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Volumn 193, Issue 9, 2011, Pages 2186-2196

The YaaA protein of the Escherichia coli OxyR regulon lessens hydrogen peroxide toxicity by diminishing the amount of intracellular unincorporated iron

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL DNA; BACTERIAL PROTEIN; CATALASE; HYDROGEN PEROXIDE; HYDROXYL RADICAL; IRON; IRON CHELATE; PEROXIDASE; UNCLASSIFIED DRUG; YAAA PROTEIN;

EID: 79955542589     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00001-11     Document Type: Article
Times cited : (61)

References (60)
  • 1
    • 0017684046 scopus 로고
    • Repair of hydrogen peroxide-induced single-strand breaks in Escherichia coli deoxyribonucleic acid
    • Ananthaswamy, H. N., and A. Eisenstark. 1977. Repair of hydrogen peroxide-induced single-strand breaks in Escherichia coli deoxyribonucleic acid. J. Bacteriol. 130:187-191.
    • (1977) J. Bacteriol. , vol.130 , pp. 187-191
    • Ananthaswamy, H.N.1    Eisenstark, A.2
  • 2
    • 65549107862 scopus 로고    scopus 로고
    • Manganese import is a key element of the OxyR response to hydrogen peroxide in Escherichia coli
    • Anjem, A., S. Varghese, and J. A. Imlay. 2009. Manganese import is a key element of the OxyR response to hydrogen peroxide in Escherichia coli. Mol. Microbiol. 72:844-858.
    • (2009) Mol. Microbiol. , vol.72 , pp. 844-858
    • Anjem, A.1    Varghese, S.2    Imlay, J.A.3
  • 3
    • 0032994431 scopus 로고    scopus 로고
    • Regulation of the OxyR transcriptional factor by hydrogen peroxide and the cellular thioldisulfide status
    • Aslund, F., M. Zheng, J. Beckwith, and G. Storz. 1999. Regulation of the OxyR transcriptional factor by hydrogen peroxide and the cellular thioldisulfide status. Proc. Natl. Acad. Sci. U. S. A. 96:6161-6165.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 6161-6165
    • Aslund, F.1    Zheng, M.2    Beckwith, J.3    Storz, G.4
  • 4
    • 34547852400 scopus 로고    scopus 로고
    • NOX family NADPH oxidases: not just in mammals
    • Bedard, K., B. Lardy, and K.-H. Krause. 2007. NOX family NADPH oxidases: not just in mammals. Biochimie 89:1107-1112.
    • (2007) Biochimie , vol.89 , pp. 1107-1112
    • Bedard, K.1    Lardy, B.2    Krause, K.-H.3
  • 5
    • 0037046523 scopus 로고    scopus 로고
    • Ocean productivity before about 1.9 Gyr ago limited by phosphorus adsorption onto iron oxides
    • Bjerrum, C. J., and D. E. Canfield. 2002. Ocean productivity before about 1.9 Gyr ago limited by phosphorus adsorption onto iron oxides. Nature 417:159-162.
    • (2002) Nature , vol.417 , pp. 159-162
    • Bjerrum, C.J.1    Canfield, D.E.2
  • 6
    • 3142749997 scopus 로고    scopus 로고
    • Iron uptake by Escherichia coli
    • Braun, V. 2003. Iron uptake by Escherichia coli. Front. Biosci. 1:s1409-s1421.
    • (2003) Front. Biosci. , vol.1
    • Braun, V.1
  • 7
    • 0022683672 scopus 로고
    • Isolation of superoxide dismutase mutants in Escherichia coli: is superoxide dismutase necessary for aerobic life?
    • Carlioz, A., and D. Touati. 1986. Isolation of superoxide dismutase mutants in Escherichia coli: is superoxide dismutase necessary for aerobic life? EMBO J. 5:623-630.
