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Volumn 12, Issue 8, 2016, Pages

The DUF59 Containing Protein SufT Is Involved in the Maturation of Iron-Sulfur (FeS) Proteins during Conditions of High FeS Cofactor Demand in Staphylococcus aureus

Author keywords

[No Author keywords available]

Indexed keywords

IRON SULFUR CLUSTER ASSEMBLY PROTEIN; IRON SULFUR PROTEIN; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG; VANCOMYCIN; BACTERIAL PROTEIN; IRON; MUTANT PROTEIN;

EID: 84984876896     PISSN: 15537390     EISSN: 15537404     Source Type: Journal    
DOI: 10.1371/journal.pgen.1006233     Document Type: Article
Times cited : (34)

References (112)
  • 1
    • 34548445911 scopus 로고    scopus 로고
    • Electron paramagnetic resonance and Mossbauer spectroscopy of intact mitochondria from respiring Saccharomyces cerevisiae
    • 17665226,. ().: –.
    • Hudder BN, Morales JG, Stubna A, Munck E, Hendrich MP, et al. (2007) Electron paramagnetic resonance and Mossbauer spectroscopy of intact mitochondria from respiring Saccharomyces cerevisiae. J Biol Inorg Chem12: 1029–1053. 17665226
    • (2007) J Biol Inorg Chem , vol.12 , pp. 1029-1053
    • Hudder, B.N.1    Morales, J.G.2    Stubna, A.3    Munck, E.4    Hendrich, M.P.5
  • 2
    • 33847753939 scopus 로고    scopus 로고
    • Micromolar intracellular hydrogen peroxide disrupts metabolism by damaging iron-sulfur enzymes
    • 17102132, ().: –.
    • Jang S, Imlay JA, (2007) Micromolar intracellular hydrogen peroxide disrupts metabolism by damaging iron-sulfur enzymes. J Biol Chem282: 929–937. 17102132
    • (2007) J Biol Chem , vol.282 , pp. 929-937
    • Jang, S.1    Imlay, J.A.2
  • 3
    • 33645065589 scopus 로고    scopus 로고
    • Iron-sulphur clusters and the problem with oxygen
    • 16430685, ().: –.
    • Imlay JA, (2006) Iron-sulphur clusters and the problem with oxygen. Mol Microbiol59: 1073–1082. 16430685
    • (2006) Mol Microbiol , vol.59 , pp. 1073-1082
    • Imlay, J.A.1
  • 4
    • 84924700922 scopus 로고    scopus 로고
    • Nfu facilitates the maturation of iron-sulfur proteins and participates in virulence in Staphylococcus aureus
    • 25388433,.: –.
    • Mashruwala AA, Pang YY, Rosario-Cruz Z, Chahal HK, Benson MA, et al. Nfu facilitates the maturation of iron-sulfur proteins and participates in virulence in Staphylococcus aureus. Mol Microbiol95: 383–409. doi: 10.1111/mmi.1286025388433
    • 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
  • 5
    • 84855667761 scopus 로고    scopus 로고
    • AirSR, a [2Fe-2S] cluster-containing two-component system, mediates global oxygen sensing and redox signaling in Staphylococcus aureus
    • 22122613,.: –.
    • Sun F, Ji Q, Jones MB, Deng X, Liang H, et al. AirSR, a [2Fe-2S] cluster-containing two-component system, mediates global oxygen sensing and redox signaling in Staphylococcus aureus. J Am Chem Soc134: 305–314. doi: 10.1021/ja207183522122613
    • 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
  • 6
    • 0019886576 scopus 로고
    • Relationship of the oxidation state of the iron-sulfur cluster of aconitase to activity and substrate binding
    • 7326240,. ().: –.
    • Ramsay RR, Dreyer JL, Schloss JV, Jackson RH, Coles CJ, et al. (1981) Relationship of the oxidation state of the iron-sulfur cluster of aconitase to activity and substrate binding. Biochemistry20: 7476–7482. 7326240
    • (1981) Biochemistry , vol.20 , pp. 7476-7482
    • Ramsay, R.R.1    Dreyer, J.L.2    Schloss, J.V.3    Jackson, R.H.4    Coles, C.J.5
  • 7
    • 84859492661 scopus 로고    scopus 로고
    • A bridging [4Fe-4S] cluster and nucleotide binding are essential for function of the Cfd1-Nbp35 complex as a scaffold in iron-sulfur protein maturation
    • 22362766,.: –.
    • Netz DJ, Pierik AJ, Stumpfig M, Bill E, Sharma AK, et al. A bridging [4Fe-4S] cluster and nucleotide binding are essential for function of the Cfd1-Nbp35 complex as a scaffold in iron-sulfur protein maturation. J Biol Chem287: 12365–12378. doi: 10.1074/jbc.M111.32891422362766
    • J Biol Chem , vol.287 , pp. 12365-12378
    • Netz, D.J.1    Pierik, A.J.2    Stumpfig, M.3    Bill, E.4    Sharma, A.K.5
  • 8
    • 65549136266 scopus 로고    scopus 로고
    • An iron-sulfur cluster is essential for the binding of broken DNA by AddAB-type helicase-nucleases
    • 19129187, ().: –.
    • Yeeles JT, Cammack R, Dillingham MS, (2009) An iron-sulfur cluster is essential for the binding of broken DNA by AddAB-type helicase-nucleases. J Biol Chem284: 7746–7755. doi: 10.1074/jbc.M80852620019129187
    • (2009) J Biol Chem , vol.284 , pp. 7746-7755
    • Yeeles, J.T.1    Cammack, R.2    Dillingham, M.S.3
  • 9
    • 33845865301 scopus 로고    scopus 로고
    • Structure of dual function iron regulatory protein 1 complexed with ferritin IRE-RNA
    • 17185597,. ().: –.
    • Walden WE, Selezneva AI, Dupuy J, Volbeda A, Fontecilla-Camps JC, et al. (2006) Structure of dual function iron regulatory protein 1 complexed with ferritin IRE-RNA. Science314: 1903–1908. 17185597
    • (2006) Science , vol.314 , pp. 1903-1908
    • Walden, W.E.1    Selezneva, A.I.2    Dupuy, J.3    Volbeda, A.4    Fontecilla-Camps, J.C.5
  • 11
    • 9844228508 scopus 로고    scopus 로고
    • Activation of the anaerobic ribonucleotide reductase from Escherichia coli. The essential role of the iron-sulfur center for S-adenosylmethionine reduction
    • 9305874,. ().: –.
    • Ollagnier S, Mulliez E, Schmidt PP, Eliasson R, Gaillard J, et al. (1997) Activation of the anaerobic ribonucleotide reductase from Escherichia coli. The essential role of the iron-sulfur center for S-adenosylmethionine reduction. J Biol Chem272: 24216–24223. 9305874
    • (1997) J Biol Chem , vol.272 , pp. 24216-24223
    • Ollagnier, S.1    Mulliez, E.2    Schmidt, P.P.3    Eliasson, R.4    Gaillard, J.5
  • 12
    • 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
    • 18686975, ().: –.
    • Martinez-Gomez NC, Downs DM, (2008) ThiC is an [Fe-S] cluster protein that requires AdoMet to generate the 4-amino-5-hydroxymethyl-2-methylpyrimidine moiety in thiamin synthesis. Biochemistry47: 9054–9056. doi: 10.1021/bi801025318686975
    • (2008) Biochemistry , vol.47 , pp. 9054-9056
    • Martinez-Gomez, N.C.1    Downs, D.M.2
  • 13
    • 23844452716 scopus 로고    scopus 로고
    • Radical S-adenosylmethionine enzyme coproporphyrinogen III oxidase HemN: functional features of the [4Fe-4S] cluster and the two bound S-adenosyl-L-methionines
    • 15967800,. ().: –.
