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Volumn 194, Issue 15, 2012, Pages 3904-3912

Pseudomonas aeruginosa Thiol Peroxidase Protects against Hydrogen Peroxide Toxicity and Displays Atypical Patterns of Gene Regulation

Author keywords

[No Author keywords available]

Indexed keywords

HYDROGEN PEROXIDE; PEROXIDASE; RECOMBINANT PROTEIN; THIOL PEROXIDASE; UNCLASSIFIED DRUG;

EID: 84866342431     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00347-12     Document Type: Article
Times cited : (39)

References (54)
  • 1
    • 0032914295 scopus 로고    scopus 로고
    • The pKNOCK series of broad-host-range mobilizable suicide vectors for gene knockout and targeted DNA insertion into the chromosome of gram-negative bacteria
    • Alexeyev MF. 1999. The pKNOCK series of broad-host-range mobilizable suicide vectors for gene knockout and targeted DNA insertion into the chromosome of gram-negative bacteria. Biotechniques 26:824-828.
    • (1999) Biotechniques , vol.26 , pp. 824-828
    • Alexeyev, M.F.1
  • 2
    • 77949424963 scopus 로고    scopus 로고
    • A new antioxidant with dual functions as a peroxidase and chaperone in Pseudomonas aeruginosa
    • An BC, et al. 2010. A new antioxidant with dual functions as a peroxidase and chaperone in Pseudomonas aeruginosa. Mol. Cells 29:145-151.
    • (2010) Mol. Cells , vol.29 , pp. 145-151
    • An, B.C.1
  • 3
    • 0037646517 scopus 로고    scopus 로고
    • Catalytic mechanism of thiol peroxidase from Escherichia coli. Sulfenic acid formation and overoxidation of essential CYS61
    • Baker LM, Poole LB. 2003. Catalytic mechanism of thiol peroxidase from Escherichia coli. Sulfenic acid formation and overoxidation of essential CYS61. J. Biol. Chem. 278:9203-9211.
    • (2003) J. Biol. Chem , vol.278 , pp. 9203-9211
    • Baker, L.M.1    Poole, L.B.2
  • 4
    • 0035108401 scopus 로고    scopus 로고
    • Essential thioredoxin-dependent peroxiredoxin system from Helicobacter pylori: genetic and kinetic characterization
    • Baker LM, Raudonikiene A, Hoffman PS, Poole LB. 2001. Essential thioredoxin-dependent peroxiredoxin system from Helicobacter pylori: genetic and kinetic characterization. J. Bacteriol. 183:1961-1973.
    • (2001) J. Bacteriol , vol.183 , pp. 1961-1973
    • Baker, L.M.1    Raudonikiene, A.2    Hoffman, P.S.3    Poole, L.B.4
  • 5
    • 0016700103 scopus 로고
    • Analysis of the regulation of Escherichia coli alkaline phosphatase synthesis using deletions and phi80 transducing phages
    • Brickman E, Beckwith J. 1975. Analysis of the regulation of Escherichia coli alkaline phosphatase synthesis using deletions and phi80 transducing phages. J. Mol. Biol. 96:307-316.
    • (1975) J. Mol. Biol , vol.96 , pp. 307-316
    • Brickman, E.1    Beckwith, J.2
  • 6
    • 0028889269 scopus 로고
    • Cloning and characterization of the katB gene of Pseudomonas aeruginosa encoding a hydrogen peroxide-inducible catalase: purification of KatB, cellular localization, and demonstration that it is essential for optimal resistance to hydrogen peroxide
    • Brown SM, Howell ML, Vasil ML, Anderson AJ, Hassett DJ. 1995. Cloning and characterization of the katB gene of Pseudomonas aeruginosa encoding a hydrogen peroxide-inducible catalase: purification of KatB, cellular localization, and demonstration that it is essential for optimal resistance to hydrogen peroxide. J. Bacteriol. 177:6536-6544.
