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Volumn 80, Issue 2, 2011, Pages 319-334

The alternative aerobic ribonucleotide reductase of Escherichia coli, NrdEF, is a manganese-dependent enzyme that enables cell replication during periods of iron starvation

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; FERRIC UPTAKE REGULATOR; HYDROGEN PEROXIDE; IRON; MANGANESE; RIBONUCLEOTIDE REDUCTASE; RIBONUCLEOTIDE REDUCTASE AB; RIBONUCLEOTIDE REDUCTASE EF; UNCLASSIFIED DRUG; YFAE PROTEIN;

EID: 79953850801     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2011.07593.x     Document Type: Article
Times cited : (113)

References (63)
  • 1
    • 70450237171 scopus 로고    scopus 로고
    • Electron paramagnetic resonance (EPR) spectroscopy of the stable-free radical in the native metallo-cofactor of the manganese-ribonucleotide reductase (Mn-RNR) of Corynebacterium glutamicum
    • Abbouni, B., Oehlmann, W., Stolle, P., Pierik, A.J., and Auling, G. (2009) Electron paramagnetic resonance (EPR) spectroscopy of the stable-free radical in the native metallo-cofactor of the manganese-ribonucleotide reductase (Mn-RNR) of Corynebacterium glutamicum. Free Radic Res 43: 943-950.
    • (2009) Free Radic Res , vol.43 , pp. 943-950
    • Abbouni, B.1    Oehlmann, W.2    Stolle, P.3    Pierik, A.J.4    Auling, G.5
  • 2
    • 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., and Imlay, J.A. (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 thiol-disulfide status
    • Aslund, F., Zheng, M., Beckwith, J., and Storz, G. (1999) Regulation of the OxyR transcriptional factor by hydrogen peroxide and the cellular thiol-disulfide status. Proc Natl Acad Sci USA 96: 6161-6165.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 6161-6165
    • Aslund, F.1    Zheng, M.2    Beckwith, J.3    Storz, G.4
  • 4
    • 0026649435 scopus 로고
    • Substitution of manganese for iron in ribonucleotide reductase from Escherichia coli. Spectroscopic and crystallographic characterization
    • Atta, M., Nordlund, P., Aberg, A., Eklund, H., and Fontecave, M. (1992) Substitution of manganese for iron in ribonucleotide reductase from Escherichia coli. Spectroscopic and crystallographic characterization. J Biol Chem 267: 20682-20688.
    • (1992) J Biol Chem , vol.267 , pp. 20682-20688
    • Atta, M.1    Nordlund, P.2    Aberg, A.3    Eklund, H.4    Fontecave, M.5
  • 5
    • 77956653207 scopus 로고    scopus 로고
    • Structural basis for activation of class Ib ribonucleotide reductase
    • Boal, A.K., Cotruvo, J.A., Jr, Stubbe, J., and Rosenzweig, A.C. (2010) Structural basis for activation of class Ib ribonucleotide reductase. Science 329: 1526-1530.
    • (2010) Science , vol.329 , pp. 1526-1530
    • Boal, A.K.1    Cotruvo Jr, J.A.2    Stubbe, J.3    Rosenzweig, A.C.4
  • 6
    • 0014411536 scopus 로고
    • Nonheme iron as a cofactor in ribonucleotide reductase from Escherichia coli
    • Brown, N.C., Eliasson, R., Reichard, P., and Thelander, L. (1968) Nonheme iron as a cofactor in ribonucleotide reductase from Escherichia coli. Biochem Biophys Res Commun 30: 522-527.
    • (1968) Biochem Biophys Res Commun , vol.30 , pp. 522-527
    • Brown, N.C.1    Eliasson, R.2    Reichard, P.3    Thelander, L.4
  • 7
    • 55249112956 scopus 로고    scopus 로고
    • Fe(II) is the native cofactor for Escherichia coli methionine aminopeptidase
    • Chai, S.C., Wang, W.L., and Ye, Z.Q. (2008) Fe(II) is the native cofactor for Escherichia coli methionine aminopeptidase. J Biol Chem 283: 26879-26885.