    • Layer G, Grage K, Teschner T, Schunemann V, Breckau D, et al. (2005) Radical S-adenosylmethionine enzyme coproporphyrinogen III oxidase HemN: functional features of the [4Fe-4S] cluster and the two bound S-adenosyl-L-methionines. J Biol Chem280: 29038–29046. 15967800
    • (2005) J Biol Chem , vol.280 , pp. 29038-29046
    • Layer, G.1    Grage, K.2    Teschner, T.3    Schunemann, V.4    Breckau, D.5
  • 14
    • 35348876543 scopus 로고    scopus 로고
    • ErpA, an iron sulfur (Fe S) protein of the A-type essential for respiratory metabolism in Escherichia coli
    • 17698959,. ().: –.
    • Loiseau L, Gerez C, Bekker M, Ollagnier-de Choudens S, Py B, et al. (2007) ErpA, an iron sulfur (Fe S) protein of the A-type essential for respiratory metabolism in Escherichia coli. Proc Natl Acad Sci U S A104: 13626–13631. 17698959
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 13626-13631
    • Loiseau, L.1    Gerez, C.2    Bekker, M.3    Ollagnier-de Choudens, S.4    Py, B.5
  • 15
    • 0016328761 scopus 로고
    • EPR studies on two ferredoxin-type iron-sulfur centers in reconstitutively active, inactive, and reactivated soluble succinate dehydrogenases
    • 4375475, ().: –.
    • Onishi T, Leigh JS, Winter DB, Lim J, King TE, (1974) EPR studies on two ferredoxin-type iron-sulfur centers in reconstitutively active, inactive, and reactivated soluble succinate dehydrogenases. Biochem Biophys Res Commun61: 1026–1035. 4375475
    • (1974) Biochem Biophys Res Commun , vol.61 , pp. 1026-1035
    • Onishi, T.1    Leigh, J.S.2    Winter, D.B.3    Lim, J.4    King, T.E.5
  • 16
    • 0016356064 scopus 로고
    • EPR studies on a Hipip type iron-sulfur center in the succinate dehydrogenase segment of the respiratory chain
    • 4375474, ().: –.
    • Onishi T, Winter DB, Lim J, King TE, (1974) EPR studies on a Hipip type iron-sulfur center in the succinate dehydrogenase segment of the respiratory chain. Biochem Biophys Res Commun61: 1017–1025. 4375474
    • (1974) Biochem Biophys Res Commun , vol.61 , pp. 1017-1025
    • Onishi, T.1    Winter, D.B.2    Lim, J.3    King, T.E.4
  • 17
    • 84896940877 scopus 로고    scopus 로고
    • Mechanism of nitrogen fixation by nitrogenase: the next stage
    • 24467365,.: –.
    • Hoffman BM, Lukoyanov D, Yang ZY, Dean DR, Seefeldt LC, Mechanism of nitrogen fixation by nitrogenase: the next stage. Chem Rev114: 4041–4062. doi: 10.1021/cr400641x24467365
    • Chem Rev , vol.114 , pp. 4041-4062
    • Hoffman, B.M.1    Lukoyanov, D.2    Yang, Z.Y.3    Dean, D.R.4    Seefeldt, L.C.5
  • 18
    • 3943074536 scopus 로고    scopus 로고
    • The metalloclusters of carbon monoxide dehydrogenase/acetyl-CoA synthase: a story in pictures
    • 15221484, ().: –.
    • Drennan CL, Doukov TI, Ragsdale SW, (2004) The metalloclusters of carbon monoxide dehydrogenase/acetyl-CoA synthase: a story in pictures. J Biol Inorg Chem9: 511–515. 15221484
    • (2004) J Biol Inorg Chem , vol.9 , pp. 511-515
    • Drennan, C.L.1    Doukov, T.I.2    Ragsdale, S.W.3
  • 21
    • 84859976622 scopus 로고    scopus 로고
    • Battles with Iron: Manganese in Oxidative Stress Protection
    • 22247543, ().: –.
    • Aguirre JD, Culotta VC, (2012) Battles with Iron: Manganese in Oxidative Stress Protection. Journal of Biological Chemistry287: 13541–13548. doi: 10.1074/jbc.R111.31218122247543
    • (2012) Journal of Biological Chemistry , vol.287 , pp. 13541-13548
    • Aguirre, J.D.1    Culotta, V.C.2
  • 22
    • 0037047411 scopus 로고    scopus 로고
    • A third bacterial system for the assembly of iron-sulfur clusters with homologs in archaea and plastids
    • 12089140, ().: –.
    • Takahashi Y, Tokumoto U, (2002) A third bacterial system for the assembly of iron-sulfur clusters with homologs in archaea and plastids. J Biol Chem277: 28380–28393. 12089140
    • (2002) J Biol Chem , vol.277 , pp. 28380-28393
    • Takahashi, Y.1    Tokumoto, U.2
  • 23
    • 0032557666 scopus 로고    scopus 로고
    • Assembly of iron-sulfur clusters. Identification of an iscSUA-hscBA-fdx gene cluster from Azotobacter vinelandii
    • 9582371, ().: –.
    • Zheng L, Cash VL, Flint DH, Dean DR, (1998) Assembly of iron-sulfur clusters. Identification of an iscSUA-hscBA-fdx gene cluster from Azotobacter vinelandii. J Biol Chem273: 13264–13272. 9582371
    • (1998) J Biol Chem , vol.273 , pp. 13264-13272
    • Zheng, L.1    Cash, V.L.2    Flint, D.H.3    Dean, D.R.4
  • 25
    • 84926221482 scopus 로고    scopus 로고
    • Interplay between oxygen and Fe-S cluster biogenesis: insights from the Suf pathway
    • 25153801,.: –.
    • Boyd ES, Thomas KM, Dai Y, Boyd JM, Outten FW, Interplay between oxygen and Fe-S cluster biogenesis: insights from the Suf pathway. Biochemistry53: 5834–5847. doi: 10.1021/bi500488r25153801
    • Biochemistry , vol.53 , pp. 5834-5847
    • Boyd, E.S.1    Thomas, K.M.2    Dai, Y.3    Boyd, J.M.4    Outten, F.W.5
  • 26
    • 34250316177 scopus 로고    scopus 로고
    • SufE transfers sulfur from SufS to SufB for iron-sulfur cluster assembly
    • 17350958,. ().: –.
    • Layer G, Gaddam SA, Ayala-Castro CN, Ollagnier-de Choudens S, Lascoux D, et al. (2007) SufE transfers sulfur from SufS to SufB for iron-sulfur cluster assembly. J Biol Chem282: 13342–13350. 17350958
    • (2007) J Biol Chem , vol.282 , pp. 13342-13350
    • Layer, G.1    Gaddam, S.A.2    Ayala-Castro, C.N.3    Ollagnier-de Choudens, S.4    Lascoux, D.5
  • 27
    • 84892609770 scopus 로고    scopus 로고
    • Fe-S cluster biogenesis in Gram-positive bacteria: SufU is a zinc-dependent sulfur transfer protein
    • 24321018,. ().: –.
    • Selbach BP, Chung AH, Scott AD, George SJ, Cramer SP, et al. (2014) Fe-S cluster biogenesis in Gram-positive bacteria: SufU is a zinc-dependent sulfur transfer protein. Biochemistry53: 152–160. doi: 10.1021/bi401197824321018
    • (2014) Biochemistry , vol.53 , pp. 152-160
    • Selbach, B.P.1    Chung, A.H.2    Scott, A.D.3    George, S.J.4    Cramer, S.P.5
  • 29
    • 84866524763 scopus 로고    scopus 로고
    • Separate FeS scaffold and carrier functions for SufB(2)C(2) and SufA during in vitro maturation of [2Fe2S] Fdx
    • 23018275,.: –.
    • Chahal HK, Outten FW, Separate FeS scaffold and carrier functions for SufB(2)C(2) and SufA during in vitro maturation of [2Fe2S] Fdx. J Inorg Biochem116: 126–134. doi: 10.1016/j.jinorgbio.2012.06.00823018275
    • J Inorg Biochem , vol.116 , pp. 126-134
    • Chahal, H.K.1    Outten, F.W.2
  • 30
    • 84943454454 scopus 로고    scopus 로고
    • Bacillithiol has a role in Fe-S cluster biogenesis in Staphylococcus aureus
    • 26135358,.: –.