    • (1986) EMBO J , vol.5 , pp. 623-630
    • Carlioz, A.1    Touati, D.2
  • 8
    • 0017807890 scopus 로고
    • Construction and characterization of amplifiable multicopy DNA cloning vehicles derived from the P15A cryptic miniplasmid
    • Chang, A. C., and S. N. Cohen. 1978. Construction and characterization of amplifiable multicopy DNA cloning vehicles derived from the P15A cryptic miniplasmid. J. Bacteriol. 134:1141-1156.
    • (1978) J. Bacteriol. , vol.134 , pp. 1141-1156
    • Chang, A.C.1    Cohen, S.N.2
  • 9
    • 0029065955 scopus 로고
    • Gene disruption in Escherichia coli: TcR and KmR cassettes with the option of Flp-catalyzed excision of the antibiotic-resistance determinant
    • Cherepanov, P. P., and W. Wackernagel. 1995. Gene disruption in Escherichia coli: TcR and KmR cassettes with the option of Flp-catalyzed excision of the antibiotic-resistance determinant. Gene 158:9-14.
    • (1995) Gene , vol.158 , pp. 9-14
    • Cherepanov, P.P.1    Wackernagel, W.2
  • 10
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K. A., and B. L. Wanner. 2000. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. U. S. A. 97:6640-6645.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 11
    • 75549090603 scopus 로고    scopus 로고
    • The Pfam protein families database
    • Finn, R. D., et al. 2010. The Pfam protein families database. Nucleic Acids Res. 38:D211-D222.
    • (2010) Nucleic Acids Res , vol.38
    • Finn, R.D.1
  • 12
    • 0027491617 scopus 로고
    • The inactivation of Fe-S cluster containing hydro-lyases by superoxide
    • Flint, D. H., J. F. Tuminello, and M. H. Emptage. 1993. The inactivation of Fe-S cluster containing hydro-lyases by superoxide. J. Biol. Chem. 268: 22369-22376.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22369-22376
    • Flint, D.H.1    Tuminello, J.F.2    Emptage, M.H.3
  • 13
    • 0022870573 scopus 로고
    • The respiratory burst oxidase of human neutrophils. Further studies of the purified enzyme
    • Glass, G. A., et al. 1986. The respiratory burst oxidase of human neutrophils. Further studies of the purified enzyme. J. Biol. Chem. 261:13247-13251.
    • (1986) J. Biol. Chem. , vol.261 , pp. 13247-13251
    • Glass, G.A.1
  • 14
    • 0031959912 scopus 로고    scopus 로고
    • The crystal structure of Dps, a ferritin homolog that binds and protects DNA
    • Grant, R. A., D. J. Filman, S. E. Finkel, R. Kolter, and J. M. Hogle. 1998. The crystal structure of Dps, a ferritin homolog that binds and protects DNA. Nat. Struct. Biol. 5:294-303.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 294-303
    • Grant, R.A.1    Filman, D.J.2    Finkel, S.E.3    Kolter, R.4    Hogle, J.M.5
  • 15
    • 12444299959 scopus 로고    scopus 로고
    • FieF (YiiP) from Escherichia coli mediates decreased cellular accumulation of iron and relieves iron stress
    • Grass, G., et al. 2005. FieF (YiiP) from Escherichia coli mediates decreased cellular accumulation of iron and relieves iron stress. Arch. Microbiol. 183: 9-18.
    • (2005) Arch. Microbiol. , vol.183 , pp. 9-18
    • Grass, G.1
  • 16
    • 0025078495 scopus 로고
    • Positive control of a global antioxidant defense regulon activated by superoxide-generating agents in Escherichia coli
    • Greenberg, J. T., P. Monach, J. H. Chou, P. D. Josephy, and B. Demple. 1990. Positive control of a global antioxidant defense regulon activated by superoxide-generating agents in Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 87:6181-6185.