    • (1995) J. Bacteriol , vol.177 , pp. 6536-6544
    • Brown, S.M.1    Howell, M.L.2    Vasil, M.L.3    Anderson, A.J.4    Hassett, D.J.5
  • 7
    • 77956800564 scopus 로고    scopus 로고
    • Multidrug resistant Pseudomonas aeruginosa infection in children undergoing chemotherapy and hematopoietic stem cell transplantation
    • Caselli D, et al. 2010. Multidrug resistant Pseudomonas aeruginosa infection in children undergoing chemotherapy and hematopoietic stem cell transplantation. Haematologica 95:1612-1615.
    • (2010) Haematologica , vol.95 , pp. 1612-1615
    • Caselli, D.1
  • 8
    • 0029839215 scopus 로고    scopus 로고
    • Mutation and mutagenesis of thiol peroxidase of Escherichia coli and a new type of thiol peroxidase family
    • Cha MK, Kim HK, Kim IH. 1996. Mutation and mutagenesis of thiol peroxidase of Escherichia coli and a new type of thiol peroxidase family. J. Bacteriol. 178:5610-5614.
    • (1996) J. Bacteriol , vol.178 , pp. 5610-5614
    • Cha, M.K.1    Kim, H.K.2    Kim, I.H.3
  • 9
    • 0028845858 scopus 로고
    • Thioredoxin-linked "thiol peroxidase" from periplasmic space of Escherichia coli
    • Cha MK, Kim HK, Kim IH. 1995. Thioredoxin-linked "thiol peroxidase" from periplasmic space of Escherichia coli. J. Biol. Chem. 270:28635-28641.
    • (1995) J. Biol. Chem , vol.270 , pp. 28635-28641
    • Cha, M.K.1    Kim, H.K.2    Kim, I.H.3
  • 10
    • 1542335652 scopus 로고    scopus 로고
    • Escherichia coli periplasmic thiol peroxidase acts as lipid hydroperoxide peroxidase and the principal antioxidative function during anaerobic growth
    • Cha MK, Kim WC, Lim CJ, Kim K, Kim IH. 2004. Escherichia coli periplasmic thiol peroxidase acts as lipid hydroperoxide peroxidase and the principal antioxidative function during anaerobic growth. J. Biol. Chem. 279:8769-8778.
    • (2004) J. Biol. Chem , vol.279 , pp. 8769-8778
    • Cha, M.K.1    Kim, W.C.2    Lim, C.J.3    Kim, K.4    Kim, I.H.5
  • 11
    • 80052531397 scopus 로고    scopus 로고
    • Evaluation of the virulence of Xanthomonas campestris pv. campestris mutant strains lacking functional genes in the OxyR regulon
    • Charoenlap N, et al. 2011. Evaluation of the virulence of Xanthomonas campestris pv. campestris mutant strains lacking functional genes in the OxyR regulon. Curr. Microbiol. 63:232-237.
    • (2011) Curr. Microbiol , vol.63 , pp. 232-237
    • Charoenlap, N.1
  • 12
    • 22144475073 scopus 로고    scopus 로고
    • OxyR mediated compensatory expression between ahpC and katA and the significance of ahpC in protection from hydrogen peroxide in Xanthomonas campestris
    • Charoenlap N, et al. 2005. OxyR mediated compensatory expression between ahpC and katA and the significance of ahpC in protection from hydrogen peroxide in Xanthomonas campestris. FEMS Microbiol. Lett. 249:73-78.
    • (2005) FEMS Microbiol. Lett , vol.249 , pp. 73-78
    • Charoenlap, N.1
  • 13
    • 14044265674 scopus 로고    scopus 로고
    • Genetic and physiological analysis of the major OxyR-regulated katA from Xanthomonas campestris pv. phaseoli
    • Chauvatcharin N, et al. 2005. Genetic and physiological analysis of the major OxyR-regulated katA from Xanthomonas campestris pv. phaseoli. Microbiology 151:597-605.
    • (2005) Microbiology , vol.151 , pp. 597-605
    • Chauvatcharin, N.1
  • 14
    • 77956229209 scopus 로고    scopus 로고
    • Structural insight into the oxidation-sensing mechanism of the antibiotic resistance of regulator MexR
    • Chen H, et al. 2010. Structural insight into the oxidation-sensing mechanism of the antibiotic resistance of regulator MexR. EMBO Rep. 11:685-690.