    • Rosario-Cruz Z, Chahal HK, Mike LA, Skaar EP, Boyd JM, Bacillithiol has a role in Fe-S cluster biogenesis in Staphylococcus aureus. Mol Microbiol98: 218–242. doi: 10.1111/mmi.1311526135358
    • Mol Microbiol , vol.98 , pp. 218-242
    • Rosario-Cruz, Z.1    Chahal, H.K.2    Mike, L.A.3    Skaar, E.P.4    Boyd, J.M.5
  • 31
    • 84908405927 scopus 로고    scopus 로고
    • Genes Contributing to Staphylococcus aureus Fitness in Abscess- and Infection-Related Ecologies
    • Valentino MD, Foulston L, Sadaka A, Kos VN, Villet RA, et al. (2014) Genes Contributing to Staphylococcus aureus Fitness in Abscess- and Infection-Related Ecologies. MBio5.
    • (2014) MBio , vol.5
    • Valentino, M.D.1    Foulston, L.2    Sadaka, A.3    Kos, V.N.4    Villet, R.A.5
  • 32
    • 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
    • 17237162, ().: –.
    • Dos Santos PC, Johnson DC, Ragle BE, Unciuleac MC, Dean DR, (2007) Controlled expression of nif and isc iron-sulfur protein maturation components reveals target specificity and limited functional replacement between the two systems. J Bacteriol189: 2854–2862. 17237162
    • (2007) J Bacteriol , vol.189 , pp. 2854-2862
    • Dos Santos, P.C.1    Johnson, D.C.2    Ragle, B.E.3    Unciuleac, M.C.4    Dean, D.R.5
  • 33
    • 84926324674 scopus 로고    scopus 로고
    • A new platform for ultra-high density Staphylococcus aureus transposon libraries
    • 25888466,.:.
    • Santiago M, Matano LM, Moussa SH, Gilmore MS, Walker S, et al. A new platform for ultra-high density Staphylococcus aureus transposon libraries. BMC Genomics16: 252. doi: 10.1186/s12864-015-1361-325888466
    • BMC Genomics , vol.16 , pp. 252
    • Santiago, M.1    Matano, L.M.2    Moussa, S.H.3    Gilmore, M.S.4    Walker, S.5
  • 34
    • 84908405927 scopus 로고    scopus 로고
    • Genes contributing to Staphylococcus aureus fitness in abscess- and infection-related ecologies
    • 25182329,.: –.
    • Valentino MD, Foulston L, Sadaka A, Kos VN, Villet RA, et al. Genes contributing to Staphylococcus aureus fitness in abscess- and infection-related ecologies. MBio5: e01729–01714. doi: 10.1128/mBio.01729-1425182329
    • MBio , vol.5 , pp. e01714-e01729
    • Valentino, M.D.1    Foulston, L.2    Sadaka, A.3    Kos, V.N.4    Villet, R.A.5
  • 35
    • 33646716659 scopus 로고    scopus 로고
    • The mechanism of superoxide production by NADH:ubiquinone oxidoreductase (complex I) from bovine heart mitochondria
    • 16682634, ().: –.
    • Kussmaul L, Hirst J, (2006) The mechanism of superoxide production by NADH:ubiquinone oxidoreductase (complex I) from bovine heart mitochondria. Proc Natl Acad Sci U S A103: 7607–7612. 16682634
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 7607-7612
    • Kussmaul, L.1    Hirst, J.2
  • 36
    • 0033538048 scopus 로고    scopus 로고
    • The identification of primary sites of superoxide and hydrogen peroxide formation in the aerobic respiratory chain and sulfite reductase complex of Escherichia coli
    • 10187794, ().: –.
    • Messner KR, Imlay JA, (1999) The identification of primary sites of superoxide and hydrogen peroxide formation in the aerobic respiratory chain and sulfite reductase complex of Escherichia coli. J Biol Chem274: 10119–10128. 10187794
    • (1999) J Biol Chem , vol.274 , pp. 10119-10128
    • Messner, K.R.1    Imlay, J.A.2
  • 37
    • 84879422944 scopus 로고    scopus 로고
    • The molecular mechanisms and physiological consequences of oxidative stress: lessons from a model bacterium
    • 23712352,.: –.
    • Imlay JA, The molecular mechanisms and physiological consequences of oxidative stress: lessons from a model bacterium. Nat Rev Microbiol11: 443–454. doi: 10.1038/nrmicro303223712352
    • Nat Rev Microbiol , vol.11 , pp. 443-454
    • Imlay, J.A.1
  • 38
    • 33847753939 scopus 로고    scopus 로고
    • Micromolar intracellular hydrogen peroxide disrupts metabolism by damaging iron-sulfur enzymes
    • 17102132, ().: –.
    • Jang S, Imlay JA, (2007) Micromolar intracellular hydrogen peroxide disrupts metabolism by damaging iron-sulfur enzymes. J Biol Chem282: 929–937. 17102132
    • (2007) J Biol Chem , vol.282 , pp. 929-937
    • Jang, S.1    Imlay, J.A.2
  • 39
    • 0030465238 scopus 로고    scopus 로고
    • Superoxide accelerates DNA damage by elevating free-iron levels
    • 8942986, ().: –.
    • Keyer K, Imlay JA, (1996) Superoxide accelerates DNA damage by elevating free-iron levels. Proc Natl Acad Sci USA93: 13635–13640. 8942986
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 13635-13640
    • Keyer, K.1    Imlay, J.A.2
  • 40
    • 7244239273 scopus 로고    scopus 로고
    • Repair of oxidized iron-sulfur clusters in Escherichia coli
    • 15308657, ().: –.
    • Djaman O, Outten FW, Imlay JA, (2004) Repair of oxidized iron-sulfur clusters in Escherichia coli. J Biol Chem279: 44590–44599. 15308657
    • (2004) J Biol Chem , vol.279 , pp. 44590-44599
    • Djaman, O.1    Outten, F.W.2    Imlay, J.A.3
  • 41
    • 40449114521 scopus 로고    scopus 로고
    • Widespread distribution in pathogenic bacteria of di-iron proteins that repair oxidative and nitrosative damage to iron-sulfur centers
    • 18203837,. ().: –.
    • Overton TW, Justino MC, Li Y, Baptista JM, Melo AM, et al. (2008) Widespread distribution in pathogenic bacteria of di-iron proteins that repair oxidative and nitrosative damage to iron-sulfur centers. J Bacteriol190: 2004–2013. doi: 10.1128/JB.01733-0718203837
    • (2008) J Bacteriol , vol.190 , pp. 2004-2013
    • Overton, T.W.1    Justino, M.C.2    Li, Y.3    Baptista, J.M.4    Melo, A.M.5
  • 42
    • 84896460464 scopus 로고    scopus 로고
    • Distinct roles of the Salmonella enterica serovar Typhimurium CyaY and YggX proteins in the biosynthesis and repair of iron-sulfur clusters
    • 24421039,.: –.
    • Velayudhan J, Karlinsey JE, Frawley ER, Becker LA, Nartea M, et al. Distinct roles of the Salmonella enterica serovar Typhimurium CyaY and YggX proteins in the biosynthesis and repair of iron-sulfur clusters. Infect Immun82: 1390–1401. doi: 10.1128/IAI.01022-1324421039
    • Infect Immun , vol.82 , pp. 1390-1401
    • Velayudhan, J.1    Karlinsey, J.E.2    Frawley, E.R.3    Becker, L.A.4    Nartea, M.5
  • 43
    • 0034043254 scopus 로고    scopus 로고
    • Role of the Azotobacter vinelandii nitrogenase-protective Shethna protein in preventing oxygen-mediated cell death
    • 10851006, ().: –.
