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Volumn 98, Issue 2, 2015, Pages 218-242

Bacillithiol has a role in Fe-S cluster biogenesis in Staphylococcus aureus

Author keywords

[No Author keywords available]

Indexed keywords

ACONITATE HYDRATASE; BACILLITHIOL; BACTERIAL ENZYME; BACTERIAL PROTEIN; GLUTAMATE SYNTHASE; INORGANIC COMPOUND; IRON; IRON SULFUR CLUSTER; ISOLEUCINE; LEUCINE; PROTEIN ILVD; PROTEIN LEUCD; PROTEIN SUFA; REACTIVE OXYGEN METABOLITE; THIOL DERIVATIVE; UNCLASSIFIED DRUG; APOPROTEIN; CYSTEINE; GLUCOSAMINE; IRON SULFUR PROTEIN; SULFUR;

EID: 84943454454     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/mmi.13115     Document Type: Article
Times cited : (39)

References (135)
  • 1
    • 46649115965 scopus 로고    scopus 로고
    • NfuA, a new factor required for maturing Fe/S proteins in Escherichia coli under oxidative stress and iron starvation conditions
    • Angelini, S., Gerez, C., Ollagnier de Choudens, S., Sanakis, Y., Fontecave, M., Barras, F., and Py, B. (2008) NfuA, a new factor required for maturing Fe/S proteins in Escherichia coli under oxidative stress and iron starvation conditions. J Biol Chem 283: 14084-14091.
    • (2008) J Biol Chem , vol.283 , pp. 14084-14091
    • Angelini, S.1    Gerez, C.2    Ollagnier de Choudens, S.3    Sanakis, Y.4    Fontecave, M.5    Barras, F.6    Py, B.7
  • 3
    • 40549132515 scopus 로고    scopus 로고
    • Generating a collection of insertion mutations in the Staphylococcus aureus genome using bursa aurealis
    • Bae, T., Glass, E.M., Schneewind, O., and Missiakas, D. (2008) Generating a collection of insertion mutations in the Staphylococcus aureus genome using bursa aurealis. Methods Mol Biol 416: 103-116.
    • (2008) Methods Mol Biol , vol.416 , pp. 103-116
    • Bae, T.1    Glass, E.M.2    Schneewind, O.3    Missiakas, D.4
  • 4
    • 41949108097 scopus 로고    scopus 로고
    • Chloroplast monothiol glutaredoxins as scaffold proteins for the assembly and delivery of [2Fe-2S] clusters
    • Bandyopadhyay, S., Gama, F., Molina-Navarro, M.M., Gualberto, J.M., Claxton, R., Naik, S.G., etal. (2008) Chloroplast monothiol glutaredoxins as scaffold proteins for the assembly and delivery of [2Fe-2S] clusters. EMBO J 27: 1122-1133.
    • (2008) EMBO J , vol.27 , pp. 1122-1133
    • Bandyopadhyay, S.1    Gama, F.2    Molina-Navarro, M.M.3    Gualberto, J.M.4    Claxton, R.5    Naik, S.G.6
  • 5
    • 46649083462 scopus 로고    scopus 로고
    • A proposed role for the Azotobacter vinelandii NfuA protein as an intermediate iron-sulfur cluster carrier
    • Bandyopadhyay, S., Naik, S.G., O'Carroll, I.P., Huynh, B.H., Dean, D.R., Johnson, M.K., and Santos Dos, P.C. (2008) A proposed role for the Azotobacter vinelandii NfuA protein as an intermediate iron-sulfur cluster carrier. J Biol Chem 283: 14092-14099.
    • (2008) J Biol Chem , vol.283 , pp. 14092-14099
    • Bandyopadhyay, S.1    Naik, S.G.2    O'Carroll, I.P.3    Huynh, B.H.4    Dean, D.R.5    Johnson, M.K.6    Santos Dos, P.C.7
  • 6
    • 0030868605 scopus 로고    scopus 로고
    • Iron-sulfur clusters: nature's modular, multipurpose structures
    • Beinert, H., Holm, R.H., and Münck, E. (1997) Iron-sulfur clusters: nature's modular, multipurpose structures. Science 277: 653-659.
    • (1997) Science , vol.277 , pp. 653-659
    • Beinert, H.1    Holm, R.H.2    Münck, E.3
  • 7
    • 84874596495 scopus 로고    scopus 로고
    • Genetic tools to enhance the study of gene function and regulation in Staphylococcus aureus
    • Bose, J.L., Fey, P.D., and Bayles, K.W. (2013) Genetic tools to enhance the study of gene function and regulation in Staphylococcus aureus. Appl Microbiol 79: 2218-2224.
    • (2013) Appl Microbiol , vol.79 , pp. 2218-2224
    • Bose, J.L.1    Fey, P.D.2    Bayles, K.W.3
  • 8
    • 48649097049 scopus 로고    scopus 로고
    • Bacterial ApbC can bind and effectively transfer iron-sulfur clusters
    • Boyd, J.M., Pierik, A.J., Netz, D.J.A., Lill, R., and Downs, D.M. (2008) Bacterial ApbC can bind and effectively transfer iron-sulfur clusters. Biochemistry 47: 8195-8202.
    • (2008) Biochemistry , vol.47 , pp. 8195-8202
    • Boyd, J.M.1    Pierik, A.J.2    Netz, D.J.A.3    Lill, R.4    Downs, D.M.5
  • 9
    • 58649101413 scopus 로고    scopus 로고
    • Bacterial ApbC protein has two biochemical activities that are required for in vivo function
    • Boyd, J.M., Sondelski, J.L., and Downs, D.M. (2009) Bacterial ApbC protein has two biochemical activities that are required for in vivo function. J Biol Chem 284: 110-118.
    • (2009) J Biol Chem , vol.284 , pp. 110-118
    • Boyd, J.M.1    Sondelski, J.L.2    Downs, D.M.3
  • 10
    • 34047266670 scopus 로고    scopus 로고
    • Global analysis of community-associated methicillin-resistant Staphylococcus aureus exoproteins reveals molecules produced in vitro and during infection
    • Burlak, C., Hammer, C.H., Robinson, M.-A., Whitney, A.R., McGavin, M.J., Kreiswirth, B.N., and DeLeo, F.R. (2007) Global analysis of community-associated methicillin-resistant Staphylococcus aureus exoproteins reveals molecules produced in vitro and during infection. Cell Microbiol 9: 1172-1190.
    • (2007) Cell Microbiol , vol.9 , pp. 1172-1190
    • Burlak, C.1    Hammer, C.H.2    Robinson, M.-A.3    Whitney, A.R.4    McGavin, M.J.5    Kreiswirth, B.N.6    DeLeo, F.R.7
  • 11
    • 0033767925 scopus 로고    scopus 로고
    • Roles of the glutathione- and thioredoxin-dependent reduction systems in the Escherichia coli and Saccharomyces cerevisiae responses to oxidative stress
    • Carmel-Harel, O., and Storz, G. (2000) Roles of the glutathione- and thioredoxin-dependent reduction systems in the Escherichia coli and Saccharomyces cerevisiae responses to oxidative stress. Annu Rev Microbiol 54: 439-461.
    • (2000) Annu Rev Microbiol , vol.54 , pp. 439-461
    • Carmel-Harel, O.1    Storz, G.2
  • 12
    • 84893791835 scopus 로고    scopus 로고
    • Methylglyoxal resistance in Bacillus subtilis: contributions of bacillithiol-dependent and independent pathways
    • Chandrangsu, P., Dusi, R., Hamilton, C.J., and Helmann, J.D. (2014) Methylglyoxal resistance in Bacillus subtilis: contributions of bacillithiol-dependent and independent pathways. Mol Microbiol 91: 706-715.
    • (2014) Mol Microbiol , vol.91 , pp. 706-715
    • Chandrangsu, P.1    Dusi, R.2    Hamilton, C.J.3    Helmann, J.D.4
  • 13
    • 68849123336 scopus 로고    scopus 로고
    • Comprehensive identification of essential Staphylococcus aureus genes using transposon-mediated differential hybridisation (TMDH)
    • Chaudhuri, R.R., Allen, A.G., Owen, P.J., Shalom, G., Stone, K., Harrison, M., etal. (2009) Comprehensive identification of essential Staphylococcus aureus genes using transposon-mediated differential hybridisation (TMDH). BMC Genomics 10: 291.