    • (2008) J Biol Chem , vol.283 , pp. 26879-26885
    • Chai, S.C.1    Wang, W.L.2    Ye, Z.Q.3
  • 8
    • 0027410196 scopus 로고
    • Interaction of six global transcription regulators in expression of manganese superoxide dismutase in Escherichia coli K-12
    • Compan, I., and Touati, D. (1993) Interaction of six global transcription regulators in expression of manganese superoxide dismutase in Escherichia coli K-12. J Bacteriol 175: 1687-1696.
    • (1993) J Bacteriol , vol.175 , pp. 1687-1696
    • Compan, I.1    Touati, D.2
  • 9
    • 55749110597 scopus 로고    scopus 로고
    • NrdI, a flavodoxin involved in maintenance of the diferric-tyrosyl radical cofactor in Escherichia coli class Ib ribonucleotide reductase
    • Cotruvo, J.A., Jr, and Stubbe, J. (2008) NrdI, a flavodoxin involved in maintenance of the diferric-tyrosyl radical cofactor in Escherichia coli class Ib ribonucleotide reductase. Proc Natl Acad Sci USA 105: 14383-14388.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 14383-14388
    • Cotruvo Jr, J.A.1    Stubbe, J.2
  • 10
    • 76749163991 scopus 로고    scopus 로고
    • An active dimanganese(III)-tyrosyl radical cofactor in Escherichia coli class Ib ribonucleotide reductase
    • Cotruvo, J.A., Jr, and Stubbe, J. (2010) An active dimanganese(III)-tyrosyl radical cofactor in Escherichia coli class Ib ribonucleotide reductase. Biochemistry 49: 1297-1309.
    • (2010) Biochemistry , vol.49 , pp. 1297-1309
    • Cotruvo Jr, J.A.1    Stubbe, J.2
  • 11
    • 79952401377 scopus 로고    scopus 로고
    • Escherichia coli class Ib ribonucleotide reductase contains a dimanganese(III)-tyrosyl radical cofactor in vivo
    • doi:10.1021/bi101881d
    • Cotruvo, J.A., Jr, and Stubbe, J. (2011) Escherichia coli class Ib ribonucleotide reductase contains a dimanganese(III)-tyrosyl radical cofactor in vivo. Biochemistry doi:10.1021/bi101881d
    • (2011) Biochemistry
    • Cotruvo Jr, J.A.1    Stubbe, J.2
  • 12
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K.A., and Wanner, B.L. (2000) One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc Natl Acad Sci USA 97: 6640-6645.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 13
    • 0019119604 scopus 로고
    • DNA gyrase on the bacterial chromosome: possibility of two levels of action
    • Drlica, K., Engle, E.C., and Manes, S.H. (1980) DNA gyrase on the bacterial chromosome: possibility of two levels of action. Proc Natl Acad Sci USA 77: 6879-6883.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 6879-6883
    • Drlica, K.1    Engle, E.C.2    Manes, S.H.3
  • 14
    • 0015501033 scopus 로고
    • Electron spin resonance of the iron-containing protein B2 from ribonucleotide reductase
    • Ehrenberg, A., and Reichard, P. (1972) Electron spin resonance of the iron-containing protein B2 from ribonucleotide reductase. J Biol Chem 247: 3485-3488.
    • (1972) J Biol Chem , vol.247 , pp. 3485-3488
    • Ehrenberg, A.1    Reichard, P.2
  • 15
    • 0037094370 scopus 로고    scopus 로고
    • Construction of targeted single copy lac fusions using lambda Red and FLP-mediated site-specific recombination in bacteria
    • Ellermeier, C.D., Janakiraman, A., and Slauch, J.M. (2002) Construction of targeted single copy lac fusions using lambda Red and FLP-mediated site-specific recombination in bacteria. Gene 290: 153-161.