    • Maier RJ, Moshiri F, (2000) Role of the Azotobacter vinelandii nitrogenase-protective Shethna protein in preventing oxygen-mediated cell death. J Bacteriol182: 3854–3857. 10851006
    • (2000) J Bacteriol , vol.182 , pp. 3854-3857
    • Maier, R.J.1    Moshiri, F.2
  • 44
    • 0030884074 scopus 로고    scopus 로고
    • Isolation and analysis of the gene encoding the pyruvate-ferredoxin oxidoreductase of Desulfovibrio africanus, production of the recombinant enzyme in Escherichia coli, and effect of carboxy-terminal deletions on its stability
    • 9294422, ().: –.
    • Pieulle L, Magro V, Hatchikian EC, (1997) Isolation and analysis of the gene encoding the pyruvate-ferredoxin oxidoreductase of Desulfovibrio africanus, production of the recombinant enzyme in Escherichia coli, and effect of carboxy-terminal deletions on its stability. J Bacteriol179: 5684–5692. 9294422
    • (1997) J Bacteriol , vol.179 , pp. 5684-5692
    • Pieulle, L.1    Magro, V.2    Hatchikian, E.C.3
  • 45
    • 84891588915 scopus 로고    scopus 로고
    • Evolution of the cytosolic iron-sulfur cluster assembly machinery in Blastocystis species and other microbial eukaryotes
    • 24243793,.: –.
    • Tsaousis AD, Gentekaki E, Eme L, Gaston D, Roger AJ, Evolution of the cytosolic iron-sulfur cluster assembly machinery in Blastocystis species and other microbial eukaryotes. Eukaryot Cell13: 143–153. doi: 10.1128/EC.00158-1324243793
    • Eukaryot Cell , vol.13 , pp. 143-153
    • Tsaousis, A.D.1    Gentekaki, E.2    Eme, L.3    Gaston, D.4    Roger, A.J.5
  • 46
    • 85045835706 scopus 로고    scopus 로고
    • Human CIA2A-FAM96A and CIA2B-FAM96B integrate iron homeostasis and maturation of different subsets of cytosolic-nuclear iron-sulfur proteins
    • 23891004,.: –.
    • Stehling O, Mascarenhas J, Vashisht AA, Sheftel AD, Niggemeyer B, et al. Human CIA2A-FAM96A and CIA2B-FAM96B integrate iron homeostasis and maturation of different subsets of cytosolic-nuclear iron-sulfur proteins. Cell Metab18: 187–198. doi: 10.1016/j.cmet.2013.06.01523891004
    • Cell Metab , vol.18 , pp. 187-198
    • Stehling, O.1    Mascarenhas, J.2    Vashisht, A.A.3    Sheftel, A.D.4    Niggemeyer, B.5
  • 47
    • 84870700689 scopus 로고    scopus 로고
    • The DUF59 family gene AE7 acts in the cytosolic iron-sulfur cluster assembly pathway to maintain nuclear genome integrity in Arabidopsis
    • 23104832,.: –.
    • Luo D, Bernard DG, Balk J, Hai H, Cui X, The DUF59 family gene AE7 acts in the cytosolic iron-sulfur cluster assembly pathway to maintain nuclear genome integrity in Arabidopsis. Plant Cell24: 4135–4148. doi: 10.1105/tpc.112.10260823104832
    • Plant Cell , vol.24 , pp. 4135-4148
    • Luo, D.1    Bernard, D.G.2    Balk, J.3    Hai, H.4    Cui, X.5
  • 49
    • 45549084273 scopus 로고    scopus 로고
    • Staphylococcal biofilms
    • 18453278, ().: –.
    • Otto M, (2008) Staphylococcal biofilms. Curr Top Microbiol Immunol322: 207–228. 18453278
    • (2008) Curr Top Microbiol Immunol , vol.322 , pp. 207-228
    • Otto, M.1
  • 50
    • 0033962325 scopus 로고    scopus 로고
    • Exotoxins of Staphylococcus aureus
    • 10627489, ().: –, table of contents.
    • Dinges MM, Orwin PM, Schlievert PM, (2000) Exotoxins of Staphylococcus aureus. Clin Microbiol Rev13: 16–34, table of contents. 10627489
    • (2000) Clin Microbiol Rev , vol.13 , pp. 16-34
    • Dinges, M.M.1    Orwin, P.M.2    Schlievert, P.M.3
  • 51
    • 84875227539 scopus 로고    scopus 로고
    • Essential Staphylococcus aureus toxin export system
    • 23396209,.: –.
    • Chatterjee SS, Joo HS, Duong AC, Dieringer TD, Tan VY, et al. Essential Staphylococcus aureus toxin export system. Nat Med19: 364–367. doi: 10.1038/nm.304723396209
    • Nat Med , vol.19 , pp. 364-367
    • Chatterjee, S.S.1    Joo, H.S.2    Duong, A.C.3    Dieringer, T.D.4    Tan, V.Y.5
  • 52
    • 36849049884 scopus 로고    scopus 로고
    • Identification of novel cytolytic peptides as key virulence determinants for community-associated MRSA
    • 17994102,. ().: –.
    • Wang R, Braughton KR, Kretschmer D, Bach TH, Queck SY, et al. (2007) Identification of novel cytolytic peptides as key virulence determinants for community-associated MRSA. Nat Med13: 1510–1514. 17994102
    • (2007) Nat Med , vol.13 , pp. 1510-1514
    • Wang, R.1    Braughton, K.R.2    Kretschmer, D.3    Bach, T.H.4    Queck, S.Y.5
  • 53
    • 77954586271 scopus 로고    scopus 로고
    • Community-associated methicillin-resistant Staphylococcus aureus: epidemiology and clinical consequences of an emerging epidemic
    • 20610826,.: –.
    • David MZ, Daum RS, Community-associated methicillin-resistant Staphylococcus aureus: epidemiology and clinical consequences of an emerging epidemic. Clin Microbiol Rev23: 616–687. doi: 10.1128/CMR.00081-0920610826
    • Clin Microbiol Rev , vol.23 , pp. 616-687
    • David, M.Z.1    Daum, R.S.2
  • 54
    • 84903772231 scopus 로고    scopus 로고
    • Mechanisms of vancomycin resistance in Staphylococcus aureus
    • 24983424,.: –.
    • Gardete S, Tomasz A, Mechanisms of vancomycin resistance in Staphylococcus aureus. J Clin Invest124: 2836–2840. doi: 10.1172/JCI6883424983424
    • J Clin Invest , vol.124 , pp. 2836-2840
    • Gardete, S.1    Tomasz, A.2
  • 55
    • 4644344349 scopus 로고    scopus 로고
    • Cell wall composition and decreased autolytic activity and lysostaphin susceptibility of glycopeptide-intermediate Staphylococcus aureus
    • 15388430,. ().: –.
    • Koehl JL, Muthaiyan A, Jayaswal RK, Ehlert K, Labischinski H, et al. (2004) Cell wall composition and decreased autolytic activity and lysostaphin susceptibility of glycopeptide-intermediate Staphylococcus aureus. Antimicrob Agents Chemother48: 3749–3757. 15388430
    • (2004) Antimicrob Agents Chemother , vol.48 , pp. 3749-3757
    • Koehl, J.L.1    Muthaiyan, A.2    Jayaswal, R.K.3    Ehlert, K.4    Labischinski, H.5
  • 56
    • 3543014927 scopus 로고    scopus 로고
    • Escherichia coli L-serine deaminase requires a [4Fe-4S] cluster in catalysis
    • 15155761,. ().: –.
    • Cicchillo RM, Baker MA, Schnitzer EJ, Newman EB, Krebs C, et al. (2004) Escherichia coli L-serine deaminase requires a [4Fe-4S] cluster in catalysis. J Biol Chem279: 32418–32425. 15155761
    • (2004) J Biol Chem , vol.279 , pp. 32418-32425
    • Cicchillo, R.M.1    Baker, M.A.2    Schnitzer, E.J.3    Newman, E.B.4    Krebs, C.5
  • 57
    • 78650078496 scopus 로고    scopus 로고
    • Quantitative reactivity profiling predicts functional cysteines in proteomes
    • 21085121,.: –.