    • (2009) BMC Genomics , vol.10 , pp. 291
    • Chaudhuri, R.R.1    Allen, A.G.2    Owen, P.J.3    Shalom, G.4    Stone, K.5    Harrison, M.6
  • 14
    • 80052929972 scopus 로고    scopus 로고
    • S-bacillithiolation protects against hypochlorite stress in Bacillus subtilis as revealed by transcriptomics and redox proteomics
    • Chi, B.K., Gronau, K., Mäder, U., Hessling, B., Becher, D., and Antelmann, H. (2011) S-bacillithiolation protects against hypochlorite stress in Bacillus subtilis as revealed by transcriptomics and redox proteomics. Mol Cell Proteomics 10: M111.009506.
    • (2011) Mol Cell Proteomics , vol.10
    • Chi, B.K.1    Gronau, K.2    Mäder, U.3    Hessling, B.4    Becher, D.5    Antelmann, H.6
  • 15
    • 0033056490 scopus 로고    scopus 로고
    • Characterization of the major superoxide dismutase of Staphylococcus aureus and its role in starvation survival, stress resistance, and pathogenicity
    • Clements, M.O., Watson, S.P., and Foster, S.J. (1999) Characterization of the major superoxide dismutase of Staphylococcus aureus and its role in starvation survival, stress resistance, and pathogenicity. J Bacteriol 181: 3898-3903.
    • (1999) J Bacteriol , vol.181 , pp. 3898-3903
    • Clements, M.O.1    Watson, S.P.2    Foster, S.J.3
  • 16
    • 77949328686 scopus 로고    scopus 로고
    • Posttranslational stability of the heme biosynthetic enzyme ferrochelatase is dependent on iron availability and intact iron-sulfur cluster assembly machinery
    • Crooks, D.R., Ghosh, M.C., Haller, R.G., Tong, W.-H., and Rouault, T.A. (2010) Posttranslational stability of the heme biosynthetic enzyme ferrochelatase is dependent on iron availability and intact iron-sulfur cluster assembly machinery. Blood 115: 860-869.
    • (2010) Blood , vol.115 , pp. 860-869
    • Crooks, D.R.1    Ghosh, M.C.2    Haller, R.G.3    Tong, W.-H.4    Rouault, T.A.5
  • 17
    • 0033785449 scopus 로고    scopus 로고
    • Accumulation of ppGpp and ppGp in Staphylococcus aureus 8325-4 following nutrient starvation
    • Crosse, A.M., Greenway, D.L., and England, R.R. (2000) Accumulation of ppGpp and ppGp in Staphylococcus aureus 8325-4 following nutrient starvation. Lett Appl Microbiol 31: 332-337.
    • (2000) Lett Appl Microbiol , vol.31 , pp. 332-337
    • Crosse, A.M.1    Greenway, D.L.2    England, R.R.3
  • 18
    • 0032489438 scopus 로고    scopus 로고
    • Coenzyme A disulfide reductase, the primary low molecular weight disulfide reductase from Staphylococcus aureus. Purification and characterization of the native enzyme
    • delCardayré, S.B., Stock, K.P., Newton, G.L., Fahey, R.C., and Davies, J.E. (1998) Coenzyme A disulfide reductase, the primary low molecular weight disulfide reductase from Staphylococcus aureus. Purification and characterization of the native enzyme. J Biol Chem 273: 5744-5751.
    • (1998) J Biol Chem , vol.273 , pp. 5744-5751
    • delCardayré, S.B.1    Stock, K.P.2    Newton, G.L.3    Fahey, R.C.4    Davies, J.E.5
  • 19
    • 0036709597 scopus 로고    scopus 로고
    • Cellular glutathione and thiols metabolism
    • Dickinson, D.A., and Forman, H.J. (2002) Cellular glutathione and thiols metabolism. Biochem Pharmacol 64: 1019-1026.
    • (2002) Biochem Pharmacol , vol.64 , pp. 1019-1026
    • Dickinson, D.A.1    Forman, H.J.2
  • 20
    • 33644659999 scopus 로고    scopus 로고
    • Complete genome sequence of USA300, an epidemic clone of community-acquired meticillin-resistant Staphylococcus aureus
    • Diep, B.A., Gill, S.R., Chang, R.F., Phan, T.H., Chen, J.H., Davidson, M.G., etal. (2006) Complete genome sequence of USA300, an epidemic clone of community-acquired meticillin-resistant Staphylococcus aureus. Lancet 367: 731-739.
    • (2006) Lancet , vol.367 , pp. 731-739
    • Diep, B.A.1    Gill, S.R.2    Chang, R.F.3    Phan, T.H.4    Chen, J.H.5    Davidson, M.G.6
  • 21
    • 23644456197 scopus 로고    scopus 로고
    • Mobilization of the iron centre in IscA for the iron-sulphur cluster assembly in IscU
    • Ding, B., Smith, E.S., and Ding, H. (2005) Mobilization of the iron centre in IscA for the iron-sulphur cluster assembly in IscU. Biochem J 389: 797-802.
    • (2005) Biochem J , vol.389 , pp. 797-802
    • Ding, B.1    Smith, E.S.2    Ding, H.3
  • 22
    • 2142654882 scopus 로고    scopus 로고
    • Characterization of iron binding in IscA, an ancient iron-sulphur cluster assembly protein
    • Ding, H., and Clark, R.J. (2004) Characterization of iron binding in IscA, an ancient iron-sulphur cluster assembly protein. Biochem J 379: 433-440.
    • (2004) Biochem J , vol.379 , pp. 433-440
    • Ding, H.1    Clark, R.J.2
  • 23
    • 4444317589 scopus 로고    scopus 로고
    • IscA mediates iron delivery for assembly of iron-sulfur clusters in IscU under the limited accessible free iron conditions
    • Ding, H., Clark, R.J., and Ding, B. (2004) IscA mediates iron delivery for assembly of iron-sulfur clusters in IscU under the limited accessible free iron conditions. J Biol Chem 279: 37499-37504.
    • (2004) J Biol Chem , vol.279 , pp. 37499-37504
    • Ding, H.1    Clark, R.J.2    Ding, B.3
  • 24
    • 7244239273 scopus 로고    scopus 로고
    • Repair of oxidized iron-sulfur clusters in Escherichia coli
    • Djaman, O., Outten, F.W., and Imlay, J.A. (2004) Repair of oxidized iron-sulfur clusters in Escherichia coli. J Biol Chem 279: 44590-44599.
    • (2004) J Biol Chem , vol.279 , pp. 44590-44599
    • Djaman, O.1    Outten, F.W.2    Imlay, J.A.3
  • 25
    • 0016187424 scopus 로고
    • Evidence for the presence of glutamate synthase in extracts of carrot cell cultures
    • Dougall, D.K. (1974) Evidence for the presence of glutamate synthase in extracts of carrot cell cultures. Biochem Biophys Res Commun 58: 639-646.
    • (1974) Biochem Biophys Res Commun , vol.58 , pp. 639-646
    • Dougall, D.K.1
  • 26
    • 84875715041 scopus 로고    scopus 로고
    • Glutathione analogs in prokaryotes
    • Fahey, R.C. (2013) Glutathione analogs in prokaryotes. Biochim Biophys Acta 1830: 3182-3198.
    • (2013) Biochim Biophys Acta , vol.1830 , pp. 3182-3198
    • Fahey, R.C.1
  • 27
    • 33745614344 scopus 로고    scopus 로고
    • Structural insight into poplar glutaredoxin C1 with a bridging iron-sulfur cluster at the active site
    • Feng, Y., Zhong, N., Rouhier, N., Hase, T., Kusunoki, M., Jacquot, J.-P., etal. (2006) Structural insight into poplar glutaredoxin C1 with a bridging iron-sulfur cluster at the active site. Biochemistry 45: 7998-8008.
    • (2006) Biochemistry , vol.45 , pp. 7998-8008
    • Feng, Y.1    Zhong, N.2    Rouhier, N.3    Hase, T.4    Kusunoki, M.5    Jacquot, J.-P.6
  • 28
    • 84874638650 scopus 로고    scopus 로고
    • A genetic resource for rapid and comprehensive phenotype screening of nonessential Staphylococcus aureus genes
    • e00537-e00512
    • Fey, P.D., Endres, J.L., Yajjala, V.K., Widhelm, T.J., Boissy, R.J., Bose, J.L., and Bayles, K.W. (2013) A genetic resource for rapid and comprehensive phenotype screening of nonessential Staphylococcus aureus genes. mBio 4: e00537-12.