    • (2010) EMBO Rep , vol.11 , pp. 685-690
    • Chen, H.1
  • 15
    • 31344471227 scopus 로고    scopus 로고
    • ohrR and ohr are the primary sensor/regulator and protective genes against organic hydroperoxide stress in Agrobacterium tumefaciens
    • Chuchue T, et al. 2006. ohrR and ohr are the primary sensor/regulator and protective genes against organic hydroperoxide stress in Agrobacterium tumefaciens. J. Bacteriol. 188:842-851.
    • (2006) J. Bacteriol , vol.188 , pp. 842-851
    • Chuchue, T.1
  • 16
    • 0037258943 scopus 로고    scopus 로고
    • Role of the thioredoxin system and the thiol-peroxidases Tpx and Bcp in mediating resistance to oxidative and nitrosative stress in Helicobacter pylori
    • Comtois SL, Gidley MD, Kelly DJ. 2003. Role of the thioredoxin system and the thiol-peroxidases Tpx and Bcp in mediating resistance to oxidative and nitrosative stress in Helicobacter pylori. Microbiology 149:121-129.
    • (2003) Microbiology , vol.149 , pp. 121-129
    • Comtois, S.L.1    Gidley, M.D.2    Kelly, D.J.3
  • 17
    • 34648813720 scopus 로고    scopus 로고
    • ROS as signalling molecules: mechanisms that generate specificity in ROS homeostasis
    • D'Autreaux B, Toledano MB. 2007. ROS as signalling molecules: mechanisms that generate specificity in ROS homeostasis. Nat. Rev. Mol. Cell Biol. 8:813-824.
    • (2007) Nat. Rev. Mol. Cell Biol , vol.8 , pp. 813-824
    • D'Autreaux, B.1    Toledano, M.B.2
  • 18
    • 0025277281 scopus 로고
    • Small, stable shuttle vectors for use in Xanthomonas
    • DeFeyter R, Kado CI, Gabriel DW. 1990. Small, stable shuttle vectors for use in Xanthomonas. Gene 88:65-72.
    • (1990) Gene , vol.88 , pp. 65-72
    • DeFeyter, R.1    Kado, C.I.2    Gabriel, D.W.3
  • 20
    • 38749140290 scopus 로고    scopus 로고
    • Peroxiredoxins in bacterial antioxidant defense
    • Dubbs JM, Mongkolsuk S. 2007. Peroxiredoxins in bacterial antioxidant defense. Subcell. Biochem. 44:143-193.
    • (2007) Subcell. Biochem , vol.44 , pp. 143-193
    • Dubbs, J.M.1    Mongkolsuk, S.2
  • 21
    • 0035685108 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa PAO1 kills Caenorhabditis elegans by cyanide poisoning
    • Gallagher LA, Manoil C. 2001. Pseudomonas aeruginosa PAO1 kills Caenorhabditis elegans by cyanide poisoning. J. Bacteriol. 183:6207-6214.
    • (2001) J. Bacteriol , vol.183 , pp. 6207-6214
    • Gallagher, L.A.1    Manoil, C.2
  • 23
    • 0032884073 scopus 로고    scopus 로고
    • Expression of the soxR gene of Pseudomonas aeruginosa is inducible during infection of burn wounds in mice and is required to cause efficient bacteremia
    • Ha U, Jin S. 1999. Expression of the soxR gene of Pseudomonas aeruginosa is inducible during infection of burn wounds in mice and is required to cause efficient bacteremia. Infect. Immun. 67:5324-5331.
    • (1999) Infect. Immun , vol.67 , pp. 5324-5331
    • Ha, U.1    Jin, S.2
  • 24
    • 0033907235 scopus 로고    scopus 로고
    • A protease-resistant catalase, KatA, released upon cell lysis during stationary phase is essential for aerobic survival of a Pseudomonas aeruginosa oxyR mutant at low cell densities
    • Hassett DJ, et al. 2000. A protease-resistant catalase, KatA, released upon cell lysis during stationary phase is essential for aerobic survival of a Pseudomonas aeruginosa oxyR mutant at low cell densities. J. Bacteriol. 182: 4557-4563.