    • Weerapana E, Wang C, Simon GM, Richter F, Khare S, et al. Quantitative reactivity profiling predicts functional cysteines in proteomes. Nature468: 790–795. doi: 10.1038/nature0947221085121
    • Nature , vol.468 , pp. 790-795
    • Weerapana, E.1    Wang, C.2    Simon, G.M.3    Richter, F.4    Khare, S.5
  • 58
    • 0015880415 scopus 로고
    • Amino acid requirements for the production of enterotoxin B by Staphylococcus aureus S-6 in a chemically defined medium
    • 4715560, ().: –.
    • Miller RD, Fung DY, (1973) Amino acid requirements for the production of enterotoxin B by Staphylococcus aureus S-6 in a chemically defined medium. Appl Microbiol25: 800–806. 4715560
    • (1973) Appl Microbiol , vol.25 , pp. 800-806
    • Miller, R.D.1    Fung, D.Y.2
  • 59
    • 0015079735 scopus 로고
    • Isolation and characterization of tricarboxylic acid cycle mutants of Bacillus subtilis
    • 4997541, ().: –.
    • Carls RA, Hanson RS, (1971) Isolation and characterization of tricarboxylic acid cycle mutants of Bacillus subtilis. J Bacteriol106: 848–855. 4997541
    • (1971) J Bacteriol , vol.106 , pp. 848-855
    • Carls, R.A.1    Hanson, R.S.2
  • 60
    • 0027165156 scopus 로고
    • The role and properties of the iron-sulfur cluster in Escherichia coli dihydroxy-acid dehydratase
    • 8325851, ().: –.
    • Flint DH, Emptage MH, Finnegan MG, Fu W, Johnson MK, (1993) The role and properties of the iron-sulfur cluster in Escherichia coli dihydroxy-acid dehydratase. Journal of Biological Chemistry268: 14732–14742. 8325851
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 14732-14742
    • Flint, D.H.1    Emptage, M.H.2    Finnegan, M.G.3    Fu, W.4    Johnson, M.K.5
  • 61
    • 0025865421 scopus 로고
    • Homology between IRE-BP, a regulatory RNA-binding protein, aconitase, and isopropylmalate isomerase
    • 1903202, ().: –.
    • Hentze MW, Argos P, (1991) Homology between IRE-BP, a regulatory RNA-binding protein, aconitase, and isopropylmalate isomerase. Nucleic Acids Res19: 1739–1740. 1903202
    • (1991) Nucleic Acids Res , vol.19 , pp. 1739-1740
    • Hentze, M.W.1    Argos, P.2
  • 62
    • 57349161245 scopus 로고    scopus 로고
    • Characterization of the oxygen-responsive NreABC regulon of Staphylococcus aureus
    • 18820014,. ().: –.
    • Schlag S, Fuchs S, Nerz C, Gaupp R, Engelmann S, et al. (2008) Characterization of the oxygen-responsive NreABC regulon of Staphylococcus aureus. J Bacteriol190: 7847–7858. doi: 10.1128/JB.00905-0818820014
    • (2008) J Bacteriol , vol.190 , pp. 7847-7858
    • Schlag, S.1    Fuchs, S.2    Nerz, C.3    Gaupp, R.4    Engelmann, S.5
  • 63
    • 84873059613 scopus 로고    scopus 로고
    • Regulation of iron-sulphur cluster homeostasis through transcriptional control of the Isc pathway by [2Fe-2S]-IscR in Escherichia coli
    • 23075318,.: –.
    • Giel JL, Nesbit AD, Mettert EL, Fleischhacker AS, Wanta BT, et al. Regulation of iron-sulphur cluster homeostasis through transcriptional control of the Isc pathway by [2Fe-2S]-IscR in Escherichia coli. Mol Microbiol87: 478–492. doi: 10.1111/mmi.1205223075318
    • Mol Microbiol , vol.87 , pp. 478-492
    • Giel, J.L.1    Nesbit, A.D.2    Mettert, E.L.3    Fleischhacker, A.S.4    Wanta, B.T.5
  • 64
    • 0033056490 scopus 로고    scopus 로고
    • Characterization of the major superoxide dismutase of Staphylococcus aureus and its role in starvation survival, stress resistance, and pathogenicity
    • 10383955, ().: –.
    • Clements MO, Watson SP, Foster SJ, (1999) Characterization of the major superoxide dismutase of Staphylococcus aureus and its role in starvation survival, stress resistance, and pathogenicity. J Bacteriol181: 3898–3903. 10383955
    • (1999) J Bacteriol , vol.181 , pp. 3898-3903
    • Clements, M.O.1    Watson, S.P.2    Foster, S.J.3
  • 65
    • 0035209075 scopus 로고    scopus 로고
    • Alkyl hydroperoxide reductase is the primary scavenger of endogenous hydrogen peroxide in Escherichia coli
    • 11717276, ().: –.
    • Seaver LC, Imlay JA, (2001) Alkyl hydroperoxide reductase is the primary scavenger of endogenous hydrogen peroxide in Escherichia coli. J Bacteriol183: 7173–7181. 11717276
    • (2001) J Bacteriol , vol.183 , pp. 7173-7181
    • Seaver, L.C.1    Imlay, J.A.2
  • 66
    • 24344488420 scopus 로고    scopus 로고
    • Identification of the Mycobacterium tuberculosis SUF machinery as the exclusive mycobacterial system of [Fe-S] cluster assembly: evidence for its implication in the pathogen's survival
    • 16109955, ().: –.
    • Huet G, Daffe M, Saves I, (2005) Identification of the Mycobacterium tuberculosis SUF machinery as the exclusive mycobacterial system of [Fe-S] cluster assembly: evidence for its implication in the pathogen's survival. J Bacteriol187: 6137–6146. 16109955
    • (2005) J Bacteriol , vol.187 , pp. 6137-6146
    • Huet, G.1    Daffe, M.2    Saves, I.3
  • 67
    • 0041744003 scopus 로고    scopus 로고
    • Correlation of acetate catabolism and growth yield in Staphylococcus aureus: implications for host-pathogen interactions
    • 12874354,. ().: –.
    • Somerville GA, Said-Salim B, Wickman JM, Raffel SJ, Kreiswirth BN, et al. (2003) Correlation of acetate catabolism and growth yield in Staphylococcus aureus: implications for host-pathogen interactions. Infect Immun71: 4724–4732. 12874354
    • (2003) Infect Immun , vol.71 , pp. 4724-4732
    • Somerville, G.A.1    Said-Salim, B.2    Wickman, J.M.3    Raffel, S.J.4    Kreiswirth, B.N.5
  • 68
    • 84922118690 scopus 로고    scopus 로고
    • The Staphylococcus aureus NuoL-like protein MpsA contributes to the generation of membrane potential
    • 25448817,.: –.
    • Mayer S, Steffen W, Steuber J, Gotz F, The Staphylococcus aureus NuoL-like protein MpsA contributes to the generation of membrane potential. J Bacteriol197: 794–806. doi: 10.1128/JB.02127-1425448817
    • J Bacteriol , vol.197 , pp. 794-806
    • Mayer, S.1    Steffen, W.2    Steuber, J.3    Gotz, F.4
  • 69
    • 84901227870 scopus 로고    scopus 로고
    • Influence of iron and aeration on Staphylococcus aureus growth, metabolism, and transcription
    • 24706736, ().: –.
    • Ledala N, Zhang B, Seravalli J, Powers R, Somerville GA, (2014) Influence of iron and aeration on Staphylococcus aureus growth, metabolism, and transcription. J Bacteriol196: 2178–2189. doi: 10.1128/JB.01475-1424706736
    • (2014) J Bacteriol , vol.196 , pp. 2178-2189
    • Ledala, N.1    Zhang, B.2    Seravalli, J.3    Powers, R.4    Somerville, G.A.5
  • 70
    • 0036840950 scopus 로고    scopus 로고
    • Staphylococcus aureus aconitase inactivation unexpectedly inhibits post-exponential-phase growth and enhances stationary-phase survival
    • 12379717,. ().: –.