    • (2013) mBio , vol.4
    • Fey, P.D.1    Endres, J.L.2    Yajjala, V.K.3    Widhelm, T.J.4    Boissy, R.J.5    Bose, J.L.6    Bayles, K.W.7
  • 29
    • 28044450837 scopus 로고    scopus 로고
    • Characterization of Bacillus anthracis germinant receptors in vitro
    • Fisher, N., and Hanna, P. (2005) Characterization of Bacillus anthracis germinant receptors in vitro. J Bacteriol 187: 8055-8062.
    • (2005) J Bacteriol , vol.187 , pp. 8055-8062
    • Fisher, N.1    Hanna, P.2
  • 30
    • 0024287137 scopus 로고
    • Dihydroxy acid dehydratase from spinach contains a [2Fe-2S] cluster
    • Flint, D.H., and Emptage, M.H. (1988) Dihydroxy acid dehydratase from spinach contains a [2Fe-2S] cluster. J Biol Chem 263: 3558-3564.
    • (1988) J Biol Chem , vol.263 , pp. 3558-3564
    • Flint, D.H.1    Emptage, M.H.2
  • 31
    • 0027165156 scopus 로고
    • The role and properties of the iron-sulfur cluster in Escherichia coli dihydroxy-acid dehydratase
    • Flint, D.H., Emptage, M.H., Finnegan, M.G., Fu, W., and Johnson, M.K. (1993) The role and properties of the iron-sulfur cluster in Escherichia coli dihydroxy-acid dehydratase. J Biol Chem 268: 14732-14742.
    • (1993) J Biol Chem , vol.268 , pp. 14732-14742
    • Flint, D.H.1    Emptage, M.H.2    Finnegan, M.G.3    Fu, W.4    Johnson, M.K.5
  • 32
    • 0036271625 scopus 로고    scopus 로고
    • A genome-wide strategy for the identification of essential genes in Staphylococcus aureus
    • Forsyth, R.A., Haselbeck, R.J., Ohlsen, K.L., Yamamoto, R.T., Xu, H., Trawick, J.D., etal. (2002) A genome-wide strategy for the identification of essential genes in Staphylococcus aureus. Mol Microbiol 43: 1387-1400.
    • (2002) Mol Microbiol , vol.43 , pp. 1387-1400
    • Forsyth, R.A.1    Haselbeck, R.J.2    Ohlsen, K.L.3    Yamamoto, R.T.4    Xu, H.5    Trawick, J.D.6
  • 33
    • 77950868171 scopus 로고    scopus 로고
    • Biosynthesis and functions of bacillithiol, a major low-molecular-weight thiol in Bacilli
    • Gaballa, A., Newton, G.L., Antelmann, H., Parsonage, D., Upton, H., Rawat, M., etal. (2010) Biosynthesis and functions of bacillithiol, a major low-molecular-weight thiol in Bacilli. Proc Natl Acad Sci USA 107: 6482-6486.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 6482-6486
    • Gaballa, A.1    Newton, G.L.2    Antelmann, H.3    Parsonage, D.4    Upton, H.5    Rawat, M.6
  • 34
    • 84884750480 scopus 로고    scopus 로고
    • Regulation of Bacillus subtilis bacillithiol biosynthesis operons by Spx
    • Gaballa, A., Antelmann, H., Hamilton, C.J., and Helmann, J.D. (2013) Regulation of Bacillus subtilis bacillithiol biosynthesis operons by Spx. Microbiology 159: 2025-2035.
    • (2013) Microbiology , vol.159 , pp. 2025-2035
    • Gaballa, A.1    Antelmann, H.2    Hamilton, C.J.3    Helmann, J.D.4
  • 35
    • 84903572069 scopus 로고    scopus 로고
    • Redox regulation in Bacillus subtilis: the bacilliredoxins BrxA (YphP) and BrxB (YqiW) function in de-bacillithiolation of S-bacillithiolated OhrR and MetE
    • Gaballa, A., Chi, B.K., Roberts, A.A., Becher, D., Hamilton, C.J., Antelmann, H., and Helmann, J.D. (2014) Redox regulation in Bacillus subtilis: the bacilliredoxins BrxA (YphP) and BrxB (YqiW) function in de-bacillithiolation of S-bacillithiolated OhrR and MetE. Antiox Redox Signal 21: 357-367.
    • (2014) Antiox Redox Signal , vol.21 , pp. 357-367
    • Gaballa, A.1    Chi, B.K.2    Roberts, A.A.3    Becher, D.4    Hamilton, C.J.5    Antelmann, H.6    Helmann, J.D.7
  • 36
    • 77954680177 scopus 로고    scopus 로고
    • Two novel point mutations in clinical Staphylococcus aureus reduce linezolid susceptibility and switch on the stringent response to promote persistent infection
    • Gao, W., Chua, K., Davies, J.K., Newton, H.J., Seemann, T., Harrison, P.F., etal. (2010) Two novel point mutations in clinical Staphylococcus aureus reduce linezolid susceptibility and switch on the stringent response to promote persistent infection. PLoS Pathog 6: e1000944.
    • (2010) PLoS Pathog , vol.6
    • Gao, W.1    Chua, K.2    Davies, J.K.3    Newton, H.J.4    Seemann, T.5    Harrison, P.F.6
  • 37
    • 0027274755 scopus 로고
    • Effect of glutathione on aconitase in Escherichia coli
    • Gardner, P.R., and Fridovich, I. (1993) Effect of glutathione on aconitase in Escherichia coli. Arch Biochem Biophys 301: 98-102.
    • (1993) Arch Biochem Biophys , vol.301 , pp. 98-102
    • Gardner, P.R.1    Fridovich, I.2
  • 38
    • 77951235714 scopus 로고    scopus 로고
    • Role of the (p)ppGpp synthase RSH, a RelA/SpoT homolog, in stringent response and virulence of Staphylococcus aureus
    • Geiger, T., Goerke, C., Fritz, M., Schäfer, T., Ohlsen, K., Liebeke, M., etal. (2010) Role of the (p)ppGpp synthase RSH, a RelA/SpoT homolog, in stringent response and virulence of Staphylococcus aureus. Infect Immun 78: 1873-1883.
    • (2010) Infect Immun , vol.78 , pp. 1873-1883
    • Geiger, T.1    Goerke, C.2    Fritz, M.3    Schäfer, T.4    Ohlsen, K.5    Liebeke, M.6
  • 39
    • 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., and 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
  • 40
    • 0344498571 scopus 로고
    • The biosynthesis of leucine. 11. The enzymic isomerization of beta-hydroxy-beta-carboxyisocaproate
    • Gross, S.R., Burns, R.O., and Umbarger, H.E. (1963) The biosynthesis of leucine. 11. The enzymic isomerization of beta-hydroxy-beta-carboxyisocaproate. Biochemistry 2: 1046-1052.
    • (1963) Biochemistry , vol.2 , pp. 1046-1052
    • Gross, S.R.1    Burns, R.O.2    Umbarger, H.E.3
  • 41
    • 69949162828 scopus 로고    scopus 로고
    • Native Escherichia coli SufA, coexpressed with SufBCDSE, purifies as a [2Fe-2S] protein and acts as an Fe-S transporter to Fe-S target enzymes
    • Gupta, V., Sendra, M., Naik, S.G., Chahal, H.K., Huynh, B.H., Outten, F.W., etal. (2009) Native Escherichia coli SufA, coexpressed with SufBCDSE, purifies as a [2Fe-2S] protein and acts as an Fe-S transporter to Fe-S target enzymes. J Am Chem Soc 131: 6149-6153.
    • (2009) J Am Chem Soc , vol.131 , pp. 6149-6153
    • Gupta, V.1    Sendra, M.2    Naik, S.G.3    Chahal, H.K.4    Huynh, B.H.5    Outten, F.W.6
  • 42
    • 84904262383 scopus 로고    scopus 로고
    • Bacillus pumilus reveals a remarkably high resistance to hydrogen peroxide provoked oxidative stress
    • Handtke, S., Schroeter, R., Jürgen, B., Methling, K., Schlüter, R., Albrecht, D., etal. (2014) Bacillus pumilus reveals a remarkably high resistance to hydrogen peroxide provoked oxidative stress. PLoS ONE 9: e85625.