    • (2000) J. Bacteriol , vol.182 , pp. 4557-4563
    • Hassett, D.J.1
  • 25
    • 0028809394 scopus 로고
    • Pseudomonas aeruginosa sodA and sodB mutants defective in manganese- and iron-cofactored superoxide dismutase activity demonstrate the importance of the ironcofactored form in aerobic metabolism
    • Hassett DJ, Schweizer HP, Ohman DE. 1995. Pseudomonas aeruginosa sodA and sodB mutants defective in manganese- and iron-cofactored superoxide dismutase activity demonstrate the importance of the ironcofactored form in aerobic metabolism. J. Bacteriol. 177:6330-6337.
    • (1995) J. Bacteriol , vol.177 , pp. 6330-6337
    • Hassett, D.J.1    Schweizer, H.P.2    Ohman, D.E.3
  • 26
    • 77953584289 scopus 로고    scopus 로고
    • Cellular responses of A549 alveolar epithelial cells to serially collected Pseudomonas aeruginosa from cystic fibrosis patients at different stages of pulmonary infection
    • Hawdon NA, et al. 2010. Cellular responses of A549 alveolar epithelial cells to serially collected Pseudomonas aeruginosa from cystic fibrosis patients at different stages of pulmonary infection. FEMS Immunol. Med. Microbiol. 59:207-220.
    • (2010) FEMS Immunol. Med. Microbiol , vol.59 , pp. 207-220
    • Hawdon, N.A.1
  • 27
    • 73649129891 scopus 로고    scopus 로고
    • The major 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, et al. 2010. The major 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: 381-390.
    • (2010) J. Bacteriol , vol.192 , pp. 381-390
    • Heo, Y.J.1
  • 28
    • 0032079338 scopus 로고    scopus 로고
    • The redox-regulated SoxR protein acts from a single DNA site as a repressor and an allosteric activator
    • Hidalgo E, Leautaud V, Demple B. 1998. The redox-regulated SoxR protein acts from a single DNA site as a repressor and an allosteric activator. EMBO J. 17:2629-2636.
    • (1998) EMBO J , vol.17 , pp. 2629-2636
    • Hidalgo, E.1    Leautaud, V.2    Demple, B.3
  • 29
    • 1042278885 scopus 로고    scopus 로고
    • Multiple thioredoxin-mediated routes to detoxify hydroperoxides in Mycobacterium tuberculosis
    • Jaeger T, et al. 2004. Multiple thioredoxin-mediated routes to detoxify hydroperoxides in Mycobacterium tuberculosis. Arch. Biochem. Biophys. 423:182-191.
    • (2004) Arch. Biochem. Biophys , vol.423 , pp. 182-191
    • Jaeger, T.1
  • 31
    • 77952098034 scopus 로고    scopus 로고
    • Mutations of ferric uptake regulator (fur) impair iron homeostasis, growth, oxidative stress survival, and virulence of Xanthomonas campestris pv. campestris
    • Jittawuttipoka T, Sallabhan R, Vattanaviboon P, Fuangthong M, Mongkolsuk S. 2010. Mutations of ferric uptake regulator (fur) impair iron homeostasis, growth, oxidative stress survival, and virulence of Xanthomonas campestris pv. campestris. Arch. Microbiol. 192:331-339.
    • (2010) Arch. Microbiol , vol.192 , pp. 331-339
    • Jittawuttipoka, T.1    Sallabhan, R.2    Vattanaviboon, P.3    Fuangthong, M.4    Mongkolsuk, S.5
  • 32
    • 0038352097 scopus 로고    scopus 로고
    • The role of Fe-S proteins in sensing and regulation in bacteria
    • Kiley PJ, Beinert H. 2003. The role of Fe-S proteins in sensing and regulation in bacteria. Curr. Opin. Microbiol. 6:181-185.