    • (2002) Gene , vol.290 , pp. 153-161
    • Ellermeier, C.D.1    Janakiraman, A.2    Slauch, J.M.3
  • 16
    • 0032549033 scopus 로고    scopus 로고
    • The manganese-containing ribonucleotide reductase of Corynebacterium ammoniagenes is a class Ib enzyme
    • Fieschi, F., Torrents, E., Toulokhonova, L., Jordan, A., Hellman, U., Barbe, J., etal. (1998) The manganese-containing ribonucleotide reductase of Corynebacterium ammoniagenes is a class Ib enzyme. J Biol Chem 273: 4329-4337.
    • (1998) J Biol Chem , vol.273 , pp. 4329-4337
    • Fieschi, F.1    Torrents, E.2    Toulokhonova, L.3    Jordan, A.4    Hellman, U.5    Barbe, J.6
  • 17
    • 0027491617 scopus 로고
    • The inactivation of Fe-S cluster containing hydro-lyases by superoxide
    • Flint, D.H., Tuminello, J.F., and Emptage, M.H. (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
  • 18
    • 0023645474 scopus 로고
    • The function of superoxide dismutase during the enzymatic formation of the free radical of ribonucleotide reductase
    • Fontecave, M., Graslund, A., and Reichard, P. (1987a) The function of superoxide dismutase during the enzymatic formation of the free radical of ribonucleotide reductase. J Biol Chem 262: 12332-12336.
    • (1987) J Biol Chem , vol.262 , pp. 12332-12336
    • Fontecave, M.1    Graslund, A.2    Reichard, P.3
  • 19
    • 0023645565 scopus 로고
    • NAD(P)H:flavin oxidoreductase of Escherichia coli. A ferric iron reductase participating in the generation of the free radical of ribonucleotide reductase
    • Fontecave, M., Eliasson, R., and Reichard, P. (1987b) NAD(P)H:flavin oxidoreductase of Escherichia coli. A ferric iron reductase participating in the generation of the free radical of ribonucleotide reductase. J Biol Chem 262: 12325-12331.
    • (1987) J Biol Chem , vol.262 , pp. 12325-12331
    • Fontecave, M.1    Eliasson, R.2    Reichard, P.3
  • 20
    • 0024360313 scopus 로고
    • Enzymatic regulation of the radical content of the small subunit of Escherichia coli ribonucleotide reductase involving reduction of its redox centers
    • Fontecave, M., Eliasson, R., and Reichard, P. (1989) Enzymatic regulation of the radical content of the small subunit of Escherichia coli ribonucleotide reductase involving reduction of its redox centers. J Biol Chem 264: 9164-9170.
    • (1989) J Biol Chem , vol.264 , pp. 9164-9170
    • Fontecave, M.1    Eliasson, R.2    Reichard, P.3
  • 22
    • 0343725830 scopus 로고    scopus 로고
    • The irreversible inactivation of ribonucleotide reductase from Escherichia coli by superoxide radicals
    • Gaudu, P., Niviere, V., Petillot, Y., Kauppi, B., and Fontecave, M. (1996) The irreversible inactivation of ribonucleotide reductase from Escherichia coli by superoxide radicals. FEBS Lett 387: 137-140.
    • (1996) FEBS Lett , vol.387 , pp. 137-140
    • Gaudu, P.1    Niviere, V.2    Petillot, Y.3    Kauppi, B.4    Fontecave, M.5
  • 24
    • 33745807629 scopus 로고    scopus 로고
    • In vivo requirement for glutaredoxins and thioredoxins in the reduction of the ribonucleotide reductases of Escherichia coli
    • Gon, S., Faulkner, M.J., and Beckwith, J. (2006) In vivo requirement for glutaredoxins and thioredoxins in the reduction of the ribonucleotide reductases of Escherichia coli. Antioxid Redox Signal 8: 735-742.
    • (2006) Antioxid Redox Signal , vol.8 , pp. 735-742
    • Gon, S.1    Faulkner, M.J.2    Beckwith, J.3
  • 25
    • 14244251491 scopus 로고    scopus 로고
    • The metal permease ZupT from Escherichia coli is a transporter with a broad substrate spectrum
    • Grass, G., Franke, S., Taudte, N., Nies, D.H., Kucharski, L.M., Maguire, M.E., and Rensing, C. (2005) The metal permease ZupT from Escherichia coli is a transporter with a broad substrate spectrum. J Bacteriol 187: 1604-1611.