    • (2014) PLoS ONE , vol.9
    • Handtke, S.1    Schroeter, R.2    Jürgen, B.3    Methling, K.4    Schlüter, R.5    Albrecht, D.6
  • 43
    • 83555173402 scopus 로고    scopus 로고
    • Glutathione: a key component of the cytoplasmic labile iron pool
    • Hider, R.C., and Kong, X.L. (2011) Glutathione: a key component of the cytoplasmic labile iron pool. Biometals 24: 1179-1187.
    • (2011) Biometals , vol.24 , pp. 1179-1187
    • Hider, R.C.1    Kong, X.L.2
  • 44
    • 0035150765 scopus 로고    scopus 로고
    • In Staphylococcus aureus, fur is an interactive regulator with PerR, contributes to virulence, and is necessary for oxidative stress resistance through positive regulation of catalase and iron homeostasis
    • Horsburgh, M.J., Ingham, E., and Foster, S.J. (2001) In Staphylococcus aureus, fur is an interactive regulator with PerR, contributes to virulence, and is necessary for oxidative stress resistance through positive regulation of catalase and iron homeostasis. J Bacteriol 183: 468-475.
    • (2001) J Bacteriol , vol.183 , pp. 468-475
    • Horsburgh, M.J.1    Ingham, E.2    Foster, S.J.3
  • 45
    • 0035013928 scopus 로고    scopus 로고
    • PerR controls oxidative stress resistance and iron storage proteins and is required for virulence in Staphylococcus aureus
    • Horsburgh, M.J., Clements, M.O., Crossley, H., Ingham, E., and Foster, S.J. (2001) PerR controls oxidative stress resistance and iron storage proteins and is required for virulence in Staphylococcus aureus. Infect Immun 69: 3744-3754.
    • (2001) Infect Immun , vol.69 , pp. 3744-3754
    • Horsburgh, M.J.1    Clements, M.O.2    Crossley, H.3    Ingham, E.4    Foster, S.J.5
  • 46
    • 0036015643 scopus 로고    scopus 로고
    • MntR modulates expression of the PerR regulon and superoxide resistance in Staphylococcus aureus through control of manganese uptake
    • Horsburgh, M.J., Wharton, S.J., Cox, A.G., Ingham, E., Peacock, S., and Foster, S.J. (2002) MntR modulates expression of the PerR regulon and superoxide resistance in Staphylococcus aureus through control of manganese uptake. Mol Microbiol 44: 1269-1286.
    • (2002) Mol Microbiol , vol.44 , pp. 1269-1286
    • Horsburgh, M.J.1    Wharton, S.J.2    Cox, A.G.3    Ingham, E.4    Peacock, S.5    Foster, S.J.6
  • 47
    • 0026322329 scopus 로고
    • Hypochlorous acid and myeloperoxidase-catalyzed oxidation of iron-sulfur clusters in bacterial respiratory dehydrogenases
    • Hurst, J.K., Barrette, W.C. Jr, Michel, B.R., and Rosen, H. (1991) Hypochlorous acid and myeloperoxidase-catalyzed oxidation of iron-sulfur clusters in bacterial respiratory dehydrogenases. Eur J Biochem 202: 1275-1282.
    • (1991) Eur J Biochem , vol.202 , pp. 1275-1282
    • Hurst, J.K.1    Barrette, W.C.2    Michel, B.R.3    Rosen, H.4
  • 48
    • 33645065589 scopus 로고    scopus 로고
    • Iron-sulphur clusters and the problem with oxygen
    • Imlay, J.A. (2006) Iron-sulphur clusters and the problem with oxygen. Mol Microbiol 59: 1073-1082.
    • (2006) Mol Microbiol , vol.59 , pp. 1073-1082
    • Imlay, J.A.1
  • 49
    • 0023886170 scopus 로고
    • DNA damage and oxygen radical toxicity
    • Imlay, J.A., and Linn, S. (1988) DNA damage and oxygen radical toxicity. Science 240: 1302-1309.
    • (1988) Science , vol.240 , pp. 1302-1309
    • Imlay, J.A.1    Linn, S.2
  • 50
    • 67650077717 scopus 로고    scopus 로고
    • Structural basis for delivery of the intact [Fe2-S2] cluster by monothiol glutaredoxin
    • Iwema, T., Picciocchi, A., Traore, D.A.K., Ferrer, J.-L., Chauvat, F., and Jacquamet, L. (2009) Structural basis for delivery of the intact [Fe2-S2] cluster by monothiol glutaredoxin. Biochemistry 48: 6041-6043.
    • (2009) Biochemistry , vol.48 , pp. 6041-6043
    • Iwema, T.1    Picciocchi, A.2    Traore, D.A.K.3    Ferrer, J.-L.4    Chauvat, F.5    Jacquamet, L.6
  • 51
    • 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
  • 52
    • 20744446399 scopus 로고    scopus 로고
    • Structure, function, and formation of biological iron-sulfur clusters
    • Johnson, D.C., Dean, D.R., Smith, A.D., and Johnson, M.K. (2005) Structure, function, and formation of biological iron-sulfur clusters. Annu Rev Biochem 74: 247-281.
    • (2005) Annu Rev Biochem , vol.74 , pp. 247-281
    • Johnson, D.C.1    Dean, D.R.2    Smith, A.D.3    Johnson, M.K.4
  • 53
    • 84896293907 scopus 로고    scopus 로고
    • A universal cloning method based on yeast homologous recombination that is simple, efficient, and versatile
    • Joska, T.M., Mashruwala, A., Boyd, J.M., and Belden, W.J. (2014) A universal cloning method based on yeast homologous recombination that is simple, efficient, and versatile. J Microbiol Methods 100: 46-51.
    • (2014) J Microbiol Methods , vol.100 , pp. 46-51
    • Joska, T.M.1    Mashruwala, A.2    Boyd, J.M.3    Belden, W.J.4
  • 54
    • 2442629407 scopus 로고    scopus 로고
    • Staphylococcal NreB: an O(2)-sensing histidine protein kinase with an O(2)-labile iron-sulphur cluster of the FNR type
    • Kamps, A., Achebach, S., Fedtke, I., Unden, G., and Götz, F. (2004) Staphylococcal NreB: an O(2)-sensing histidine protein kinase with an O(2)-labile iron-sulphur cluster of the FNR type. Mol Microbiol 52: 713-723.
    • (2004) Mol Microbiol , vol.52 , pp. 713-723
    • Kamps, A.1    Achebach, S.2    Fedtke, I.3    Unden, G.4    Götz, F.5
  • 55
    • 0142074789 scopus 로고    scopus 로고
    • Role and regulation of the superoxide dismutases of Staphylococcus aureus
    • Karavolos, M.H., Horsburgh, M.J., Ingham, E., and Foster, S.J. (2003) Role and regulation of the superoxide dismutases of Staphylococcus aureus. Microbiology 149: 2749-2758.
    • (2003) Microbiology , vol.149 , pp. 2749-2758
    • Karavolos, M.H.1    Horsburgh, M.J.2    Ingham, E.3    Foster, S.J.4
  • 56
    • 0023952439 scopus 로고
    • 2- of aconitase during cluster interconversions and removal. A convenient preparation of apoenzyme
    • 2- of aconitase during cluster interconversions and removal. A convenient preparation of apoenzyme. J Biol Chem 263: 8194-8198.
    • (1988) J Biol Chem , vol.263 , pp. 8194-8198
    • Kennedy, M.C.1    Beinert, H.2
  • 57
    • 0021112587 scopus 로고
    • The role of iron in the activation-inactivation of aconitase
    • Kennedy, M.C., Emptage, M.H., Dreyer, J.-L., and Beinert, H. (1983) The role of iron in the activation-inactivation of aconitase. J Biol Chem 258: 11098-11105.
    • (1983) J Biol Chem , vol.258 , pp. 11098-11105
    • Kennedy, M.C.1    Emptage, M.H.2    Dreyer, J.-L.3    Beinert, H.4
  • 59
    • 0030465238 scopus 로고    scopus 로고
    • Superoxide accelerates DNA damage by elevating free-iron levels
    • Keyer, K., and Imlay, J.A. (1996) Superoxide accelerates DNA damage by elevating free-iron levels. Proc Natl Acad Sci USA 93: 13635-13640.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 13635-13640
    • Keyer, K.1    Imlay, J.A.2
  • 60
    • 0030783602 scopus 로고    scopus 로고
    • Inactivation of dehydratase [4Fe-4S] clusters and disruption of iron homeostasis upon cell exposure to peroxynitrite
    • Keyer, K., and Imlay, J.A. (1997) Inactivation of dehydratase [4Fe-4S] clusters and disruption of iron homeostasis upon cell exposure to peroxynitrite. J Biol Chem 272: 27652-27659.