    • (2003) Curr. Opin. Microbiol , vol.6 , pp. 181-185
    • Kiley, P.J.1    Beinert, H.2
  • 33
    • 74749093665 scopus 로고    scopus 로고
    • IscR modulates catalase A (KatA) activity, peroxide resistance and full virulence of Pseudomonas aeruginosa PA14
    • Kim SH, Lee BY, Lau GW, Cho YH. 2009. IscR modulates catalase A (KatA) activity, peroxide resistance and full virulence of Pseudomonas aeruginosa PA14. J. Microbiol. Biotechnol. 19:1520-1526.
    • (2009) J. Microbiol. Biotechnol , vol.19 , pp. 1520-1526
    • Kim, S.H.1    Lee, B.Y.2    Lau, G.W.3    Cho, Y.H.4
  • 34
    • 0028793123 scopus 로고
    • Four new derivatives of the broad-host-range cloning vector pBBR1MCS, carrying different antibiotic-resistance cassettes
    • Kovach ME, et al. 1995. Four new derivatives of the broad-host-range cloning vector pBBR1MCS, carrying different antibiotic-resistance cassettes. Gene 166:175-176.
    • (1995) Gene , vol.166 , pp. 175-176
    • Kovach, M.E.1
  • 35
    • 72949110182 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa OspR is an oxidative stress sensing regulator that affects pigment production, antibiotic resistance and dissemination during infection
    • Lan L, Murray TS, Kazmierczak BI, He C. 2010. Pseudomonas aeruginosa OspR is an oxidative stress sensing regulator that affects pigment production, antibiotic resistance and dissemination during infection. Mol. Microbiol. 75:76-91.
    • (2010) Mol. Microbiol , vol.75 , pp. 76-91
    • Lan, L.1    Murray, T.S.2    Kazmierczak, B.I.3    He, C.4
  • 36
    • 36448991500 scopus 로고    scopus 로고
    • Clustal W and Clustal X version 2.0
    • Larkin MA, et al. 2007. Clustal W and Clustal X version 2.0. Bioinformatics 23:2947-2948.
    • (2007) Bioinformatics , vol.23 , pp. 2947-2948
    • Larkin, M.A.1
  • 37
    • 21544440596 scopus 로고    scopus 로고
    • KatA, the major catalase, is critical for osmoprotection and virulence in Pseudomonas aeruginosa PA14
    • Lee JS, Heo YJ, Lee JK, Cho YH. 2005. KatA, the major catalase, is critical for osmoprotection and virulence in Pseudomonas aeruginosa PA14. Infect. Immun. 73:4399-4403.
    • (2005) Infect. Immun , vol.73 , pp. 4399-4403
    • Lee, J.S.1    Heo, Y.J.2    Lee, J.K.3    Cho, Y.H.4
  • 38
    • 57349087129 scopus 로고    scopus 로고
    • Oxidant-responsive induction of the suf operon, encoding a Fe-S assembly system, through Fur and IscR in Escherichia coli
    • Lee KC, Yeo WS, Roe JH. 2008. Oxidant-responsive induction of the suf operon, encoding a Fe-S assembly system, through Fur and IscR in Escherichia coli. J. Bacteriol. 190:8244-8247.
    • (2008) J. Bacteriol , vol.190 , pp. 8244-8247
    • Lee, K.C.1    Yeo, W.S.2    Roe, J.H.3
  • 39
    • 0032980609 scopus 로고    scopus 로고
    • Bacterioferritin A modulates catalase A (KatA) activity and resistance to hydrogen peroxide in Pseudomonas aeruginosa
    • Ma JF, et al. 1999. Bacterioferritin A modulates catalase A (KatA) activity and resistance to hydrogen peroxide in Pseudomonas aeruginosa. J. Bacteriol. 181:3730-3742.