    • (2005) J Bacteriol , vol.187 , pp. 1604-1611
    • Grass, G.1    Franke, S.2    Taudte, N.3    Nies, D.H.4    Kucharski, L.M.5    Maguire, M.E.6    Rensing, C.7
  • 26
    • 60849105356 scopus 로고    scopus 로고
    • Functional analysis of the Streptomyces coelicolor NrdR ATP-cone domain: role in nucleotide binding, oligomerization, and DNA interactions
    • Grinberg, I., Shteinberg, T., Hassan, A.Q., Aharonowitz, Y., Borovok, I., and Cohen, G. (2009) Functional analysis of the Streptomyces coelicolor NrdR ATP-cone domain: role in nucleotide binding, oligomerization, and DNA interactions. J Bacteriol 191: 1169-1179.
    • (2009) J Bacteriol , vol.191 , pp. 1169-1179
    • Grinberg, I.1    Shteinberg, T.2    Hassan, A.Q.3    Aharonowitz, Y.4    Borovok, I.5    Cohen, G.6
  • 27
    • 0035682064 scopus 로고    scopus 로고
    • Conditional-replication, integration, excision, and retrieval plasmid-host systems for gene structure-function studies of bacteria
    • Haldimann, A., and Wanner, B.L. (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
  • 29
    • 41449098456 scopus 로고    scopus 로고
    • Importance of the maintenance pathway in the regulation of the activity of Escherichia coli ribonucleotide reductase
    • Hristova, D., Wu, C.H., Jiang, W., Krebs, C., and Stubbe, J. (2008) Importance of the maintenance pathway in the regulation of the activity of Escherichia coli ribonucleotide reductase. Biochemistry 47: 3989-3999.
    • (2008) Biochemistry , vol.47 , pp. 3989-3999
    • Hristova, D.1    Wu, C.H.2    Jiang, W.3    Krebs, C.4    Stubbe, J.5
  • 30
    • 50649117912 scopus 로고    scopus 로고
    • Cellular defenses against superoxide and hydrogen peroxide
    • Imlay, J.A. (2008) Cellular defenses against superoxide and hydrogen peroxide. Annu Rev Biochem 77: 755-776.
    • (2008) Annu Rev Biochem , vol.77 , pp. 755-776
    • Imlay, J.A.1
  • 31
    • 0036304598 scopus 로고    scopus 로고
    • The structure of Escherichia coli cytosine deaminase
    • Ireton, G.C., McDermott, G., Black, M.E., and Stoddard, B.L. (2002) The structure of Escherichia coli cytosine deaminase. J Mol Biol 315: 687-697.
    • (2002) J Mol Biol , vol.315 , pp. 687-697
    • Ireton, G.C.1    McDermott, G.2    Black, M.E.3    Stoddard, B.L.4
  • 32
    • 16844364707 scopus 로고    scopus 로고
    • Structures of Escherichia coli peptide deformylase bound to formate: insight into the preference for Fe2+ over Zn2+ as the active site metal
    • Jain, R., Hao, B., Liu, R.P., and Chan, M.K. (2005) Structures of Escherichia coli peptide deformylase bound to formate: insight into the preference for Fe2+ over Zn2+ as the active site metal. J Am Chem Soc 127: 4558-4559.
    • (2005) J Am Chem Soc , vol.127 , pp. 4558-4559
    • Jain, R.1    Hao, B.2    Liu, R.P.3    Chan, M.K.4
  • 33
    • 33847753939 scopus 로고    scopus 로고
    • Micromolar intracellular hydrogen peroxide disrupts metabolism by damaging iron-sulfur enzymes
    • Jang, S., and Imlay, J.A. (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
  • 34
    • 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 Imlay, J.A. (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
  • 35
    • 0028342531 scopus 로고
    • Cloning and sequencing of the genes from Salmonella typhimurium encoding a new bacterial ribonucleotide reductase
    • Jordan, A., Gibert, I., and Barbe, J. (1994) Cloning and sequencing of the genes from Salmonella typhimurium encoding a new bacterial ribonucleotide reductase. J Bacteriol 176: 3420-3427.