    • (1997) J Biol Chem , vol.272 , pp. 27652-27659
    • Keyer, K.1    Imlay, J.A.2
  • 62
    • 37049001066 scopus 로고    scopus 로고
    • Hospitalizations and deaths caused by methicillin-resistant Staphylococcus aureus, United States, 1999-2005
    • Klein, E., Smith, D.L., and Laxminarayan, R. (2007) Hospitalizations and deaths caused by methicillin-resistant Staphylococcus aureus, United States, 1999-2005. Emerg Infect Dis 13: 1840-1846.
    • (2007) Emerg Infect Dis , vol.13 , pp. 1840-1846
    • Klein, E.1    Smith, D.L.2    Laxminarayan, R.3
  • 63
    • 0024198152 scopus 로고
    • Isopropylmalate dehydratase from yeast
    • Kohlhaw, G.B. (1988) Isopropylmalate dehydratase from yeast. Methods Enzymol 166: 423-429.
    • (1988) Methods Enzymol , vol.166 , pp. 423-429
    • Kohlhaw, G.B.1
  • 66
    • 84873673139 scopus 로고    scopus 로고
    • Iron binding activity is essential for the function of IscA in iron-sulphur cluster biogenesis
    • Landry, A.P., Cheng, Z., and Ding, H. (2013) Iron binding activity is essential for the function of IscA in iron-sulphur cluster biogenesis. Dalton Trans 42: 3100-3106.
    • (2013) Dalton Trans , vol.42 , pp. 3100-3106
    • Landry, A.P.1    Cheng, Z.2    Ding, H.3
  • 67
    • 33645037891 scopus 로고    scopus 로고
    • The PerR transcription factor senses H2O2 by metal-catalysed histidine oxidation
    • Lee, J.-W., and Helmann, J.D. (2006) The PerR transcription factor senses H2O2 by metal-catalysed histidine oxidation. Nature 440: 363-367.
    • (2006) Nature , vol.440 , pp. 363-367
    • Lee, J.-W.1    Helmann, J.D.2
  • 68
    • 77951882083 scopus 로고    scopus 로고
    • Structural and biochemical characterization of yeast monothiol glutaredoxin Grx6
    • Luo, M., Jiang, Y.-L., Ma, X.-X., Tang, Y.-J., He, Y.-X., Yu, J., etal. (2010) Structural and biochemical characterization of yeast monothiol glutaredoxin Grx6. J Mol Biol 398: 614-622.
    • (2010) J Mol Biol , vol.398 , pp. 614-622
    • Luo, M.1    Jiang, Y.-L.2    Ma, X.-X.3    Tang, Y.-J.4    He, Y.-X.5    Yu, J.6
  • 70
    • 0014106134 scopus 로고
    • Nutritional requirements of Staphylococcus aureus S-6'
    • Mah, R.A., Fung, D.Y.C., and Morse, S.A. (1967) Nutritional requirements of Staphylococcus aureus S-6'. Appl Microbiol 15: 866-870.
    • (1967) Appl Microbiol , vol.15 , pp. 866-870
    • Mah, R.A.1    Fung, D.Y.C.2    Morse, S.A.3
  • 72
    • 84867533021 scopus 로고    scopus 로고
    • Spectroscopic and functional characterization of iron-sulfur cluster-bound forms of Azotobacter vinelandii (Nif)IscA
    • Mapolelo, D.T., Zhang, B., Naik, S.G., Huynh, B.H., and Johnson, M.K. (2012) Spectroscopic and functional characterization of iron-sulfur cluster-bound forms of Azotobacter vinelandii (Nif)IscA. Biochemistry 51: 8071-8084.
    • (2012) Biochemistry , vol.51 , pp. 8071-8084
    • Mapolelo, D.T.1    Zhang, B.2    Naik, S.G.3    Huynh, B.H.4    Johnson, M.K.5
  • 73
    • 84873672762 scopus 로고    scopus 로고
    • Monothiol glutaredoxins and A-type proteins: partners in Fe-S cluster trafficking
    • Mapolelo, D.T., Zhang, B., Randeniya, S., Albetel, A.-N., Li, H., Couturier, J., etal. (2013) Monothiol glutaredoxins and A-type proteins: partners in Fe-S cluster trafficking. Dalton Trans 42: 3107-3115.
    • (2013) Dalton Trans , vol.42 , pp. 3107-3115
    • Mapolelo, D.T.1    Zhang, B.2    Randeniya, S.3    Albetel, A.-N.4    Li, H.5    Couturier, J.6
  • 74
    • 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., and 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
  • 75
    • 84924700922 scopus 로고    scopus 로고
    • Nfu facilitates the maturation of iron-sulfur proteins and participates in virulence in Staphylococcus aureus
    • Mashruwala, A.A., Pang, Y.Y., Rosario-Cruz, Z., Chahal, H.K., Benson, M.A., Mike, L.A., etal. (2015) Nfu facilitates the maturation of iron-sulfur proteins and participates in virulence in Staphylococcus aureus. Mol Microbiol 95: 383-409.
    • (2015) Mol Microbiol , vol.95 , pp. 383-409
    • Mashruwala, A.A.1    Pang, Y.Y.2    Rosario-Cruz, Z.3    Chahal, H.K.4    Benson, M.A.5    Mike, L.A.6
  • 76
    • 27644589698 scopus 로고    scopus 로고
    • ClpXP-dependent proteolysis of FNR upon loss of its O2-sensing [4Fe-4S] cluster
    • Mettert, E.L., and Kiley, P.J. (2005) ClpXP-dependent proteolysis of FNR upon loss of its O2-sensing [4Fe-4S] cluster. J Mol Biol 354: 220-232.
    • (2005) J Mol Biol , vol.354 , pp. 220-232
    • Mettert, E.L.1    Kiley, P.J.2
  • 77
    • 33845421546 scopus 로고    scopus 로고
    • Iron starvation triggers the stringent response and induces amino acid biosynthesis for bacillibactin production in Bacillus subtilis
    • Miethke, M., Westers, H., Blom, E.-J., Kuipers, O.P., and Marahiel, M.A. (2006) Iron starvation triggers the stringent response and induces amino acid biosynthesis for bacillibactin production in Bacillus subtilis. J Bacteriol 188: 8655-8657.
    • (2006) J Bacteriol , vol.188 , pp. 8655-8657
    • Miethke, M.1    Westers, H.2    Blom, E.-J.3    Kuipers, O.P.4    Marahiel, M.A.5
  • 78
    • 70449174079 scopus 로고
    • Hemoglobin catabolism I. Glutathione peroxidase, an erythrocyte enzyme which protects hemoglobin from oxidative breakdown
    • Mills, G.C. (1957) Hemoglobin catabolism I. Glutathione peroxidase, an erythrocyte enzyme which protects hemoglobin from oxidative breakdown. J Biol Chem 229: 189-197.
    • (1957) J Biol Chem , vol.229 , pp. 189-197
    • Mills, G.C.1
  • 79
    • 77957674907 scopus 로고    scopus 로고
    • Cytosolic monothiol glutaredoxins function in intracellular iron sensing and trafficking via their bound iron-sulfur cluster
    • Mühlenhoff, U., Molik, S., Godoy, J.R., Uzarska, M.A., Richter, N., Seubert, A., etal. (2010) Cytosolic monothiol glutaredoxins function in intracellular iron sensing and trafficking via their bound iron-sulfur cluster. Cell Metab 12: 376-385.
    • (2010) Cell Metab , vol.12 , pp. 376-385
    • Mühlenhoff, U.1    Molik, S.2    Godoy, J.R.3    Uzarska, M.A.4    Richter, N.5    Seubert, A.6
  • 80
    • 0037718255 scopus 로고    scopus 로고
    • Evaluation of the probes 2',7'-dichlorofluorescin diacetate, luminol, and lucigenin as indicators of reactive species formation
    • Myhre, O., Andersen, J.M., Aarnes, H., and Fonnum, F. (2003) Evaluation of the probes 2', 7'-dichlorofluorescin diacetate, luminol, and lucigenin as indicators of reactive species formation. Biochem Pharmacol 65: 1575-1582.