    • (1999) J. Bacteriol , vol.181 , pp. 3730-3742
    • Ma, J.F.1
  • 40
    • 0036841380 scopus 로고    scopus 로고
    • Broad-host-range cre-lox system for antibiotic marker recycling in gram-negative bacteria
    • Marx CJ, Lidstrom ME. 2002. Broad-host-range cre-lox system for antibiotic marker recycling in gram-negative bacteria. Biotechniques 33: 1062-1067.
    • (2002) Biotechniques , vol.33 , pp. 1062-1067
    • Marx, C.J.1    Lidstrom, M.E.2
  • 41
    • 0035157997 scopus 로고    scopus 로고
    • Genetic and physiological characterization of ohr, encoding a protein involved in organic hydroperoxide resistance in Pseudomonas aeruginosa
    • Ochsner UA, Hassett DJ, Vasil ML. 2001. Genetic and physiological characterization of ohr, encoding a protein involved in organic hydroperoxide resistance in Pseudomonas aeruginosa. J. Bacteriol. 183:773-778.
    • (2001) J. Bacteriol , vol.183 , pp. 773-778
    • Ochsner, U.A.1    Hassett, D.J.2    Vasil, M.L.3
  • 42
    • 0033874090 scopus 로고    scopus 로고
    • Role of the Pseudomonas aeruginosa oxyR-recG operon in oxidative stress defense andDNArepair: OxyR-dependent regulation of katB-ankB, ahpB, and ahpC-ahpF
    • Ochsner UA, Vasil ML, Alsabbagh E, Parvatiyar K, Hassett DJ. 2000. Role of the Pseudomonas aeruginosa oxyR-recG operon in oxidative stress defense andDNArepair: OxyR-dependent regulation of katB-ankB, ahpB, and ahpC-ahpF. J. Bacteriol. 182:4533-4544.
    • (2000) J. Bacteriol , vol.182 , pp. 4533-4544
    • Ochsner, U.A.1    Vasil, M.L.2    Alsabbagh, E.3    Parvatiyar, K.4    Hassett, D.J.5
  • 43
    • 78349231296 scopus 로고    scopus 로고
    • IscR regulates RNase LS activity by repressing rnlA transcription
    • Otsuka Y, et al. 2010. IscR regulates RNase LS activity by repressing rnlA transcription. Genetics 185:823-830.
    • (2010) Genetics , vol.185 , pp. 823-830
    • Otsuka, Y.1
  • 44
    • 65649152967 scopus 로고    scopus 로고
    • Differential roles of OxyR-controlled antioxidant enzymes alkyl hydroperoxide reductase (AhpCF) and catalase (KatB) in the protection of Pseudomonas aeruginosa against hydrogen peroxide in biofilm vs. planktonic culture
    • Panmanee W, Hassett DJ. 2009. Differential roles of OxyR-controlled antioxidant enzymes alkyl hydroperoxide reductase (AhpCF) and catalase (KatB) in the protection of Pseudomonas aeruginosa against hydrogen peroxide in biofilm vs. planktonic culture. FEMS Microbiol. Lett. 295:238-244.
    • (2009) FEMS Microbiol. Lett , vol.295 , pp. 238-244
    • Panmanee, W.1    Hassett, D.J.2
  • 45
    • 0036032183 scopus 로고    scopus 로고
    • OhrR, a transcription repressor that senses and responds to changes in organic peroxide levels in Xanthomonas campestris pv. phaseoli
    • Panmanee W, et al. 2002. OhrR, a transcription repressor that senses and responds to changes in organic peroxide levels in Xanthomonas campestris pv. phaseoli. Mol. Microbiol. 45:1647-1654.
    • (2002) Mol. Microbiol , vol.45 , pp. 1647-1654
    • Panmanee, W.1
  • 46
    • 33746896639 scopus 로고    scopus 로고
    • Functional and structural characterization of a thiol peroxidase from Mycobacterium tuberculosis
    • Rho BS, et al. 2006. Functional and structural characterization of a thiol peroxidase from Mycobacterium tuberculosis. J. Mol. Biol. 361:850-863.