    • (1994) J Bacteriol , vol.176 , pp. 3420-3427
    • Jordan, A.1    Gibert, I.2    Barbe, J.3
  • 36
    • 0030068006 scopus 로고    scopus 로고
    • Promoter identification and expression analysis of Salmonella typhimurium and Escherichia coli nrdEF operons encoding one of two class I ribonucleotide reductases present in both bacteria
    • Jordan, A., Aragall, E., Gibert, I., and Barbe, J. (1996) Promoter identification and expression analysis of Salmonella typhimurium and Escherichia coli nrdEF operons encoding one of two class I ribonucleotide reductases present in both bacteria. Mol Microbiol 19: 777-790.
    • (1996) Mol Microbiol , vol.19 , pp. 777-790
    • Jordan, A.1    Aragall, E.2    Gibert, I.3    Barbe, J.4
  • 37
    • 0030829520 scopus 로고    scopus 로고
    • Characterization of Escherichia coli NrdH. A glutaredoxin-like protein with a thioredoxin-like activity profile
    • Jordan, A., Aslund, F., Pontis, E., Reichard, P., and Holmgren, A. (1997) Characterization of Escherichia coli NrdH. A glutaredoxin-like protein with a thioredoxin-like activity profile. J Biol Chem 272: 18044-18050.
    • (1997) J Biol Chem , vol.272 , pp. 18044-18050
    • Jordan, A.1    Aslund, F.2    Pontis, E.3    Reichard, P.4    Holmgren, A.5
  • 38
    • 0036267337 scopus 로고    scopus 로고
    • Regulation of Salmonella enterica serovar Typhimurium mntH transcription by H(2)O(2), Fe(2+), and Mn(2+).
    • Kehres, D.G., Janakiraman, A., Slauch, J.M., and Maguire, M.E. (2002) Regulation of Salmonella enterica serovar Typhimurium mntH transcription by H(2)O(2), Fe(2+), and Mn(2+). J Bacteriol 184: 3151-3158.
    • (2002) J Bacteriol , vol.184 , pp. 3151-3158
    • Kehres, D.G.1    Janakiraman, A.2    Slauch, J.M.3    Maguire, M.E.4
  • 39
    • 0019015731 scopus 로고
    • Distinguishing between Mn-containing and Fe-containing superoxide dismutases in crude extracts of cells
    • Kirby, T., Blum, J., Kahane, I., and Fridovich, I. (1980) Distinguishing between Mn-containing and Fe-containing superoxide dismutases in crude extracts of cells. Arch Biochem Biophys 201: 551-555.
    • (1980) Arch Biochem Biophys , vol.201 , pp. 551-555
    • Kirby, T.1    Blum, J.2    Kahane, I.3    Fridovich, I.4
  • 40
    • 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, K.C., Yeo, W.S., and Roe, J.H. (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
  • 41
    • 0014691242 scopus 로고
    • Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)
    • McCord, J.M., and Fridovich, I. (1969) Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem 244: 6049-6055.
    • (1969) J Biol Chem , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 43
    • 27144539863 scopus 로고    scopus 로고
    • Resolvase-in vivo expression technology analysis of the Salmonella enterica serovar Typhimurium PhoP and PmrA regulons in BALB/c mice
    • Merighi, M., Ellermeier, C.D., Slauch, J.M., and Gunn, J.S. (2005) Resolvase-in vivo expression technology analysis of the Salmonella enterica serovar Typhimurium PhoP and PmrA regulons in BALB/c mice. J Bacteriol 187: 7407-7416.