    • (2003) Biochem Pharmacol , vol.65 , pp. 1575-1582
    • Myhre, O.1    Andersen, J.M.2    Aarnes, H.3    Fonnum, F.4
  • 81
    • 0030758614 scopus 로고    scopus 로고
    • Comparative studies of enhanced iron-mediated production of hydroxyl radical by glutathione, cysteine, ascorbic acid, and selected catechols
    • Nappi, A.J., and Vass, E. (1997) Comparative studies of enhanced iron-mediated production of hydroxyl radical by glutathione, cysteine, ascorbic acid, and selected catechols. Biochim Biophys Acta 1336: 295-301.
    • (1997) Biochim Biophys Acta , vol.1336 , pp. 295-301
    • Nappi, A.J.1    Vass, E.2
  • 82
    • 84943453900 scopus 로고    scopus 로고
    • Active Bacterial Core surveillance (ABCs) report emerging infections program network methicillin-resistant
    • Staphylococcus aureus, 2011
    • NCIRS, C. (2011) Active Bacterial Core surveillance (ABCs) report emerging infections program network methicillin-resistant Staphylococcus aureus, 2011. 1-3. http://www.cdc.gov/abcs/reports-findings/survreports/mrsa11.pdf
    • (2011) , pp. 1-3
  • 84
    • 84859140103 scopus 로고    scopus 로고
    • Detoxification of toxins by bacillithiol in Staphylococcus aureus
    • Newton, G.L., Fahey, R.C., and Rawat, M. (2012) Detoxification of toxins by bacillithiol in Staphylococcus aureus. Microbiology 158: 1117-1126.
    • (2012) Microbiology , vol.158 , pp. 1117-1126
    • Newton, G.L.1    Fahey, R.C.2    Rawat, M.3
  • 85
    • 35348850722 scopus 로고    scopus 로고
    • National trends in Staphylococcus aureus infection rates: impact on economic burden and mortality over a 6-year period (1998-2003)
    • Noskin, G.A., Rubin, R.J., Schentag, J.J., Kluytmans, J., Hedblom, E.C., Jacobson, C., etal. (2007) National trends in Staphylococcus aureus infection rates: impact on economic burden and mortality over a 6-year period (1998-2003). Clin Infect Dis 45: 1132-1140.
    • (2007) Clin Infect Dis , vol.45 , pp. 1132-1140
    • Noskin, G.A.1    Rubin, R.J.2    Schentag, J.J.3    Kluytmans, J.4    Hedblom, E.C.5    Jacobson, C.6
  • 86
    • 0025837196 scopus 로고
    • Genetic systems in Staphylococci
    • Novick, R.P. (1991) Genetic systems in Staphylococci. Methods Enzymol 204: 587-636.
    • (1991) Methods Enzymol , vol.204 , pp. 587-636
    • Novick, R.P.1
  • 87
    • 84928586175 scopus 로고    scopus 로고
    • Assays for determination of protein concentration
    • Unit34
    • Olson, B.J., and Markwell, J. (2007) Assays for determination of protein concentration. Curr Protoc Protein Sci 3: Unit3.4.
    • (2007) Curr Protoc Protein Sci , vol.3
    • Olson, B.J.1    Markwell, J.2
  • 88
    • 0014295806 scopus 로고
    • On the sulfur components of iron-sulfur proteins. I. The number of acid-labile sulfur groups sharing an unpaired electron with iron
    • Orme-Johnson, W.H., Hansen, R.E., Beinert, H., Tsibris, J.C.M., Bartholomaus, R.C., and Gunsalus, I.C. (1968) On the sulfur components of iron-sulfur proteins. I. The number of acid-labile sulfur groups sharing an unpaired electron with iron. Proc Natl Acad Sci USA 60: 368-372.
    • (1968) Proc Natl Acad Sci USA , vol.60 , pp. 368-372
    • Orme-Johnson, W.H.1    Hansen, R.E.2    Beinert, H.3    Tsibris, J.C.M.4    Bartholomaus, R.C.5    Gunsalus, I.C.6
  • 89
    • 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
  • 90
    • 84862846170 scopus 로고    scopus 로고
    • A region at the C-terminus of the Escherichia coli global transcription factor FNR negatively mediates its degradation by the ClpXP protease
    • Pan, Q., Shan, Y., and Yan, A. (2012) A region at the C-terminus of the Escherichia coli global transcription factor FNR negatively mediates its degradation by the ClpXP protease. Biochemistry 51: 5061-5071.
    • (2012) Biochemistry , vol.51 , pp. 5061-5071
    • Pan, Q.1    Shan, Y.2    Yan, A.3
  • 91
    • 77956356704 scopus 로고    scopus 로고
    • agr-Dependent interactions of Staphylococcus aureus USA300 with human polymorphonuclear neutrophils
    • Pang, Y.Y., Schwartz, J., Thoendel, M., Ackermann, L.W., Horswill, A.R., and Nauseef, W.M. (2010) agr-Dependent interactions of Staphylococcus aureus USA300 with human polymorphonuclear neutrophils. J Innate Immun 2: 546-559.
    • (2010) J Innate Immun , vol.2 , pp. 546-559
    • Pang, Y.Y.1    Schwartz, J.2    Thoendel, M.3    Ackermann, L.W.4    Horswill, A.R.5    Nauseef, W.M.6
  • 92
    • 77957061103 scopus 로고    scopus 로고
    • Characterization of the N-acetyl-α-D-glucosaminyl l-malate synthase and deacetylase functions for bacillithiol biosynthesis in Bacillus anthracis
    • Parsonage, D., Newton, G.L., Holder, R.C., Wallace, B.D., Paige, C., Hamilton, C.J., etal. (2010) Characterization of the N-acetyl-α-D-glucosaminyl l-malate synthase and deacetylase functions for bacillithiol biosynthesis in Bacillus anthracis. Biochemistry 49: 8398-8414.
    • (2010) Biochemistry , vol.49 , pp. 8398-8414
    • Parsonage, D.1    Newton, G.L.2    Holder, R.C.3    Wallace, B.D.4    Paige, C.5    Hamilton, C.J.6
  • 93
    • 0035283587 scopus 로고    scopus 로고
    • Redox-operated genetic switches: the SoxR and OxyR transcription factors
    • Pomposiello, P.J., and Demple, B. (2001) Redox-operated genetic switches: the SoxR and OxyR transcription factors. Trends Biotechnol 19: 109-114.
    • (2001) Trends Biotechnol , vol.19 , pp. 109-114
    • Pomposiello, P.J.1    Demple, B.2
  • 94
    • 84890842489 scopus 로고    scopus 로고
    • The importance of bacillithiol in the oxidative stress response of Staphylococcus aureus
    • Posada, A.C., Kolar, S.L., Dusi, R.G., Francois, P., Roberts, A.A., Hamilton, C.J., etal. (2014) The importance of bacillithiol in the oxidative stress response of Staphylococcus aureus. Infect Immun 82: 316-332.
    • (2014) Infect Immun , vol.82 , pp. 316-332
    • Posada, A.C.1    Kolar, S.L.2    Dusi, R.G.3    Francois, P.4    Roberts, A.A.5    Hamilton, C.J.6
  • 96
    • 0030941829 scopus 로고    scopus 로고
    • The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm
    • Prinz, W.A.W., Aslund, F.F., Holmgren, A.A., and Beckwith, J.J. (1997) The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm. J Biol Chem 272: 15661-15667.
    • (1997) J Biol Chem , vol.272 , pp. 15661-15667
    • Prinz, W.A.W.1    Aslund, F.F.2    Holmgren, A.A.3    Beckwith, J.J.4
  • 97
    • 77952813340 scopus 로고    scopus 로고
    • Building Fe-S proteins: bacterial strategies
    • Py, B., and Barras, F. (2010) Building Fe-S proteins: bacterial strategies. Nat Rev Microbiol 8: 436-446.
    • (2010) Nat Rev Microbiol , vol.8 , pp. 436-446
    • Py, B.1    Barras, F.2
  • 99
    • 4744349398 scopus 로고    scopus 로고
    • Structure and regulation of the neutrophil respiratory burst oxidase: comparison with nonphagocyte oxidases
    • Quinn, M.T., and Gauss, K.A. (2004) Structure and regulation of the neutrophil respiratory burst oxidase: comparison with nonphagocyte oxidases. J Leukoc Biol 76: 760-781.
