메뉴 건너뛰기




Volumn 155, Issue 1, 2009, Pages 295-304

Oxidative stress and disruption of labile iron generate specific auxotrophic requirements in Salmonella enterica

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; METHIONINE; PROTEIN CYAY; PROTEIN YGGX; SULFITE REDUCTASE; THIAMINE; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; COBALT; IRON; IRON SULFUR PROTEIN; OXIDOREDUCTASE;

EID: 61449135987     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.020727-0     Document Type: Article
Times cited : (27)

References (56)
  • 1
    • 8644265127 scopus 로고    scopus 로고
    • A locking mechanism preventing radical damage in the absence of substrate, as revealed by the x-ray structure of lysine 5,6-aminomutase
    • Berkovitch, F., Behshad, E., Tang, K. H., Enns, E. A., Frey, P. A. & Drennan, C. L. (2004). A locking mechanism preventing radical damage in the absence of substrate, as revealed by the x-ray structure of lysine 5,6-aminomutase. Proc Natl Acad Sci U S A 101, 15870-15875.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 15870-15875
    • Berkovitch, F.1    Behshad, E.2    Tang, K.H.3    Enns, E.A.4    Frey, P.A.5    Drennan, C.L.6
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72, 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 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, 623-630.
    • (1986) EMBO J , vol.5 , pp. 623-630
    • Carlioz, A.1    Touati, D.2
  • 6
    • 0021112605 scopus 로고
    • Mossbauer studies of Escherichia coli sulfite reductase complexes with carbon monoxide and cyanide. Exchange coupling and intrinsic properties of the [4Fe-4S] cluster
    • Christner, J. A., Janick, P. A., Siegel, L. M. & Munck, E. (1983). Mossbauer studies of Escherichia coli sulfite reductase complexes with carbon monoxide and cyanide. Exchange coupling and intrinsic properties of the [4Fe-4S] cluster. J Biol Chem 258, 11157-11164.
    • (1983) J Biol Chem , vol.258 , pp. 11157-11164
    • Christner, J.A.1    Janick, P.A.2    Siegel, L.M.3    Munck, E.4
  • 7
    • 0015881958 scopus 로고
    • Nitrite reductase-deficient mutants of Escherichia coli K12
    • Cole, J. A. & Ward, F. B. (1973). Nitrite reductase-deficient mutants of Escherichia coli K12. J Gen Microbiol 76, 21-29.
    • (1973) J Gen Microbiol , vol.76 , pp. 21-29
    • Cole, J.A.1    Ward, F.B.2
  • 8
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K. A. & Wanner, B. L. (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
  • 9
    • 34247197625 scopus 로고    scopus 로고
    • Distinct iron binding property of two putative iron donors for the iron-sulfur cluster assembly: IscA and the bacterial frataxin ortholog CyaY under physiological and oxidative stress conditions
    • Ding, H., Yang, J., Coleman, L. C. & Yeung, S. (2007). Distinct iron binding property of two putative iron donors for the iron-sulfur cluster assembly: IscA and the bacterial frataxin ortholog CyaY under physiological and oxidative stress conditions. J Biol Chem 282, 7997-8004.
    • (2007) J Biol Chem , vol.282 , pp. 7997-8004
    • Ding, H.1    Yang, J.2    Coleman, L.C.3    Yeung, S.4
  • 10
    • 33747103795 scopus 로고    scopus 로고
    • A connection between iron-sulfur cluster metabolism and the biosynthesis of 4-amino-5-hydroxymethyl-2-methylpyrimidine pyrophosphate in Salmonella enterica
    • Dougherty, M. J. & Downs, D. M. (2006). A connection between iron-sulfur cluster metabolism and the biosynthesis of 4-amino-5-hydroxymethyl-2-methylpyrimidine pyrophosphate in Salmonella enterica. Microbiology 152, 2345-2353.
    • (2006) Microbiology , vol.152 , pp. 2345-2353
    • Dougherty, M.J.1    Downs, D.M.2
  • 11
    • 10544244681 scopus 로고
    • Coincident repression of the reduction of 3′-phosphoadenosine 5′-phosphosulfate, sulfite, and thiosulfate in the cysteine pathway of Salmonella typhimurium
    • Dreyfuss, J. & Monty, K. J. (1963). Coincident repression of the reduction of 3′-phosphoadenosine 5′-phosphosulfate, sulfite, and thiosulfate in the cysteine pathway of Salmonella typhimurium. J Biol Chem 238, 3781-3783.