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 6181-6185
    • Greenberg, J.T.1    Monach, P.2    Chou, J.H.3    Josephy, P.D.4    Demple, B.5
  • 18
    • 0035682064 scopus 로고    scopus 로고
    • Conditional-replication, integration, excision, and retrieval plasmid-host systems for gene structure-function studies of bacteria
    • Haldimann, A., and B. L. Wanner. 2001. Conditional-replication, integration, excision, and retrieval plasmid-host systems for gene structure-function studies of bacteria. J. Bacteriol. 183:6384-6393.
    • (2001) J. Bacteriol. , vol.183 , pp. 6384-6393
    • Haldimann, A.1    Wanner, B.L.2
  • 19
    • 0037020069 scopus 로고    scopus 로고
    • Iron incorporation into Escherichia coli Dps gives rise to a ferritin-like microcrystalline core
    • Ilari, A., P. Ceci, D. Ferrari, G. Rossi, and E. Chiancone. 2002. Iron incorporation into Escherichia coli Dps gives rise to a ferritin-like microcrystalline core. J. Biol. Chem. 277:37619-37623.
    • (2002) J. Biol. Chem. , vol.277 , pp. 37619-37623
    • Ilari, A.1    Ceci, P.2    Ferrari, D.3    Rossi, G.4    Chiancone, E.5
  • 20
    • 0023905646 scopus 로고
    • Toxic DNA damage by hydrogen peroxide through the Fenton reaction in vivo and in vitro
    • Imlay, J. A., S. M. Chin, and S. Linn. 1988. Toxic DNA damage by hydrogen peroxide through the Fenton reaction in vivo and in vitro. Science 240:640-642.
    • (1988) Science , vol.240 , pp. 640-642
    • Imlay, J.A.1    Chin, S.M.2    Linn, S.3
  • 21
    • 0025800392 scopus 로고
    • Assay of metabolic superoxide production in Escherichia coli
    • Imlay, J. A., and I. Fridovich. 1991. Assay of metabolic superoxide production in Escherichia coli. J. Biol. Chem. 266:6957-6965.
    • (1991) J. Biol. Chem. , vol.266 , pp. 6957-6965
    • Imlay, J.A.1    Fridovich, I.2
  • 22
    • 1642498276 scopus 로고    scopus 로고
    • Cytotoxic action of juglone and plumbagin: a mechanistic study using HaCaT keratinocytes
    • Inbaraj, J. J., and C. F. Chignell. 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
  • 23
    • 33847753939 scopus 로고    scopus 로고
    • Micromolar intracellular hydrogen peroxide disrupts metabolism by damaging iron-sulfur enzymes
    • Jang, S., and J. A. Imlay. 2007. Micromolar intracellular hydrogen peroxide disrupts metabolism by damaging iron-sulfur enzymes. J. Biol. Chem. 282: 929-937.
    • (2007) J. Biol. Chem. , vol.282 , pp. 929-937
    • Jang, S.1    Imlay, J.A.2
  • 24
    • 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., and J. A. Imlay. 2010. Hydrogen peroxide inactivates the Escherichia coli Isc iron-sulphur assembly system, and OxyR induces the Suf system to compensate. Mol. Microbiol. 78:1448-1467.
    • (2010) Mol. Microbiol. , vol.78 , pp. 1448-1467
    • Jang, S.1    Imlay, J.A.2
  • 26
    • 0030465238 scopus 로고    scopus 로고
    • Superoxide accelerates DNA damage by elevating free-iron levels
    • Keyer, K., and J. A. Imlay. 1996. Superoxide accelerates DNA damage by elevating free-iron levels. Proc. Natl. Acad. Sci. U. S. A. 93:13635-13640.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 13635-13640
    • Keyer, K.1    Imlay, J.A.2
  • 27
    • 33749017348 scopus 로고    scopus 로고
    • Detection and quantification of superoxide formed within the periplasm of Escherichia coli
    • Korshunov, S., and J. A. Imlay. 2006. Detection and quantification of superoxide formed within the periplasm of Escherichia coli. J. Bacteriol. 188: 6326-6334.