    • (2005) J Bacteriol , vol.187 , pp. 7407-7416
    • Merighi, M.1    Ellermeier, C.D.2    Slauch, J.M.3    Gunn, J.S.4
  • 44
  • 45
    • 0035947685 scopus 로고    scopus 로고
    • Expression analysis of the nrdHIEF operon from Escherichia coli. Conditions that trigger the transcript level in vivo
    • Monje-Casas, F., Jurado, J., Prieto-Alamo, M.J., Holmgren, A., and Pueyo, C. (2001) Expression analysis of the nrdHIEF operon from Escherichia coli. Conditions that trigger the transcript level in vivo. J Biol Chem 276: 18031-18037.
    • (2001) J Biol Chem , vol.276 , pp. 18031-18037
    • Monje-Casas, F.1    Jurado, J.2    Prieto-Alamo, M.J.3    Holmgren, A.4    Pueyo, C.5
  • 47
    • 61349134073 scopus 로고    scopus 로고
    • Sequence-specific binding to a subset of IscR-regulated promoters does not require IscR Fe-S cluster ligation
    • Nesbit, A.D., Giel, J.L., Rose, J.C., and Kiley, P.J. (2009) Sequence-specific binding to a subset of IscR-regulated promoters does not require IscR Fe-S cluster ligation. J Mol Biol 387: 28-41.
    • (2009) J Mol Biol , vol.387 , pp. 28-41
    • Nesbit, A.D.1    Giel, J.L.2    Rose, J.C.3    Kiley, P.J.4
  • 48
    • 2442567822 scopus 로고    scopus 로고
    • A suf operon requirement for Fe-S cluster assembly during iron starvation in Escherichia coli
    • Outten, F.W., Djaman, O., and Storz, G. (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
  • 49
    • 77956202067 scopus 로고    scopus 로고
    • Ribonucleotide reductases of Salmonella typhimurium: transcriptional regulation and differential role in pathogenesis
    • Panosa, A., Roca, I., and Gibert, I. (2010) Ribonucleotide reductases of Salmonella typhimurium: transcriptional regulation and differential role in pathogenesis. PLoS ONE 5: e11328.
    • (2010) PLoS ONE , vol.5
    • Panosa, A.1    Roca, I.2    Gibert, I.3
  • 50
    • 21544465580 scopus 로고    scopus 로고
    • Substantial DNA damage from submicromolar intracellular hydrogen peroxide detected in Hpx- mutants of Escherichia coli
    • Park, S., You, X., and Imlay, J.A. (2005) Substantial DNA damage from submicromolar intracellular hydrogen peroxide detected in Hpx- mutants of Escherichia coli. Proc Natl Acad Sci USA 102: 9317-9322.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 9317-9322
    • Park, S.1    You, X.2    Imlay, J.A.3
  • 51
    • 0034902162 scopus 로고    scopus 로고
    • Dual repression by Fe(2+)-Fur and Mn(2+)-MntR of the mntH gene, encoding an NRAMP-like Mn(2+) transporter in Escherichia coli
    • Patzer, S.I., and Hantke, K. (2001) Dual repression by Fe(2+)-Fur and Mn(2+)-MntR of the mntH gene, encoding an NRAMP-like Mn(2+) transporter in Escherichia coli. J Bacteriol 183: 4806-4813.
    • (2001) J Bacteriol , vol.183 , pp. 4806-4813
    • Patzer, S.I.1    Hantke, K.2
  • 52
    • 0034595617 scopus 로고    scopus 로고
    • Lack of a role for iron in the Lyme disease pathogen
    • Posey, J.E., and Gherardini, F.C. (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
  • 53
    • 0036123210 scopus 로고    scopus 로고
    • Multiplex reverse transcription-polymerase chain reaction for determining transcriptional regulation of thioredoxin and glutaredoxin pathways
    • Pueyo, C., Jurado, J., Prieto-Alamo, M.J., Monje-Casas, F., and Lopez-Barea, J. (2002) Multiplex reverse transcription-polymerase chain reaction for determining transcriptional regulation of thioredoxin and glutaredoxin pathways. Methods Enzymol 347: 441-451.