    • (1963) J Biol Chem , vol.238 , pp. 3781-3783
    • Dreyfuss, J.1    Monty, K.J.2
  • 12
    • 0029834919 scopus 로고    scopus 로고
    • Evidence that the CysG protein catalyzes the first reaction specific to B12 synthesis in Salmonella typhimurium, insertion of cobalt
    • Fazzio, T. G. & Roth, J. R. (1996). Evidence that the CysG protein catalyzes the first reaction specific to B12 synthesis in Salmonella typhimurium, insertion of cobalt. J Bacteriol 178, 6952-6959.
    • (1996) J Bacteriol , vol.178 , pp. 6952-6959
    • Fazzio, T.G.1    Roth, J.R.2
  • 13
    • 0027491617 scopus 로고
    • The inactivation of Fe-S cluster containing hydro-lyases by superoxide
    • Flint, D. H., Tuminello, J. F. & 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
  • 14
    • 29144509819 scopus 로고    scopus 로고
    • Nickel and cobalt resistance engineered in Escherichia coli by overexpression of serine acetyltransferase from the nickel hyperaccumulator plant Thlaspi goesingense
    • Freeman, J. L., Persans, M. W., Nieman, K. & Salt, D. E. (2005). Nickel and cobalt resistance engineered in Escherichia coli by overexpression of serine acetyltransferase from the nickel hyperaccumulator plant Thlaspi goesingense. Appl Environ Microbiol 71, 8627-8633.
    • (2005) Appl Environ Microbiol , vol.71 , pp. 8627-8633
    • Freeman, J.L.1    Persans, M.W.2    Nieman, K.3    Salt, D.E.4
  • 15
    • 1642451816 scopus 로고    scopus 로고
    • The gross structure of the respiratory complex I: A Lego system
    • Friedrich, T. & Bottcher, B. (2004). The gross structure of the respiratory complex I: a Lego system. Biochim Biophys Acta 1608, 1-9.
    • (2004) Biochim Biophys Acta , vol.1608 , pp. 1-9
    • Friedrich, T.1    Bottcher, B.2
  • 16
    • 0026045587 scopus 로고
    • Superoxide sensitivity of the Escherichia coli aconitase
    • Gardner, P. R. & Fridovich, I. (1991). Superoxide sensitivity of the Escherichia coli aconitase. J Biol Chem 266, 19328-19333.
    • (1991) J Biol Chem , vol.266 , pp. 19328-19333
    • Gardner, P.R.1    Fridovich, I.2
  • 17
    • 0026806913 scopus 로고
    • Inactivation-reactivation of aconitase in Escherichia coli. A sensitive measure of superoxide radical
    • Gardner, P. R. & Fridovich, I. (1992). Inactivation-reactivation of aconitase in Escherichia coli. A sensitive measure of superoxide radical. J Biol Chem 267, 8757-8763.
    • (1992) J Biol Chem , vol.267 , pp. 8757-8763
    • Gardner, P.R.1    Fridovich, I.2
  • 18
    • 0027415691 scopus 로고
    • Genetic structure and regulation of the cysG gene in Salmonella typhimurium
    • Goldman, B. S. & Roth, J. R. (1993). Genetic structure and regulation of the cysG gene in Salmonella typhimurium. J Bacteriol 175, 1457-1466.
    • (1993) J Bacteriol , vol.175 , pp. 1457-1466
    • Goldman, B.S.1    Roth, J.R.2
  • 19
    • 0034940979 scopus 로고    scopus 로고
    • Protection from superoxide damage associated with an increased level of the YggX protein in Salmonella enterica
    • Gralnick, J. & Downs, D. (2001). Protection from superoxide damage associated with an increased level of the YggX protein in Salmonella enterica. Proc Natl Acad Sci U S A 98, 8030-8035.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 8030-8035
    • Gralnick, J.1    Downs, D.2
  • 20
    • 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, J. A. & Downs, D. M. (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, 20708-20715.