    • (2006) J. Mol. Biol , vol.361 , pp. 850-863
    • Rho, B.S.1
  • 47
    • 0035909963 scopus 로고    scopus 로고
    • IscR, an Fe-S cluster-containing transcription factor, represses expression of Escherichia coli genes encoding Fe-S cluster assembly proteins
    • Schwartz CJ, et al. 2001. IscR, an Fe-S cluster-containing transcription factor, represses expression of Escherichia coli genes encoding Fe-S cluster assembly proteins. Proc. Natl. Acad. Sci. U. S. A. 98:14895-14900.
    • (2001) Proc. Natl. Acad. Sci. U. S. A , vol.98 , pp. 14895-14900
    • Schwartz, C.J.1
  • 48
    • 39749141713 scopus 로고    scopus 로고
    • Comparative study of catalase-peroxidases (KatGs)
    • Singh R, et al. 2008. Comparative study of catalase-peroxidases (KatGs). Arch. Biochem. Biophys. 471:207-214.
    • (2008) Arch. Biochem. Biophys , vol.471 , pp. 207-214
    • Singh, R.1
  • 49
    • 0034739007 scopus 로고    scopus 로고
    • Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen
    • Stover CK, et al. 2000. Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen. Nature 406:959-964.
    • (2000) Nature , vol.406 , pp. 959-964
    • Stover, C.K.1
  • 50
    • 0037095620 scopus 로고    scopus 로고
    • Diversity of properties among catalases
    • Switala J, Loewen PC. 2002. Diversity of properties among catalases. Arch. Biochem. Biophys. 401:145-154.
    • (2002) Arch. Biochem. Biophys , vol.401 , pp. 145-154
    • Switala, J.1    Loewen, P.C.2
  • 51
    • 0033582314 scopus 로고    scopus 로고
    • Killing of Caenorhabditis elegans by Pseudomonas aeruginosa used to model mammalian bacterial pathogenesis
    • Tan MW, Mahajan-Miklos S, Ausubel FM. 1999. Killing of Caenorhabditis elegans by Pseudomonas aeruginosa used to model mammalian bacterial pathogenesis. Proc. Natl. Acad. Sci. U. S. A. 96:715-720.
    • (1999) Proc. Natl. Acad. Sci. U. S. A , vol.96 , pp. 715-720
    • Tan, M.W.1    Mahajan-Miklos, S.2    Ausubel, F.M.3
  • 52
    • 65449152830 scopus 로고    scopus 로고
    • Inactivation of thioredoxin-like gene alters oxidative stress resistance and reduces cytochrome c oxidase activity in Agrobacterium tumefaciens
    • Tanboon W, Chuchue T, Vattanaviboon P, Mongkolsuk S. 2009. Inactivation of thioredoxin-like gene alters oxidative stress resistance and reduces cytochrome c oxidase activity in Agrobacterium tumefaciens. FEMS Microbiol. Lett. 295:110-116.
    • (2009) FEMS Microbiol. Lett , vol.295 , pp. 110-116
    • Tanboon, W.1    Chuchue, T.2    Vattanaviboon, P.3    Mongkolsuk, S.4
  • 53
    • 54249104170 scopus 로고    scopus 로고
    • Subcellular localization and in vivo oxidation-reduction kinetics of thiol peroxidase in Escherichia coli
    • Tao K. 2008. Subcellular localization and in vivo oxidation-reduction kinetics of thiol peroxidase in Escherichia coli. FEMS Microbiol. Lett. 289: 41-45.
    • (2008) FEMS Microbiol. Lett , vol.289 , pp. 41-45
    • Tao, K.1
  • 54
    • 33745187803 scopus 로고    scopus 로고
    • IscR acts as an activator in response to oxidative stress for the suf operon encoding Fe-S assembly proteins
    • Yeo WS, Lee JH, Lee KC, Roe JH. 2006. IscR acts as an activator in response to oxidative stress for the suf operon encoding Fe-S assembly proteins. Mol. Microbiol. 61:206-218.
    • (2006) Mol. Microbiol , vol.61 , pp. 206-218
    • Yeo, W.S.1    Lee, J.H.2    Lee, K.C.3    Roe, J.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.