    • (2006) J. Bacteriol. , vol.188 , pp. 6326-6334
    • Korshunov, S.1    Imlay, J.A.2
  • 28
    • 77949342990 scopus 로고    scopus 로고
    • Two sources of endogenous hydrogen peroxide in Escherichia coli
    • Korshunov, S., and J. A. Imlay. 2010. Two sources of endogenous hydrogen peroxide in Escherichia coli. Mol. Microbiol. 75:1389-1401.
    • (2010) Mol. Microbiol. , vol.75 , pp. 1389-1401
    • Korshunov, S.1    Imlay, J.A.2
  • 29
    • 0028965108 scopus 로고
    • Mutational analysis of the redox-sensitive transcriptional regulator OxyR: regions important for oxidation and transcriptional activation
    • Kullik, I., M. B. Toledano, L. A. Tartaglia, and G. Storz. 1995. Mutational analysis of the redox-sensitive transcriptional regulator OxyR: regions important for oxidation and transcriptional activation. J. Bacteriol. 177:1275-1284.
    • (1995) J. Bacteriol. , vol.177 , pp. 1275-1284
    • Kullik, I.1    Toledano, M.B.2    Tartaglia, L.A.3    Storz, G.4
  • 30
    • 0023178381 scopus 로고
    • α,β-Dihydroxyisovalerate dehydratase: a superoxide-sensitive enzyme
    • Kuo, C. F., T. Mashino, and I. Fridovich. 1987. α,β-Dihydroxyisovalerate dehydratase: a superoxide-sensitive enzyme. J. Biol. Chem. 262:4724-4727.
    • (1987) J. Biol. Chem. , vol.262 , pp. 4724-4727
    • Kuo, C.F.1    Mashino, T.2    Fridovich, I.3
  • 31
    • 16544369973 scopus 로고    scopus 로고
    • Redox regulation of OxyR requires specific disulfide bond formation involving a rapid kinetic reaction path
    • Lee, C., et al. 2004. Redox regulation of OxyR requires specific disulfide bond formation involving a rapid kinetic reaction path. Nat. Struct. Mol. Biol. 11:1179-1185.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 1179-1185
    • Lee, C.1
  • 32
    • 1642565394 scopus 로고    scopus 로고
    • Induction of the sufA operon encoding Fe-S assembly proteins by superoxide generators and hydrogen peroxide: involvement of OxyR, IHF and an unidentified oxidant-responsive factor
    • Lee, J. H., W. S. Yeo, and J. H. Roe. 2004. Induction of the sufA operon encoding Fe-S assembly proteins by superoxide generators and hydrogen peroxide: involvement of OxyR, IHF and an unidentified oxidant-responsive factor. Mol. Microbiol. 51:1745-1755.
    • (2004) Mol. Microbiol. , vol.51 , pp. 1745-1755
    • Lee, J.H.1    Yeo, W.S.2    Roe, J.H.3
  • 33
    • 33947364844 scopus 로고    scopus 로고
    • Intracellular copper does not catalyze the formation of oxidative DNA damage in Escherichia coli
    • Macomber, L., C. Rensing, and J. A. Imlay. 2007. Intracellular copper does not catalyze the formation of oxidative DNA damage in Escherichia coli. J. Bacteriol. 189:1616-1626.
    • (2007) J. Bacteriol. , vol.189 , pp. 1616-1626
    • Macomber, L.1    Rensing, C.2    Imlay, J.A.3
  • 35
    • 0027951017 scopus 로고
    • Active oxygen species in plant defense against pathogens
    • Mehdy, M. C. 1994. Active oxygen species in plant defense against pathogens. Plant Physiol. 105:467-472.