    • (2003) J Biol Chem , vol.278 , pp. 20708-20715
    • Gralnick, J.A.1    Downs, D.M.2
  • 21
    • 0033821173 scopus 로고    scopus 로고
    • Lesions in gshA (encoding gamma-L-glutamyl-L-cysteine synthetase) prevent aerobic synthesis of thiamine in Salmonella enterica serovar typhimurium LT2
    • Gralnick, J., Webb, E., Beck, B. & Downs, D. (2000). Lesions in gshA (encoding gamma-L-glutamyl-L-cysteine synthetase) prevent aerobic synthesis of thiamine in Salmonella enterica serovar typhimurium LT2. J Bacteriol 182, 5180-5187.
    • (2000) J Bacteriol , vol.182 , pp. 5180-5187
    • Gralnick, J.1    Webb, E.2    Beck, B.3    Downs, D.4
  • 22
    • 48149108241 scopus 로고    scopus 로고
    • Glutathione and transition-metal homeostasis in Escherichia coli
    • Helbig, K., Bleuel, C., Krauss, G. J. & Nies, D. H. (2008). Glutathione and transition-metal homeostasis in Escherichia coli. J Bacteriol 190, 5431-5438.
    • (2008) J Bacteriol , vol.190 , pp. 5431-5438
    • Helbig, K.1    Bleuel, C.2    Krauss, G.J.3    Nies, D.H.4
  • 23
    • 23044477952 scopus 로고    scopus 로고
    • Organization of iron-sulfur clusters in respiratory complex I
    • Hinchliffe, P. & Sazanov, L. A. (2005). Organization of iron-sulfur clusters in respiratory complex I. Science 309, 771-774.
    • (2005) Science , vol.309 , pp. 771-774
    • Hinchliffe, P.1    Sazanov, L.A.2
  • 24
    • 33847753939 scopus 로고    scopus 로고
    • Micromolar intracellular hydrogen peroxide disrupts metabolism by damaging iron-sulfur enzymes
    • Jang, S. & 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
  • 26
    • 0030465238 scopus 로고    scopus 로고
    • Superoxide accelerates DNA damage by elevating free-iron levels
    • Keyer, K. & Imlay, J. A. (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
    • 34547107087 scopus 로고    scopus 로고
    • Thiazole synthase from Escherichia coli: An investigation of the substrates and purified proteins required for activity in vitro
    • Kriek, M., Martins, F., Leonardi, R., Fairhurst, S. A., Lowe, D. J. & Roach, P. L. (2007). Thiazole synthase from Escherichia coli: an investigation of the substrates and purified proteins required for activity in vitro. J Biol Chem 282, 17413-17423.
    • (2007) J Biol Chem , vol.282 , pp. 17413-17423
    • Kriek, M.1    Martins, F.2    Leonardi, R.3    Fairhurst, S.A.4    Lowe, D.J.5    Roach, P.L.6
  • 28
    • 0347504850 scopus 로고    scopus 로고
    • Crystal structure of coproporphyrinogen III oxidase reveals cofactor geometry of radical SAM enzymes
    • Layer, G., Moser, J., Heinz, D. W., Jahn, D. & Schubert, W. D. (2003). Crystal structure of coproporphyrinogen III oxidase reveals cofactor geometry of radical SAM enzymes. EMBO J 22, 6214-6224.
    • (2003) EMBO J , vol.22 , pp. 6214-6224
    • Layer, G.1    Moser, J.2    Heinz, D.W.3    Jahn, D.4    Schubert, W.D.5
  • 29
    • 2342435513 scopus 로고    scopus 로고
    • Thiamine biosynthesis in Escherichia coli: In vitro reconstitution of the thiazole synthase activity
    • Leonardi, R. & Roach, P. L. (2004). Thiamine biosynthesis in Escherichia coli: in vitro reconstitution of the thiazole synthase activity. J Biol Chem 279, 17054-17062.
    • (2004) J Biol Chem , vol.279 , pp. 17054-17062
    • Leonardi, R.1    Roach, P.L.2
  • 30
    • 33947467119 scopus 로고
    • Some metal complexes of sulfur-containing amino acids
    • Li, N. C. & Manning, R. A. (1955). Some metal complexes of sulfur-containing amino acids. J Am Chem Soc 77, 5225-5227.