    • Somerville GA, Chaussee MS, Morgan CI, Fitzgerald JR, Dorward DW, et al. (2002) Staphylococcus aureus aconitase inactivation unexpectedly inhibits post-exponential-phase growth and enhances stationary-phase survival. Infect Immun70: 6373–6382. 12379717
    • (2002) Infect Immun , vol.70 , pp. 6373-6382
    • Somerville, G.A.1    Chaussee, M.S.2    Morgan, C.I.3    Fitzgerald, J.R.4    Dorward, D.W.5
  • 71
    • 0037634030 scopus 로고    scopus 로고
    • Mutation of sarA in Staphylococcus aureus limits biofilm formation
    • 12819120, ().: –.
    • Beenken KE, Blevins JS, Smeltzer MS, (2003) Mutation of sarA in Staphylococcus aureus limits biofilm formation. Infect Immun71: 4206–4211. 12819120
    • (2003) Infect Immun , vol.71 , pp. 4206-4211
    • Beenken, K.E.1    Blevins, J.S.2    Smeltzer, M.S.3
  • 72
    • 43049135194 scopus 로고    scopus 로고
    • Agr-mediated dispersal of Staphylococcus aureus biofilms
    • 18437240, ().:.
    • Boles BR, Horswill AR, (2008) Agr-mediated dispersal of Staphylococcus aureus biofilms. PLoS Pathog4: e1000052. doi: 10.1371/journal.ppat.100005218437240
    • (2008) PLoS Pathog , vol.4 , pp. e1000052
    • Boles, B.R.1    Horswill, A.R.2
  • 73
    • 63149097265 scopus 로고    scopus 로고
    • Interconnections between Sigma B, agr, and Proteolytic Activity in Staphylococcus aureus Biofilm Maturation
    • 19188357, ().: –.
    • Lauderdale KJ, Boles BR, Cheung AL, Horswill AR, (2009) Interconnections between Sigma B, agr, and Proteolytic Activity in Staphylococcus aureus Biofilm Maturation. Infect Immun77: 1623–1635. doi: 10.1128/IAI.01036-0819188357
    • (2009) Infect Immun , vol.77 , pp. 1623-1635
    • Lauderdale, K.J.1    Boles, B.R.2    Cheung, A.L.3    Horswill, A.R.4
  • 74
    • 0033972069 scopus 로고    scopus 로고
    • Characterization of passage-selected vancomycin-resistant Staphylococcus aureus strains of diverse parental backgrounds
    • 10639353,. ().: –.
    • Pfeltz RF, Singh VK, Schmidt JL, Batten MA, Baranyk CS, et al. (2000) Characterization of passage-selected vancomycin-resistant Staphylococcus aureus strains of diverse parental backgrounds. Antimicrob Agents Chemother44: 294–303. 10639353
    • (2000) Antimicrob Agents Chemother , vol.44 , pp. 294-303
    • Pfeltz, R.F.1    Singh, V.K.2    Schmidt, J.L.3    Batten, M.A.4    Baranyk, C.S.5
  • 75
    • 68349146112 scopus 로고    scopus 로고
    • Understanding synergy in genetic interactions
    • 19665253, ().: –.
    • Perez-Perez JM, Candela H, Micol JL, (2009) Understanding synergy in genetic interactions. Trends Genet25: 368–376. doi: 10.1016/j.tig.2009.06.00419665253
    • (2009) Trends Genet , vol.25 , pp. 368-376
    • Perez-Perez, J.M.1    Candela, H.2    Micol, J.L.3
  • 76
    • 67149111967 scopus 로고    scopus 로고
    • Iron-sulfur (Fe/S) protein biogenesis: phylogenomic and genetic studies of A-type carriers
    • 19478995, ().:.
    • Vinella D, Brochier-Armanet C, Loiseau L, Talla E, Barras F, (2009) Iron-sulfur (Fe/S) protein biogenesis: phylogenomic and genetic studies of A-type carriers. PLoS Genet5: e1000497. doi: 10.1371/journal.pgen.100049719478995
    • (2009) PLoS Genet , vol.5 , pp. e1000497
    • Vinella, D.1    Brochier-Armanet, C.2    Loiseau, L.3    Talla, E.4    Barras, F.5
  • 77
    • 2442567822 scopus 로고    scopus 로고
    • A suf operon requirement for Fe-S cluster assembly during iron starvation in Escherichia coli
    • 15101990, ().: –.
    • Outten FW, Djaman O, Storz G, (2004) A suf operon requirement for Fe-S cluster assembly during iron starvation in Escherichia coli. Mol Microbiol52: 861–872. 15101990
    • (2004) Mol Microbiol , vol.52 , pp. 861-872
    • Outten, F.W.1    Djaman, O.2    Storz, G.3
  • 78
    • 78649983777 scopus 로고    scopus 로고
    • Hydrogen peroxide inactivates the Escherichia coli Isc iron-sulphur assembly system, and OxyR induces the Suf system to compensate
    • 21143317, ().: –.
    • Jang S, Imlay JA, (2010) Hydrogen peroxide inactivates the Escherichia coli Isc iron-sulphur assembly system, and OxyR induces the Suf system to compensate. Mol Microbiol78: 1448–1467. doi: 10.1111/j.1365-2958.2010.07418.x21143317
    • (2010) Mol Microbiol , vol.78 , pp. 1448-1467
    • Jang, S.1    Imlay, J.A.2
  • 79
    • 84866513533 scopus 로고    scopus 로고
    • Monothiol glutaredoxins function in storing and transporting [Fe2S2] clusters assembled on IscU scaffold proteins
    • 22963613,.: –.
    • Shakamuri P, Zhang B, Johnson MK, Monothiol glutaredoxins function in storing and transporting [Fe2S2] clusters assembled on IscU scaffold proteins. J Am Chem Soc134: 15213–15216. 22963613
    • J Am Chem Soc , vol.134 , pp. 15213-15216
    • Shakamuri, P.1    Zhang, B.2    Johnson, M.K.3
  • 80
    • 84889850708 scopus 로고    scopus 로고
    • Modulation of cell wall synthesis and susceptibility to vancomycin by the two-component system AirSR in Staphylococcus aureus NCTC8325
    • 24320748,.:.
    • Sun H, Yang Y, Xue T, Sun B, Modulation of cell wall synthesis and susceptibility to vancomycin by the two-component system AirSR in Staphylococcus aureus NCTC8325. BMC Microbiol13: 286. doi: 10.1186/1471-2180-13-28624320748
    • BMC Microbiol , vol.13 , pp. 286
    • Sun, H.1    Yang, Y.2    Xue, T.3    Sun, B.4
  • 81
    • 67349128581 scopus 로고    scopus 로고
    • Loss of vancomycin bactericidal activity against accessory gene regulator (agr) dysfunctional Staphylococcus aureus under conditions of high bacterial density
    • 19345040, ().: –.
    • Tsuji BT, Harigaya Y, Lesse AJ, Sakoulas G, Mylotte JM, (2009) Loss of vancomycin bactericidal activity against accessory gene regulator (agr) dysfunctional Staphylococcus aureus under conditions of high bacterial density. Diagnostic Microbiology and Infectious Disease64: 220–224. doi: 10.1016/j.diagmicrobio.2009.01.02819345040
    • (2009) Diagnostic Microbiology and Infectious Disease , vol.64 , pp. 220-224
    • Tsuji, B.T.1    Harigaya, Y.2    Lesse, A.J.3    Sakoulas, G.4    Mylotte, J.M.5
  • 82
    • 0036237753 scopus 로고    scopus 로고
    • Accessory gene regulator (agr) locus in geographically diverse Staphylococcus aureus isolates with reduced susceptibility to vancomycin
    • 11959587,. ().: –.