    • (2004) J Leukoc Biol , vol.76 , pp. 760-781
    • Quinn, M.T.1    Gauss, K.A.2
  • 102
    • 49249087227 scopus 로고    scopus 로고
    • Staphylococcus aureus haem oxygenases are differentially regulated by iron and haem
    • Reniere, M.L., and Skaar, E.P. (2008) Staphylococcus aureus haem oxygenases are differentially regulated by iron and haem. Mol Microbiol 69: 1304-1315.
    • (2008) Mol Microbiol , vol.69 , pp. 1304-1315
    • Reniere, M.L.1    Skaar, E.P.2
  • 103
    • 84875125084 scopus 로고    scopus 로고
    • Mechanistic studies of FosB: a divalent-metal-dependent bacillithiol-S-transferase that mediates fosfomycin resistance in Staphylococcus aureus
    • Roberts, A.A., Sharma, S.V., Strankman, A., Duran, S.R., Rawat, M., and Hamilton, C.J. (2013) Mechanistic studies of FosB: a divalent-metal-dependent bacillithiol-S-transferase that mediates fosfomycin resistance in Staphylococcus aureus. Biochem J 451: 69-79.
    • (2013) Biochem J , vol.451 , pp. 69-79
    • Roberts, A.A.1    Sharma, S.V.2    Strankman, A.3    Duran, S.R.4    Rawat, M.5    Hamilton, C.J.6
  • 104
    • 0036226063 scopus 로고    scopus 로고
    • Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes
    • Rodríguez-Manzaneque, M.T., Tamarit, J., Bellí, G., Ros, J., and Herrero, E. (2002) Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes. Mol Bio Cell 13: 1109-1121.
    • (2002) Mol Bio Cell , vol.13 , pp. 1109-1121
    • Rodríguez-Manzaneque, M.T.1    Tamarit, J.2    Bellí, G.3    Ros, J.4    Herrero, E.5
  • 105
    • 84855928763 scopus 로고    scopus 로고
    • Lag phase is a distinct growth phase that prepares bacteria for exponential growth and involves transient metal accumulation
    • Rolfe, M.D., Rice, C.J., Lucchini, S., Pin, C., Thompson, A., Cameron, A.D.S., etal. (2012) Lag phase is a distinct growth phase that prepares bacteria for exponential growth and involves transient metal accumulation. J Bacteriol 194: 686-701.
    • (2012) J Bacteriol , vol.194 , pp. 686-701
    • Rolfe, M.D.1    Rice, C.J.2    Lucchini, S.3    Pin, C.4    Thompson, A.5    Cameron, A.D.S.6
  • 106
    • 33748428875 scopus 로고    scopus 로고
    • The DNA repair helicases XPD and FancJ have essential iron-sulfur domains
    • Rudolf, J., Makrantoni, V., Ingledew, W.J., Stark, M.J.R., and White, M.F. (2006) The DNA repair helicases XPD and FancJ have essential iron-sulfur domains. Mol Cell 23: 801-808.
    • (2006) Mol Cell , vol.23 , pp. 801-808
    • Rudolf, J.1    Makrantoni, V.2    Ingledew, W.J.3    Stark, M.J.R.4    White, M.F.5
  • 107
    • 34147189950 scopus 로고    scopus 로고
    • Controlled expression of nif and isc iron-sulfur protein maturation components reveals target specificity and limited functional replacement between the two systems
    • Santos Dos, P.C., Johnson, D.C., Ragle, B.E., Unciuleac, M.C., and Dean, D.R. (2007) Controlled expression of nif and isc iron-sulfur protein maturation components reveals target specificity and limited functional replacement between the two systems. J Bacteriol 189: 2854-2862.
    • (2007) J Bacteriol , vol.189 , pp. 2854-2862
    • Santos Dos, P.C.1    Johnson, D.C.2    Ragle, B.E.3    Unciuleac, M.C.4    Dean, D.R.5
  • 108
    • 0035371184 scopus 로고    scopus 로고
    • Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple
    • Schafer, F.Q., and Buettner, G.R. (2001) Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple. Free Radic Biol Med 30: 1191-1212.
    • (2001) Free Radic Biol Med , vol.30 , pp. 1191-1212
    • Schafer, F.Q.1    Buettner, G.R.2
  • 109
    • 77957657538 scopus 로고    scopus 로고
    • Kinetic analysis of the bisubstrate cysteine desulfurase SufS from Bacillus subtilis
    • Selbach, B., Earles, E., and Santos Dos, P.C. (2010) Kinetic analysis of the bisubstrate cysteine desulfurase SufS from Bacillus subtilis. Biochemistry 49: 8794-8802.
    • (2010) Biochemistry , vol.49 , pp. 8794-8802
    • Selbach, B.1    Earles, E.2    Santos Dos, P.C.3
  • 110
    • 84889569252 scopus 로고    scopus 로고
    • Biophysical features of bacillithiol, the glutathione surrogate of Bacillus subtilis and other firmicutes
    • Sharma, S.V., Arbach, M., Roberts, A.A., Macdonald, C.J., Groom, M., and Hamilton, C.J. (2013) Biophysical features of bacillithiol, the glutathione surrogate of Bacillus subtilis and other firmicutes. Chembiochem 14: 2160-2168.
    • (2013) Chembiochem , vol.14 , pp. 2160-2168
    • Sharma, S.V.1    Arbach, M.2    Roberts, A.A.3    Macdonald, C.J.4    Groom, M.5    Hamilton, C.J.6
  • 111
    • 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., and 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
  • 112
    • 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., and 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
  • 114
    • 84896800834 scopus 로고    scopus 로고
    • Crystal structures of nucleotide-free and glutathione-bound mitochondrial ABC transporter Atm1
    • Srinivasan, V., Pierik, A.J., and Lill, R. (2014) Crystal structures of nucleotide-free and glutathione-bound mitochondrial ABC transporter Atm1. Science 343: 1137-1140.
    • (2014) Science , vol.343 , pp. 1137-1140
    • Srinivasan, V.1    Pierik, A.J.2    Lill, R.3
  • 115
    • 84855667761 scopus 로고    scopus 로고
    • AirSR, a [2Fe-2S] cluster-containing two-component system, mediates global oxygen sensing and redox signaling in Staphylococcus aureus
    • Sun, F., Ji, Q., Jones, M.B., Deng, X., Liang, H., Frank, B., etal. (2012) AirSR, a [2Fe-2S] cluster-containing two-component system, mediates global oxygen sensing and redox signaling in Staphylococcus aureus. J Am Chem Soc 134: 305-314.
    • (2012) J Am Chem Soc , vol.134 , pp. 305-314
    • Sun, F.1    Ji, Q.2    Jones, M.B.3    Deng, X.4    Liang, H.5    Frank, B.6
  • 116
    • 0037047411 scopus 로고    scopus 로고
    • A third bacterial system for the assembly of iron-sulfur clusters with homologs in archaea and plastids
    • Takahashi, Y., and Tokumoto, U. (2002) A third bacterial system for the assembly of iron-sulfur clusters with homologs in archaea and plastids. J Biol Chem 277: 28380-28383.
    • (2002) J Biol Chem , vol.277 , pp. 28380-28383
    • Takahashi, Y.1    Tokumoto, U.2
  • 117
    • 79960671726 scopus 로고    scopus 로고
    • Reactive oxygen species mediate bactericidal killing elicited by carbon monoxide-releasing molecules
    • Tavares, A.F.N., Teixeira, M., Romão, C.C., Seixas, J.D., Nobre, L.S., and Saraiva, L.M. (2011) Reactive oxygen species mediate bactericidal killing elicited by carbon monoxide-releasing molecules. J Biol Chem 286: 26708-26717.
    • (2011) J Biol Chem , vol.286 , pp. 26708-26717
    • Tavares, A.F.N.1    Teixeira, M.2    Romão, C.C.3    Seixas, J.D.4    Nobre, L.S.5    Saraiva, L.M.6
  • 118
    • 57349100413 scopus 로고    scopus 로고
    • Analysis of yggX and gshA mutants provides insights into the labile iron pool in Salmonella enterica
    • Thorgersen, M.P., and Downs, D.M. (2008) Analysis of yggX and gshA mutants provides insights into 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.M.2
  • 119
    • 61449135987 scopus 로고    scopus 로고
    • Oxidative stress and disruption of labile iron generate specific auxotrophic requirements in Salmonella enterica
    • Thorgersen, M.P., and Downs, D.M. (2009) Oxidative stress and disruption of labile iron generate specific auxotrophic requirements in Salmonella enterica. Microbiology 155: 295-304.