    • (1994) Plant Physiol , vol.105 , pp. 467-472
    • Mehdy, M.C.1
  • 36
    • 0033538048 scopus 로고    scopus 로고
    • The identification of primary sites of superoxide and hydrogen peroxide formation in the aerobic respiratory chain and sulfite reductase complex of Escherichia coli
    • Messner, K. R., and J. A. Imlay. 1999. The identification of primary sites of superoxide and hydrogen peroxide formation in the aerobic respiratory chain and sulfite reductase complex of Escherichia coli. J. Biol. Chem. 274:10119-10128.
    • (1999) J. Biol. Chem. , vol.274 , pp. 10119-10128
    • Messner, K.R.1    Imlay, J.A.2
  • 37
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Miller, J. H. 1972. Experiments in molecular genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1972) Experiments in molecular genetics
    • Miller, J.H.1
  • 38
    • 2442567822 scopus 로고    scopus 로고
    • A suf operon requirement for Fe-S cluster assembly during iron starvation in Escherichia coli
    • Outten, F. W., O. Djaman, and G. Storz. 2004. A suf operon requirement for Fe-S cluster assembly during iron starvation in Escherichia coli. Mol. Microbiol. 52:861-872.
    • (2004) Mol. Microbiol. , vol.52 , pp. 861-872
    • Outten, F.W.1    Djaman, O.2    Storz, G.3
  • 39
    • 0037336269 scopus 로고    scopus 로고
    • High levels of intracellular cysteine promote oxidative DNA damage by driving the Fenton reaction
    • Park, S., and J. A. Imlay. 2003. High levels of intracellular cysteine promote oxidative DNA damage by driving the Fenton reaction. J. Bacteriol. 185: 1942-1950.
    • (2003) J. Bacteriol. , vol.185 , pp. 1942-1950
    • Park, S.1    Imlay, J.A.2
  • 40
    • 21544465580 scopus 로고    scopus 로고
    • Substantial DNA damage from submicromolar intracellular hydrogen peroxide detected in Hpx-mutants of Escherichia coli
    • Park, S., X. You, and J. A. Imlay. 2005. Substantial DNA damage from submicromolar intracellular hydrogen peroxide detected in Hpx-mutants of Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 102:9317-9322.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 9317-9322
    • Park, S.1    You, X.2    Imlay, J.A.3
  • 41
    • 77952843550 scopus 로고    scopus 로고
    • A new model for SOS-induced mutagenesis: how RecA protein activates DNA polymerase V
    • Patel, M., Q. Jiang, R. Woodgate, M. M. Cox, and M. F. Goodman. 2010. A new model for SOS-induced mutagenesis: how RecA protein activates DNA polymerase V. Crit. Rev. Biochem. Mol. Biol. 45:171-184.
    • (2010) Crit. Rev. Biochem. Mol. Biol. , vol.45 , pp. 171-184
    • Patel, M.1    Jiang, Q.2    Woodgate, R.3    Cox, M.M.4    Goodman, M.F.5
  • 42
    • 0034595617 scopus 로고    scopus 로고
    • Lack of a role for iron in the Lyme disease pathogen
    • Posey, J. E., and F. C. Gherardini. 2000. Lack of a role for iron in the Lyme disease pathogen. Science 288:1651-1653.
    • (2000) Science , vol.288 , pp. 1651-1653
    • Posey, J.E.1    Gherardini, F.C.2
  • 43
    • 0035209075 scopus 로고    scopus 로고
    • Alkyl hydroperoxide reductase is the primary scavenger of endogenous hydrogen peroxide in Escherichia coli
    • Seaver, L. C., and J. A. Imlay. 2001. Alkyl hydroperoxide reductase is the primary scavenger of endogenous hydrogen peroxide in Escherichia coli. J. Bacteriol. 183:7173-7181.