    • Sakoulas G, Eliopoulos GM, Moellering RC, Wennersten C, Venkataraman L, et al. (2002) Accessory gene regulator (agr) locus in geographically diverse Staphylococcus aureus isolates with reduced susceptibility to vancomycin. Antimicrobial Agents and Chemotherapy46: 1492–1502. 11959587
    • (2002) Antimicrobial Agents and Chemotherapy , vol.46 , pp. 1492-1502
    • Sakoulas, G.1    Eliopoulos, G.M.2    Moellering, R.C.3    Wennersten, C.4    Venkataraman, L.5
  • 83
    • 77956321151 scopus 로고    scopus 로고
    • Identification of genes involved in polysaccharide-independent Staphylococcus aureus biofilm formation
    • 20418950, ().:.
    • Boles BR, Thoendel M, Roth AJ, Horswill AR, (2010) Identification of genes involved in polysaccharide-independent Staphylococcus aureus biofilm formation. PLoS One5: e10146. doi: 10.1371/journal.pone.001014620418950
    • (2010) PLoS One , vol.5 , pp. e10146
    • Boles, B.R.1    Thoendel, M.2    Roth, A.J.3    Horswill, A.R.4
  • 84
    • 84897411855 scopus 로고    scopus 로고
    • Methionine sulfoxide reductases protect against oxidative stress in Staphylococcus aureus encountering exogenous oxidants and human neutrophils
    • 24247266,. ().: –.
    • Pang YY, Schwartz J, Bloomberg S, Boyd JM, Horswill AR, et al. (2014) Methionine sulfoxide reductases protect against oxidative stress in Staphylococcus aureus encountering exogenous oxidants and human neutrophils. J Innate Immun6: 353–364. doi: 10.1159/00035591524247266
    • (2014) J Innate Immun , vol.6 , pp. 353-364
    • Pang, Y.Y.1    Schwartz, J.2    Bloomberg, S.3    Boyd, J.M.4    Horswill, A.R.5
  • 86
    • 0000721718 scopus 로고
    • Analysis by Transduction of Mutations Affecting Penicillinase Formation in Staphylococcus Aureus
    • 14072829, ().: –.
    • Novick RP, (1963) Analysis by Transduction of Mutations Affecting Penicillinase Formation in Staphylococcus Aureus. J Gen Microbiol33: 121–136. 14072829
    • (1963) J Gen Microbiol , vol.33 , pp. 121-136
    • Novick, R.P.1
  • 87
    • 84944909980 scopus 로고    scopus 로고
    • De Novo Assembly of Plasmids Using Yeast Recombinational Cloning
    • 26194707,.: –.
    • Mashruwala AA, Boyd JM, De Novo Assembly of Plasmids Using Yeast Recombinational Cloning. Methods Mol Biol1373: 33–41. doi: 10.1007/7651_2015_27526194707
    • Methods Mol Biol , vol.1373 , pp. 33-41
    • Mashruwala, A.A.1    Boyd, J.M.2
  • 88
    • 84896293907 scopus 로고    scopus 로고
    • A universal cloning method based on yeast homologous recombination that is simple, efficient, and versatile
    • 24418681, ().: –.
    • Joska TM, Mashruwala A, Boyd JM, Belden WJ, (2014) A universal cloning method based on yeast homologous recombination that is simple, efficient, and versatile. J Microbiol Methods100: 46–51. doi: 10.1016/j.mimet.2013.11.01324418681
    • (2014) J Microbiol Methods , vol.100 , pp. 46-51
    • Joska, T.M.1    Mashruwala, A.2    Boyd, J.M.3    Belden, W.J.4
  • 89
    • 34249822802 scopus 로고    scopus 로고
    • Anaerobic gene expression in Staphylococcus aureus
    • 17384184, ().: –.
    • Fuchs S, Pane-Farre J, Kohler C, Hecker M, Engelmann S, (2007) Anaerobic gene expression in Staphylococcus aureus. J Bacteriol189: 4275–4289. 17384184
    • (2007) J Bacteriol , vol.189 , pp. 4275-4289
    • Fuchs, S.1    Pane-Farre, J.2    Kohler, C.3    Hecker, M.4    Engelmann, S.5
  • 90
    • 35648960309 scopus 로고    scopus 로고
    • Inhibition of staphylococcal biofilm formation by nitrite
    • 17720780, ().: –.
    • Schlag S, Nerz C, Birkenstock TA, Altenberend F, Gotz F, (2007) Inhibition of staphylococcal biofilm formation by nitrite. J Bacteriol189: 7911–7919. 17720780
    • (2007) J Bacteriol , vol.189 , pp. 7911-7919
    • Schlag, S.1    Nerz, C.2    Birkenstock, T.A.3    Altenberend, F.4    Gotz, F.5
  • 91
    • 56449093155 scopus 로고    scopus 로고
    • Reactions of synthetic [2Fe-2S] and [4Fe-4S] clusters with nitric oxide and nitrosothiols
    • 18939795, ().: –.
    • Harrop TC, Tonzetich ZJ, Reisner E, Lippard SJ, (2008) Reactions of synthetic [2Fe-2S] and [4Fe-4S] clusters with nitric oxide and nitrosothiols. J Am Chem Soc130: 15602–15610. doi: 10.1021/ja805499618939795
    • (2008) J Am Chem Soc , vol.130 , pp. 15602-15610
    • Harrop, T.C.1    Tonzetich, Z.J.2    Reisner, E.3    Lippard, S.J.4
  • 92
    • 78650602342 scopus 로고    scopus 로고
    • Characterization of iron dinitrosyl species formed in the reaction of nitric oxide with a biological Rieske center
    • 21133361,.: –.
    • Tinberg CE, Tonzetich ZJ, Wang H, Do LH, Yoda Y, et al. Characterization of iron dinitrosyl species formed in the reaction of nitric oxide with a biological Rieske center. J Am Chem Soc132: 18168–18176. doi: 10.1021/ja106290p21133361
    • J Am Chem Soc , vol.132 , pp. 18168-18176
    • Tinberg, C.E.1    Tonzetich, Z.J.2    Wang, H.3    Do, L.H.4    Yoda, Y.5
  • 94
    • 48649097049 scopus 로고    scopus 로고
    • Bacterial ApbC can bind and effectively transfer iron-sulfur clusters
    • 18616280, ().: –.
    • Boyd JM, Pierik AJ, Netz DJ, Lill R, Downs DM, (2008) Bacterial ApbC can bind and effectively transfer iron-sulfur clusters. Biochemistry47: 8195–8202. doi: 10.1021/bi800551y18616280
    • (2008) Biochemistry , vol.47 , pp. 8195-8202
    • Boyd, J.M.1    Pierik, A.J.2    Netz, D.J.3    Lill, R.4    Downs, D.M.5
  • 95
    • 41049100518 scopus 로고
    • A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase
    • 14938361, ().: –.
    • Beers RF, Jr.Sizer IW, (1952) A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase. J Biol Chem195: 133–140. 14938361
    • (1952) J Biol Chem , vol.195 , pp. 133-140
    • Beers, R.F.1    Sizer, I.W.2
  • 96
    • 0014691242 scopus 로고
    • Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)
    • 5389100, ().: –.
    • McCord JM, Fridovich I, (1969) Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem244: 6049–6055. 5389100
    • (1969) J Biol Chem , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 97
    • 63149097265 scopus 로고    scopus 로고
    • Interconnections between Sigma B, agr, and proteolytic activity in Staphylococcus aureus biofilm maturation
    • 19188357, ().: –.
    • Lauderdale KJ, Boles BR, Cheung AL, Horswill AR, (2009) Interconnections between Sigma B, agr, and proteolytic activity in Staphylococcus aureus biofilm maturation. Infect Immun77: 1623–1635. doi: 10.1128/IAI.01036-0819188357
    • (2009) Infect Immun , vol.77 , pp. 1623-1635
    • Lauderdale, K.J.1    Boles, B.R.2    Cheung, A.L.3    Horswill, A.R.4
  • 98
    • 84864461105 scopus 로고    scopus 로고
    • Contribution of the Staphylococcus aureus Atl AM and GL murein hydrolase activities in cell division, autolysis, and biofilm formation
    • 22860095,.:.
