, Miki K. 2008. Crystal structure of the [2Fe-2S] oxidative-stress sensor SoxR bound to DNA. PNAS 105: 4121-26
    • (2008) PNAS , vol.105 , pp. 4121-4126
    • Watanabe, S.1    Kita, A.2    Kobayashi, K.3    Miki, K.4
  • 115
    • 33845997473 scopus 로고    scopus 로고
    • Modeling the reactions of superoxide and myeloperoxidase in the neutrophil phagosome: Implications for microbial killing
    • Winterbourn CC, Hampton MB, Livesey JH, Kettle AJ. 2006. Modeling the reactions of superoxide and myeloperoxidase in the neutrophil phagosome: implications for microbial killing. J. Biol. Chem. 281: 39860-69
    • (2006) J. Biol. Chem. , vol.281 , pp. 39860-39869
    • Winterbourn, C.C.1    Hampton, M.B.2    Livesey, J.H.3    Kettle, A.J.4
  • 116
    • 0032865515 scopus 로고    scopus 로고
    • Reactivity of biologically important thiol compounds with superoxide and hydrogen peroxide
    • Winterbourn CC, Metodiewa D. 1999. Reactivity of biologically important thiol compounds with superoxide and hydrogen peroxide. Free Rad. Biol. Med. 27: 322-28
    • (1999) Free Rad. Biol. Med. , vol.27 , pp. 322-328
    • Winterbourn, C.C.1    Metodiewa, D.2
  • 117
    • 79952382558 scopus 로고    scopus 로고
    • The Escherichia coli K-12 MntR miniregulon includes dps, which encodes the major stationary-phase DNA-binding protein
    • Yamamoto K, Ishihama A, Busby SJ, Grainger DC. 2011. The Escherichia coli K-12 MntR miniregulon includes dps, which encodes the major stationary-phase DNA-binding protein. J. Bacteriol. 193: 1477-80
    • (2011) J. Bacteriol. , vol.193 , pp. 1477-1480
    • Yamamoto, K.1    Ishihama, A.2    Busby, S.J.3    Grainger, D.C.4
  • 118
    • 0032513362 scopus 로고    scopus 로고
    • Activation of the OxyR transcription factor by reversible disulfide bond formation
    • Zheng M, Aslund F, Storz G. 1998. Activation of the OxyR transcription factor by reversible disulfide bond formation. Science 279: 1718-21
    • (1998) Science , vol.279 , pp. 1718-1721
    • Zheng, M.1    Aslund, F.2    Storz, G.3
  • 120
    • 0034932337 scopus 로고    scopus 로고
    • DNAmicroarray-mediated transcriptional profiling of the Escherichia coli response to hydrogen peroxide
    • ZhengM, WangX, Templeton LJ, Smulski DR, LaRossa RA, Storz G. 2001. DNAmicroarray-mediated transcriptional profiling of the Escherichia coli response to hydrogen peroxide. J. Bacteriol. 183: 4562-70
    • (2001) J. Bacteriol. , vol.183 , pp. 4562-4570
    • Zheng, M.1    Wang, X.2    Templeton, L.J.3    Smulski, D.R.4    LaRossa, R.A.5    Storz, G.6
  • 121
    • 70349547204 scopus 로고    scopus 로고
    • Management of oxidative stress in Bacillus
    • Zuber P. 2009. Management of oxidative stress in Bacillus. Annu. Rev. Microbiol. 63: 575-97
    • (2009) Annu. Rev. Microbiol. , vol.63 , pp. 575-597
    • Zuber, P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.