    • (2001) J. Bacteriol. , vol.183 , pp. 7173-7181
    • Seaver, L.C.1    Imlay, J.A.2
  • 44
    • 0035212036 scopus 로고    scopus 로고
    • Hydrogen peroxide fluxes and compartmentalization inside growing Escherichia coli
    • Seaver, L. C., and J. A. Imlay. 2001. Hydrogen peroxide fluxes and compartmentalization inside growing Escherichia coli. J. Bacteriol. 183:7182-7189.
    • (2001) J. Bacteriol. , vol.183 , pp. 7182-7189
    • Seaver, L.C.1    Imlay, J.A.2
  • 45
    • 10344238617 scopus 로고    scopus 로고
    • Are respiratory enzymes the primary sources of intracellular hydrogen peroxide?
    • Seaver, L. C., and J. A. Imlay. 2004. Are respiratory enzymes the primary sources of intracellular hydrogen peroxide? J. Biol. Chem. 279:48742-48750.
    • (2004) J. Biol. Chem. , vol.279 , pp. 48742-48750
    • Seaver, L.C.1    Imlay, J.A.2
  • 46
    • 79953896180 scopus 로고    scopus 로고
    • Posting date. Iron enzyme ribulose-5-phosphate 3-epimerase in Escherichia coli is rapidly damaged by hydrogen peroxide but can be protected by manganese
    • 14 March, doi:10.1073/pnas.1100410108
    • Sobota, J. M., and J. A. Imlay. 14 March 2011, posting date. Iron enzyme ribulose-5-phosphate 3-epimerase in Escherichia coli is rapidly damaged by hydrogen peroxide but can be protected by manganese. Proc. Natl. Acad. Sci. U. S. A. doi:10.1073/pnas.1100410108.
    • (2011) Proc. Natl. Acad. Sci. U. S. A
    • Sobota, J.M.1    Imlay, J.A.2
  • 47
    • 0032790525 scopus 로고    scopus 로고
    • Identification of and hydrogen peroxide production by fecal and vaginal lactobacilli isolated from Japanese women and newborn infants
    • Song, Y.-L., et al. 1999. Identification of and hydrogen peroxide production by fecal and vaginal lactobacilli isolated from Japanese women and newborn infants. J. Clin. Microbiol. 37:3062-3064.
    • (1999) J. Clin. Microbiol. , vol.37 , pp. 3062-3064
    • Song, Y.-L.1
  • 48
    • 0029041226 scopus 로고
    • Lethal oxidative damage and mutagenesis are generated by iron in delta fur mutants of Escherichia coli: protective role of superoxide dismutase
    • Touati, D., M. Jacques, B. Tardat, L. Bouchard, and S. Despied. 1995. Lethal oxidative damage and mutagenesis are generated by iron in delta fur mutants of Escherichia coli: protective role of superoxide dismutase. J. Bacteriol. 177:2305-2314.
    • (1995) J. Bacteriol. , vol.177 , pp. 2305-2314
    • Touati, D.1    Jacques, M.2    Tardat, B.3    Bouchard, L.4    Despied, S.5
  • 49
    • 0025369726 scopus 로고
    • soxR, a locus governing a superoxide response regulon in Escherichia coli K-12
    • Tsaneva, I. R., and B. Weiss. 1990. soxR, a locus governing a superoxide response regulon in Escherichia coli K-12. J. Bacteriol. 172:4197-4205.
    • (1990) J. Bacteriol. , vol.172 , pp. 4197-4205
    • Tsaneva, I.R.1    Weiss, B.2
  • 50
    • 0022484538 scopus 로고
    • Occurrence, biochemistry, and physiology of phenazine pigment production
    • Turner, J. M., and A. J. Messenger. 1986. Occurrence, biochemistry, and physiology of phenazine pigment production. Adv. Microb. Physiol. 27:211-275.