    • Bose JL, Lehman MK, Fey PD, Bayles KW, Contribution of the Staphylococcus aureus Atl AM and GL murein hydrolase activities in cell division, autolysis, and biofilm formation. PLoS One7: e42244. doi: 10.1371/journal.pone.004224422860095
    • PLoS One , vol.7 , pp. e42244
    • Bose, J.L.1    Lehman, M.K.2    Fey, P.D.3    Bayles, K.W.4
  • 99
    • 0037805576 scopus 로고    scopus 로고
    • The KEGG database
    • 12539951, ().: –; discussion 101–103, 119–128, 244–152.
    • Kanehisa M, (2002) The KEGG database. Novartis Found Symp247: 91–101; discussion 101–103, 119–128, 244–152. 12539951
    • (2002) Novartis Found Symp , vol.247 , pp. 91-101
    • Kanehisa, M.1
  • 100
    • 54049108449 scopus 로고    scopus 로고
    • Multiple sequence alignment using ClustalW and ClustalX
    • 18792934, ().:.
    • Thompson JD, Gibson TJ, Higgins DG, (2002) Multiple sequence alignment using ClustalW and ClustalX. Curr Protoc BioinformaticsChapter 2: Unit 2 3. doi: 10.1002/0471250953.bi0203s0018792934
    • (2002) Curr Protoc Bioinformatics , vol.Chapter 2 , pp. Unit 2 3
    • Thompson, J.D.1    Gibson, T.J.2    Higgins, D.G.3
  • 101
    • 68049139485 scopus 로고    scopus 로고
    • Estimating maximum likelihood phylogenies with PhyML
    • 19378142, ().: –.
    • Guindon S, Delsuc F, Dufayard JF, Gascuel O, (2009) Estimating maximum likelihood phylogenies with PhyML. Methods Mol Biol537: 113–137. doi: 10.1007/978-1-59745-251-9_619378142
    • (2009) Methods Mol Biol , vol.537 , pp. 113-137
    • Guindon, S.1    Delsuc, F.2    Dufayard, J.F.3    Gascuel, O.4
  • 102
    • 33845873289 scopus 로고    scopus 로고
    • Interactive Tree Of Life (iTOL): an online tool for phylogenetic tree display and annotation
    • 17050570, ().: –.
    • Letunic I, Bork P, (2007) Interactive Tree Of Life (iTOL): an online tool for phylogenetic tree display and annotation. Bioinformatics23: 127–128. 17050570
    • (2007) Bioinformatics , vol.23 , pp. 127-128
    • Letunic, I.1    Bork, P.2
  • 103
    • 78651285748 scopus 로고    scopus 로고
    • CDD: a Conserved Domain Database for the functional annotation of proteins
    • 21109532,.: –.
    • Marchler-Bauer A, Lu S, Anderson JB, Chitsaz F, Derbyshire MK, et al. CDD: a Conserved Domain Database for the functional annotation of proteins. Nucleic Acids Res39: D225–229. doi: 10.1093/nar/gkq118921109532
    • Nucleic Acids Res , vol.39 , pp. D225-229
    • Marchler-Bauer, A.1    Lu, S.2    Anderson, J.B.3    Chitsaz, F.4    Derbyshire, M.K.5
  • 104
    • 0020610320 scopus 로고
    • The toxic shock syndrome exotoxin structural gene is not detectably transmitted by a prophage
    • 6226876,. ().: –.
    • Kreiswirth BN, Lofdahl S, Betley MJ, O'Reilly M, Schlievert PM, et al. (1983) The toxic shock syndrome exotoxin structural gene is not detectably transmitted by a prophage. Nature305: 709–712. 6226876
    • (1983) Nature , vol.305 , pp. 709-712
    • Kreiswirth, B.N.1    Lofdahl, S.2    Betley, M.J.3    O'Reilly, M.4    Schlievert, P.M.5
  • 105
    • 84874638650 scopus 로고    scopus 로고
    • A genetic resource for rapid and comprehensive phenotype screening of nonessential Staphylococcus aureus genes
    • 23404398,. ().: –.
    • Fey PD, Endres JL, Yajjala VK, Widhelm TJ, Boissy RJ, et al. (2013) A genetic resource for rapid and comprehensive phenotype screening of nonessential Staphylococcus aureus genes. MBio4: e00537–00512. doi: 10.1128/mBio.00537-1223404398
    • (2013) MBio , vol.4 , pp. e00512-e00537
    • Fey, P.D.1    Endres, J.L.2    Yajjala, V.K.3    Widhelm, T.J.4    Boissy, R.J.5
  • 106
    • 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
    • 11133939, ().: –.
    • Horsburgh MJ, Ingham E, Foster SJ, (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 Bacteriol183: 468–475. 11133939
    • (2001) J Bacteriol , vol.183 , pp. 468-475
    • Horsburgh, M.J.1    Ingham, E.2    Foster, S.J.3
  • 107
    • 77749279738 scopus 로고    scopus 로고
    • Tricarboxylic acid cycle-dependent synthesis of Staphylococcus aureus Type 5 and 8 capsular polysaccharides
    • 20061474,. ().: –.
    • Sadykov MR, Mattes TA, Luong TT, Zhu Y, Day SR, et al. (2010) Tricarboxylic acid cycle-dependent synthesis of Staphylococcus aureus Type 5 and 8 capsular polysaccharides. J Bacteriol192: 1459–1462. doi: 10.1128/JB.01377-0920061474
    • (2010) J Bacteriol , vol.192 , pp. 1459-1462
    • Sadykov, M.R.1    Mattes, T.A.2    Luong, T.T.3    Zhu, Y.4    Day, S.R.5
  • 108
    • 84874596495 scopus 로고    scopus 로고
    • Genetic tools to enhance the study of gene function and regulation in Staphylococcus aureus
    • 23354696, ().: –.
    • Bose JL, Fey PD, Bayles KW, (2013) Genetic tools to enhance the study of gene function and regulation in Staphylococcus aureus. Appl Environ Microbiol79: 2218–2224. doi: 10.1128/AEM.00136-1323354696
    • (2013) Appl Environ Microbiol , vol.79 , pp. 2218-2224
    • Bose, J.L.1    Fey, P.D.2    Bayles, K.W.3
  • 110
    • 34250768844 scopus 로고    scopus 로고
    • Improved single-copy integration vectors for Staphylococcus aureus
    • 17512993, ().: –.
    • Luong TT, Lee CY, (2007) Improved single-copy integration vectors for Staphylococcus aureus. J Microbiol Methods70: 186–190. 17512993
    • (2007) J Microbiol Methods , vol.70 , pp. 186-190
    • Luong, T.T.1    Lee, C.Y.2
  • 111
    • 0036271625 scopus 로고    scopus 로고
    • A genome-wide strategy for the identification of essential genes in Staphylococcus aureus
    • 11952893,. ().: –.
    • Forsyth RA, Haselbeck RJ, Ohlsen KL, Yamamoto RT, Xu H, et al. (2002) A genome-wide strategy for the identification of essential genes in Staphylococcus aureus. Mol Microbiol43: 1387–1400. 11952893
    • (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
  • 112
    • 0029590029 scopus 로고
    • Antibiotic-resistance cassettes for Bacillus subtilis
    • 8566804, ().: –.
    • Guerout-Fleury AM, Shazand K, Frandsen N, Stragier P, (1995) Antibiotic-resistance cassettes for Bacillus subtilis. Gene167: 335–336. 8566804
    • (1995) Gene , vol.167 , pp. 335-336
    • Guerout-Fleury, A.M.1    Shazand, K.2    Frandsen, N.3    Stragier, P.4


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