    • (1955) J Am Chem Soc , vol.77 , pp. 5225-5227
    • Li, N.C.1    Manning, R.A.2
  • 32
    • 0035970292 scopus 로고    scopus 로고
    • The mitochondrial proteins Ssq1 and Jac1 are required for the assembly of iron sulfur clusters in mitochondria
    • Lutz, T., Westermann, B., Neupert, W. & Herrmann, J. M. (2001). The mitochondrial proteins Ssq1 and Jac1 are required for the assembly of iron sulfur clusters in mitochondria. J Mol Biol 307, 815-825.
    • (2001) J Mol Biol , vol.307 , pp. 815-825
    • Lutz, T.1    Westermann, B.2    Neupert, W.3    Herrmann, J.M.4
  • 33
    • 50849098497 scopus 로고    scopus 로고
    • ThiC is an [Fe-S] cluster protein that requires AdoMet to generate the 4-amino-5-hydroxymethyl-2-methylpyrimidine moiety in thiamin synthesis
    • Martinez-Gomez, N. C. & Downs, D. M. (2008). ThiC is an [Fe-S] cluster protein that requires AdoMet to generate the 4-amino-5-hydroxymethyl-2-methylpyrimidine moiety in thiamin synthesis. Biochemistry 47, 9054-9056.
    • (2008) Biochemistry , vol.47 , pp. 9054-9056
    • Martinez-Gomez, N.C.1    Downs, D.M.2
  • 34
    • 4644357750 scopus 로고    scopus 로고
    • Mutational analysis of ThiH, a member of the radical S-adenosyl-methionine (AdoMet) protein superfamily
    • Martinez-Gomez, N. C., Robers, M. & Downs, D. M. (2004). Mutational analysis of ThiH, a member of the radical S-adenosyl-methionine (AdoMet) protein superfamily. J Biol Chem 279, 40505-40510.
    • (2004) J Biol Chem , vol.279 , pp. 40505-40510
    • Martinez-Gomez, N.C.1    Robers, M.2    Downs, D.M.3
  • 35
    • 0037007078 scopus 로고    scopus 로고
    • A small RNA regulates the expression of genes involved in iron metabolism in Escherichia coli
    • Masse, E. & Gottesman, S. (2002). A small RNA regulates the expression of genes involved in iron metabolism in Escherichia coli. Proc Natl Acad Sci U S A 99, 4620-4625.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 4620-4625
    • Masse, E.1    Gottesman, S.2
  • 36
    • 7944225865 scopus 로고    scopus 로고
    • Solution structure of the bacterial frataxin ortholog, CyaY: Mapping the iron binding sites
    • Nair, M., Adinolfi, S., Pastore, C., Kelly, G., Temussi, P. & Pastore, A. (2004). Solution structure of the bacterial frataxin ortholog, CyaY: mapping the iron binding sites. Structure 12, 2037-2048.
    • (2004) Structure , vol.12 , pp. 2037-2048
    • Nair, M.1    Adinolfi, S.2    Pastore, C.3    Kelly, G.4    Temussi, P.5    Pastore, A.6
  • 37
    • 0015240660 scopus 로고
    • Complex formation of zinc and cadmium with glutathione
    • Perrin, D. D. & Watt, A. E. (1971). Complex formation of zinc and cadmium with glutathione. Biochim Biophys Acta 230, 96-104.
    • (1971) Biochim Biophys Acta , vol.230 , pp. 96-104
    • Perrin, D.D.1    Watt, A.E.2
  • 38
    • 0036249684 scopus 로고    scopus 로고
    • The chelatable iron pool in living cells: A methodically defined quantity
    • Petrat, F., de Groot, H., Sustmann, R. & Rauen, U. (2002). The chelatable iron pool in living cells: a methodically defined quantity. Biol Chem 383, 489-502.
    • (2002) Biol Chem , vol.383 , pp. 489-502
    • Petrat, F.1    de Groot, H.2    Sustmann, R.3    Rauen, U.4
  • 39
    • 0033989893 scopus 로고    scopus 로고
    • Identification of SoxS-regulated genes in Salmonella enterica serovar Typhimurium
    • Pomposiello, P. J. & Demple, B. (2000). Identification of SoxS-regulated genes in Salmonella enterica serovar Typhimurium. J Bacteriol 182, 23-29.