    • (2009) Microbiology , vol.155 , pp. 295-304
    • Thorgersen, M.P.1    Downs, D.M.2
  • 120
    • 4644354002 scopus 로고    scopus 로고
    • Interchangeability and distinct properties of bacterial Fe-S cluster assembly systems: functional replacement of the isc and suf operons in Escherichia coli with the nifSU-like operon from Helicobacter pylori
    • Tokumoto, U., Kitamura, S., Fukuyama, K., and Takahashi, Y. (2004) Interchangeability and distinct properties of bacterial Fe-S cluster assembly systems: functional replacement of the isc and suf operons in Escherichia coli with the nifSU-like operon from Helicobacter pylori. J Biochem 136: 199-209.
    • (2004) J Biochem , vol.136 , pp. 199-209
    • Tokumoto, U.1    Kitamura, S.2    Fukuyama, K.3    Takahashi, Y.4
  • 121
    • 77950219265 scopus 로고    scopus 로고
    • Staphylococcus aureus Fur regulates the expression of virulence factors that contribute to the pathogenesis of pneumonia
    • Torres, V.J., Attia, A.S., Mason, W.J., Hood, M.I., Corbin, B.D., Beasley, F.C., etal. (2010) Staphylococcus aureus Fur regulates the expression of virulence factors that contribute to the pathogenesis of pneumonia. Infect Immun 78: 1618-1628.
    • (2010) Infect Immun , vol.78 , pp. 1618-1628
    • Torres, V.J.1    Attia, A.S.2    Mason, W.J.3    Hood, M.I.4    Corbin, B.D.5    Beasley, F.C.6
  • 122
    • 84859267227 scopus 로고    scopus 로고
    • Characterization of BshA, bacillithiol glycosyltransferase from Staphylococcus aureus and Bacillus subtilis
    • Upton, H., Newton, G.L., Gushiken, M., Lo, K., Holden, D., Fahey, R.C., and Rawat, M. (2012) Characterization of BshA, bacillithiol glycosyltransferase from Staphylococcus aureus and Bacillus subtilis. FEBS Lett 586: 1004-1008.
    • (2012) FEBS Lett , vol.586 , pp. 1004-1008
    • Upton, H.1    Newton, G.L.2    Gushiken, M.3    Lo, K.4    Holden, D.5    Fahey, R.C.6    Rawat, M.7
  • 123
    • 0032951727 scopus 로고    scopus 로고
    • Glutamate synthase: a complex iron-sulfur flavoprotein
    • Vanoni, M.A., and Curti, B. (1999) Glutamate synthase: a complex iron-sulfur flavoprotein. Cell Mol Life Sci 55: 617-638.
    • (1999) Cell Mol Life Sci , vol.55 , pp. 617-638
    • Vanoni, M.A.1    Curti, B.2
  • 124
    • 18444368425 scopus 로고    scopus 로고
    • Iron limitation induces SpoT-dependent accumulation of ppGpp in Escherichia coli
    • Vinella, D., Albrecht, C., Cashel, M., and D'Ari, R. (2005) Iron limitation induces SpoT-dependent accumulation of ppGpp in Escherichia coli. Mol Microbiol 56: 958-970.
    • (2005) Mol Microbiol , vol.56 , pp. 958-970
    • Vinella, D.1    Albrecht, C.2    Cashel, M.3    D'Ari, R.4
  • 125
    • 67149111967 scopus 로고    scopus 로고
    • Iron-sulfur (Fe/S) protein biogenesis: phylogenomic and genetic studies of A-type carriers
    • Vinella, D., Brochier-Armanet, C., Loiseau, L., Talla, E., and Barras, F. (2009) Iron-sulfur (Fe/S) protein biogenesis: phylogenomic and genetic studies of A-type carriers. PLoS Genet 5: e1000497-e1000497.
    • (2009) PLoS Genet , vol.5 , pp. e1000497-e1000497
    • Vinella, D.1    Brochier-Armanet, C.2    Loiseau, L.3    Talla, E.4    Barras, F.5
  • 126
    • 24744461675 scopus 로고    scopus 로고
    • Insights into mechanisms used by Staphylococcus aureus to avoid destruction by human neutrophils
    • Voyich, J.M., Braughton, K.R., Sturdevant, D.E., Whitney, A.R., Saïd-Salim, B., Porcella, S.F., etal. (2005) Insights into mechanisms used by Staphylococcus aureus to avoid destruction by human neutrophils. J Immunol 175: 3907-3919.
    • (2005) J Immunol , vol.175 , pp. 3907-3919
    • Voyich, J.M.1    Braughton, K.R.2    Sturdevant, D.E.3    Whitney, A.R.4    Saïd-Salim, B.5    Porcella, S.F.6
  • 127
    • 0032820452 scopus 로고    scopus 로고
    • Quantifying cellular oxidative stress by dichlorofluorescein assay using microplate reader
    • Wang, H., and Joseph, J.A. (1999) Quantifying cellular oxidative stress by dichlorofluorescein assay using microplate reader. Free Radic Biol Med 27: 612-616.
    • (1999) Free Radic Biol Med , vol.27 , pp. 612-616
    • Wang, H.1    Joseph, J.A.2
  • 128
    • 34147195143 scopus 로고    scopus 로고
    • Iron-dependent degradation of apo-IRP1 by the ubiquitin-proteasome pathway
    • Wang, J., Fillebeen, C., Chen, G., Biederbick, A., Lill, R., and Pantopoulos, K. (2007) Iron-dependent degradation of apo-IRP1 by the ubiquitin-proteasome pathway. Mol Cell Biol 27: 2423-2430.
    • (2007) Mol Cell Biol , vol.27 , pp. 2423-2430
    • Wang, J.1    Fillebeen, C.2    Chen, G.3    Biederbick, A.4    Lill, R.5    Pantopoulos, K.6
  • 129
    • 0038409882 scopus 로고    scopus 로고
    • A dimer of the FeS cluster biosynthesis protein IscA from cyanobacteria binds a [2Fe2S] cluster between two protomers and transfers it to [2Fe2S] and [4Fe4S] apo proteins
    • Wollenberg, M., Berndt, C., Bill, E., Schwenn, J.D., and Seidler, A. (2003) A dimer of the FeS cluster biosynthesis protein IscA from cyanobacteria binds a [2Fe2S] cluster between two protomers and transfers it to [2Fe2S] and [4Fe4S] apo proteins. Eur J Biochem 270: 1662-1671.
    • (2003) Eur J Biochem , vol.270 , pp. 1662-1671
    • Wollenberg, M.1    Berndt, C.2    Bill, E.3    Schwenn, J.D.4    Seidler, A.5
  • 130
    • 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 Imlay, J.A. (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
  • 131
    • 0035036429 scopus 로고    scopus 로고
    • Identification and characterization of a second superoxide dismutase gene (sodM) from Staphylococcus aureus
    • Wright Valderas, M., and Hart, M.E. (2001) Identification and characterization of a second superoxide dismutase gene (sodM) from Staphylococcus aureus. J Bacteriol 183: 3399-3407.
    • (2001) J Bacteriol , vol.183 , pp. 3399-3407
    • Wright Valderas, M.1    Hart, M.E.2
  • 133
    • 80054720193 scopus 로고    scopus 로고
    • The E. coli monothiol glutaredoxin GrxD forms homodimeric and heterodimeric FeS cluster containing complexes
    • Yeung, N., Gold, B., Liu, N.L., Prathapam, R., Sterling, H.J., Willams, E.R., and Butland, G. (2011) The E. coli monothiol glutaredoxin GrxD forms homodimeric and heterodimeric FeS cluster containing complexes. Biochemistry 50: 8957-8969.
    • (2011) Biochemistry , vol.50 , pp. 8957-8969
    • Yeung, N.1    Gold, B.2    Liu, N.L.3    Prathapam, R.4    Sterling, H.J.5    Willams, E.R.6    Butland, G.7
  • 135
    • 0027450059 scopus 로고
    • Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis
    • Zheng, L., White, R.H., Cash, V.L., Jack, R.F., and Dean, D.R. (1993) Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis. Proc Natl Acad Sci USA 90: 2754-2758.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 2754-2758
    • Zheng, L.1    White, R.H.2    Cash, V.L.3    Jack, R.F.4    Dean, D.R.5


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