    • (1986) Adv. Microb. Physiol. , vol.27 , pp. 211-275
    • Turner, J.M.1    Messenger, A.J.2
  • 51
    • 34247472147 scopus 로고    scopus 로고
    • Submicromolar hydrogen peroxide disrupts the ability of Fur protein to control free-iron levels in Escherichia coli
    • Varghese, S., A. Wu, S. Park, K. R. C. Imlay, and J. A. Imlay. 2007. Submicromolar hydrogen peroxide disrupts the ability of Fur protein to control free-iron levels in Escherichia coli. Mol. Microbiol. 64:822-830.
    • (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
  • 52
    • 0025782890 scopus 로고
    • Construction of versatile low-copynumber vectors for cloning, sequencing and gene expression in Escherichia coli
    • Wang, R. F., and S. R. Kushner. 1991. Construction of versatile low-copynumber vectors for cloning, sequencing and gene expression in Escherichia coli. Gene 100:195-199.
    • (1991) Gene , vol.100 , pp. 195-199
    • Wang, R.F.1    Kushner, S.R.2
  • 53
    • 23044489264 scopus 로고    scopus 로고
    • TonB-dependent outer membrane transport: going for baroque?
    • Wiener, M. C. 2005. TonB-dependent outer membrane transport: going for baroque? Curr. Opin. Struct. Biol. 15:294-400.
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 294-400
    • Wiener, M.C.1
  • 54
    • 0036125229 scopus 로고    scopus 로고
    • Quantitation of intracellular free iron by electron paramagnetic resonance spectroscopy
    • Woodmansee, A. L., and J. A. Imlay. 2002. Quantitation of intracellular free iron by electron paramagnetic resonance spectroscopy. Methods Enzymol. 349:3-9.
    • (2002) Methods Enzymol , vol.349 , pp. 3-9
    • Woodmansee, A.L.1    Imlay, J.A.2
  • 55
    • 0037072770 scopus 로고    scopus 로고
    • Reduced flavins promote oxidative DNA damage in non-respiring Escherichia coli by delivering electrons to intracellular free iron
    • Woodmansee, A. N., and J. A. Imlay. 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.
    • (2002) J. Biol. Chem. , vol.277 , pp. 34055-34066
    • Woodmansee, A.N.1    Imlay, J.A.2
  • 56
    • 0037008743 scopus 로고    scopus 로고
    • Iron and hydrogen peroxide detoxification properties of DNA-binding protein from starved cells. A ferritin-like DNA-binding protein of Escherichia coli
    • Zhao, G., et al. 2002. Iron and hydrogen peroxide detoxification properties of DNA-binding protein from starved cells. A ferritin-like DNA-binding protein of Escherichia coli. J. Biol. Chem. 277:27689-27696.
    • (2002) J. Biol. Chem. , vol.277 , pp. 27689-27696
    • Zhao, G.1
  • 57
    • 0032513362 scopus 로고    scopus 로고
    • Activation of the OxyR transcription factor by reversible disulfide bond formation
    • Zheng, M., F. Aslund, and G. Storz. 1998. Activation of the OxyR transcription factor by reversible disulfide bond formation. Science 279:1718-1721.
    • (1998) Science , vol.279 , pp. 1718-1721
    • Zheng, M.1    Aslund, F.2    Storz, G.3
  • 59
    • 0034932337 scopus 로고    scopus 로고
    • DNA microarray-mediated transcriptional profiling of the Escherichia coli response to hydrogen peroxide
    • Zheng, M., et al. 2001. DNA microarray-mediated transcriptional profiling of the Escherichia coli response to hydrogen peroxide. J. Bacteriol. 183:4562-4570.
    • (2001) J. Bacteriol. , vol.183 , pp. 4562-4570
    • Zheng, M.1
  • 60
    • 0034943657 scopus 로고    scopus 로고
    • Computation-directed identification of OxyR DNA binding sites in Escherichia coli
    • Zheng, M., et al. 2001. Computation-directed identification of OxyR DNA binding sites in Escherichia coli. J. Bacteriol. 183:4571-4579.
    • (2001) J. Bacteriol. , vol.183 , pp. 4571-4579
    • Zheng, M.1


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