    • (2000) J Bacteriol , vol.182 , pp. 23-29
    • Pomposiello, P.J.1    Demple, B.2
  • 40
    • 0342700237 scopus 로고    scopus 로고
    • Recent advances in the molecular pathogenesis of Friedreich ataxia
    • Puccio, H. & Koenig, M. (2000). Recent advances in the molecular pathogenesis of Friedreich ataxia. Hum Mol Genet 9, 887-892.
    • (2000) Hum Mol Genet , vol.9 , pp. 887-892
    • Puccio, H.1    Koenig, M.2
  • 41
    • 0000904065 scopus 로고
    • A direct microdetermination for sulfide
    • Siegel, L. M. (1965). A direct microdetermination for sulfide. Anal Biochem 11, 126-132.
    • (1965) Anal Biochem , vol.11 , pp. 126-132
    • Siegel, L.M.1
  • 42
    • 0033942998 scopus 로고    scopus 로고
    • Metabolic defects caused by mutations in the isc gene cluster in Salmonella enterica serovar Typhimurium: Implications for thiamine synthesis
    • Skovran, E. & Downs, D. M. (2000). Metabolic defects caused by mutations in the isc gene cluster in Salmonella enterica serovar Typhimurium: implications for thiamine synthesis. J Bacteriol 182, 3896-3903.
    • (2000) J Bacteriol , vol.182 , pp. 3896-3903
    • Skovran, E.1    Downs, D.M.2
  • 43
    • 0037216551 scopus 로고    scopus 로고
    • Lack of the ApbC or ApbE protein results in a defect in Fe-S cluster metabolism in Salmonella enterica serovar Typhimurium
    • Skovran, E. & Downs, D. M. (2003). Lack of the ApbC or ApbE protein results in a defect in Fe-S cluster metabolism in Salmonella enterica serovar Typhimurium. J Bacteriol 185, 98-106.
    • (2003) J Bacteriol , vol.185 , pp. 98-106
    • Skovran, E.1    Downs, D.M.2
  • 44
    • 7744232644 scopus 로고    scopus 로고
    • Lack of YggX results in chronic oxidative stress and uncovers subtle defects in Fe-S cluster metabolism in Salmonella enterica
    • Skovran, E., Lauhon, C. T. & Downs, D. M. (2004). Lack of YggX results in chronic oxidative stress and uncovers subtle defects in Fe-S cluster metabolism in Salmonella enterica. J Bacteriol 186, 7626-7634.
    • (2004) J Bacteriol , vol.186 , pp. 7626-7634
    • Skovran, E.1    Lauhon, C.T.2    Downs, D.M.3
  • 46
    • 0027497266 scopus 로고
    • The Escherichia coli cysG gene encodes the multifunctional protein, siroheme synthase
    • Spencer, J. B., Stolowich, N. J., Roessner, C. A. & Scott, A. I. (1993). The Escherichia coli cysG gene encodes the multifunctional protein, siroheme synthase. FEBS Lett 335, 57-60.
    • (1993) FEBS Lett , vol.335 , pp. 57-60
    • Spencer, J.B.1    Stolowich, N.J.2    Roessner, C.A.3    Scott, A.I.4
  • 47
    • 0034703101 scopus 로고    scopus 로고
    • Yeast lacking superoxide dismutase(s) show elevated levels of "free iron" as measured by whole cell electron paramagnetic resonance
    • Srinivasan, C., Liba, A., Imlay, J. A., Valentine, J. S. & Gralla, E. B. (2000). Yeast lacking superoxide dismutase(s) show elevated levels of "free iron" as measured by whole cell electron paramagnetic resonance. J Biol Chem 275, 29187-29192.
    • (2000) J Biol Chem , vol.275 , pp. 29187-29192
    • Srinivasan, C.1    Liba, A.2    Imlay, J.A.3    Valentine, J.S.4    Gralla, E.B.5
  • 48
    • 0344197088 scopus 로고    scopus 로고
    • CysG structure reveals tetrapyrrole-binding features and novel regulation of siroheme biosynthesis
    • Stroupe, M. E., Leech, H. K., Daniels, D. S., Warren, M. J. & Getzoff, E. D. (2003). CysG structure reveals tetrapyrrole-binding features and novel regulation of siroheme biosynthesis. Nat Struct Biol 10, 1064-1073.