    • (2002) Methods Enzymol , vol.347 , pp. 441-451
    • Pueyo, C.1    Jurado, J.2    Prieto-Alamo, M.J.3    Monje-Casas, F.4    Lopez-Barea, J.5
  • 54
    • 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, C.J., Giel, J.L., Patschkowski, T., Luther, C., Ruzicka, F.J., Beinert, H., and Kiley, P.J. (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 USA 98: 14895-14900.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 14895-14900
    • Schwartz, C.J.1    Giel, J.L.2    Patschkowski, T.3    Luther, C.4    Ruzicka, F.J.5    Beinert, H.6    Kiley, P.J.7
  • 55
    • 0035212036 scopus 로고    scopus 로고
    • Hydrogen peroxide fluxes and compartmentalization inside growing Escherichia coli
    • Seaver, L.C., and Imlay, J.A. (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
  • 56
    • 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
    • (in press).
    • Sobota, J.M., and Imlay, J.A. (2011) 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 USA (in press).
    • (2011) Proc Natl Acad Sci USA
    • Sobota, J.M.1    Imlay, J.A.2
  • 57
    • 0028327173 scopus 로고
    • Fur regulon in Gram-negative bacteria. Identification and characterization of new iron-regulated Escherichia coli genes by a Fur titration assay
    • Stojiljkovic, I., Baumler, A.J., and Hantke, K. (1994) Fur regulon in Gram-negative bacteria. Identification and characterization of new iron-regulated Escherichia coli genes by a Fur titration assay. J Mol Biol 236: 531-545.
    • (1994) J Mol Biol , vol.236 , pp. 531-545
    • Stojiljkovic, I.1    Baumler, A.J.2    Hantke, K.3
  • 58
    • 34447506556 scopus 로고    scopus 로고
    • NrdR controls differential expression of the Escherichia coli ribonucleotide reductase genes
    • Torrents, E., Grinberg, I., Gorovitz-Harris, B., Lundstrom, H., Borovok, I., Aharonowitz, Y., etal. (2007) NrdR controls differential expression of the Escherichia coli ribonucleotide reductase genes. J Bacteriol 189: 5012-5021.
    • (2007) J Bacteriol , vol.189 , pp. 5012-5021
    • Torrents, E.1    Grinberg, I.2    Gorovitz-Harris, B.3    Lundstrom, H.4    Borovok, I.5    Aharonowitz, Y.6
  • 59
    • 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, K.R.C., and Imlay, J.A. (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
  • 60
    • 0034532850 scopus 로고    scopus 로고
    • A method for direct cloning of Fur-regulated genes: identification of seven new Fur-regulated loci in Escherichia coli
    • Vassinova, N., and Kozyrev, D. (2000) A method for direct cloning of Fur-regulated genes: identification of seven new Fur-regulated loci in Escherichia coli. Microbiology 146 (Part 12): 3171-3182.
    • (2000) Microbiology , vol.146 , Issue.PART 12 , pp. 3171-3182
    • Vassinova, N.1    Kozyrev, D.2
  • 61
    • 35348849676 scopus 로고    scopus 로고
    • YfaE, a ferredoxin involved in diferric-tyrosyl radical maintenance in Escherichia coli ribonucleotide reductase
    • Wu, C.H., Jiang, W., Krebs, C., and Stubbe, J. (2007) YfaE, a ferredoxin involved in diferric-tyrosyl radical maintenance in Escherichia coli ribonucleotide reductase. Biochemistry 46: 11577-11588.
    • (2007) Biochemistry , vol.46 , pp. 11577-11588
    • Wu, C.H.1    Jiang, W.2    Krebs, C.3    Stubbe, J.4
  • 62
    • 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, W.S., Lee, J.H., Lee, K.C., and Roe, J.H. (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
  • 63
    • 0034932337 scopus 로고    scopus 로고
    • DNA microarray-mediated transcriptional profiling of the Escherichia coli response to hydrogen peroxide
    • Zheng, M., Wang, X., Templeton, L.J., Smulski, D.R., LaRossa, R.A., and Storz, G. (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    Wang, X.2    Templeton, L.J.3    Smulski, D.R.4    LaRossa, R.A.5    Storz, G.6


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