    • (2003) Nat Struct Biol , vol.10 , pp. 1064-1073
    • Stroupe, M.E.1    Leech, H.K.2    Daniels, D.S.3    Warren, M.J.4    Getzoff, E.D.5
  • 49
    • 0015530573 scopus 로고
    • Iron-sulfide chelates of some sulfur-containing peptides as model complex of non-heme iron proteins
    • Sugiura, Y. & Tanaka, H. (1972). Iron-sulfide chelates of some sulfur-containing peptides as model complex of non-heme iron proteins. Biochem Biophys Res Commun 46, 335-340.
    • (1972) Biochem Biophys Res Commun , vol.46 , pp. 335-340
    • Sugiura, Y.1    Tanaka, H.2
  • 50
    • 35648957710 scopus 로고    scopus 로고
    • Cobalt targets multiple metabolic processes in Salmonella enterica
    • Thorgersen, M. P. & Downs, D. M. (2007). Cobalt targets multiple metabolic processes in Salmonella enterica. J Bacteriol 189, 7774-7781.
    • (2007) J Bacteriol , vol.189 , pp. 7774-7781
    • Thorgersen, M.P.1    Downs, D.M.2
  • 51
    • 57349100413 scopus 로고    scopus 로고
    • Analysis of yggX and gshA mutants provides insights on the labile iron pool in Salmonella enterica
    • Thorgersen, M. P. & Downs, D. (2008). Analysis of yggX and gshA mutants provides insights on the labile iron pool in Salmonella enterica. J Bacteriol 190, 7608-7613.
    • (2008) J Bacteriol , vol.190 , pp. 7608-7613
    • Thorgersen, M.P.1    Downs, D.2
  • 52
    • 31344438920 scopus 로고    scopus 로고
    • Salmonella enterica strains lacking the frataxin homolog CyaY show defects in Fe-S cluster metabolism in vivo
    • Vivas, E., Skovran, E. & Downs, D. M. (2006). Salmonella enterica strains lacking the frataxin homolog CyaY show defects in Fe-S cluster metabolism in vivo. J Bacteriol 188, 1175-1179.
    • (2006) J Bacteriol , vol.188 , pp. 1175-1179
    • Vivas, E.1    Skovran, E.2    Downs, D.M.3
  • 53
    • 0021681568 scopus 로고
    • New Tn10 derivatives for transposon mutagenesis and for construction of lacZ operon fusions by transposition
    • Way, J. C., Davis, M. A., Morisato, D., Roberts, D. E. & Kleckner, N. (1984). New Tn10 derivatives for transposon mutagenesis and for construction of lacZ operon fusions by transposition. Gene 32, 369-379.
    • (1984) Gene , vol.32 , pp. 369-379
    • Way, J.C.1    Davis, M.A.2    Morisato, D.3    Roberts, D.E.4    Kleckner, N.5
  • 55
    • 0037613459 scopus 로고    scopus 로고
    • Iron-sulfur cluster biosynthesis. Characterization of frataxin as an iron donor for assembly of [2Fe-2S] clusters in ISU-type proteins
    • Yoon, T. & Cowan, J. A. (2003). Iron-sulfur cluster biosynthesis. Characterization of frataxin as an iron donor for assembly of [2Fe-2S] clusters in ISU-type proteins. J Am Chem Soc 125, 6078-6084.
    • (2003) J Am Chem Soc , vol.125 , pp. 6078-6084
    • Yoon, T.1    Cowan, J.A.2
  • 56
    • 0027216609 scopus 로고
    • Escherichia coli mutants lacking NADH dehydrogenase I have a competitive disadvantage in stationary phase
    • Zambrano, M. M. & Kolter, R. (1993). Escherichia coli mutants lacking NADH dehydrogenase I have a competitive disadvantage in stationary phase. J Bacteriol 175, 5642-5647.
    • (1993) J Bacteriol , vol.175 , pp. 5642-5647
    • Zambrano, M.M.1    Kolter, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.