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Volumn 197, Issue 5, 2015, Pages 794-806

The staphylococcus aureus nuoL-like protein MpsA contributes to the generation of membrane potential

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; NUOL LIKE PROTEIN MPSA; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (QUINONE); REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); UNCLASSIFIED DRUG; ESCHERICHIA COLI PROTEIN; NUOL PROTEIN, E COLI; OXYGEN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; SODIUM;

EID: 84922118690     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.02127-14     Document Type: Article
Times cited : (31)

References (75)
  • 1
    • 36949083936 scopus 로고
    • Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism
    • Mitchell P. 1961. Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism. Nature 191:144-148. http://dx.doi.org/10.1038/191144a0.
    • (1961) Nature , vol.191 , pp. 144-148
    • Mitchell, P.1
  • 2
    • 50649102939 scopus 로고    scopus 로고
    • The genera Staphylococcus and Macrococcus
    • Dworkin M(ed), Springer, New York, NY.
    • Götz F, Bannerman T, Schleifer KH. 2006. The genera Staphylococcus and Macrococcus, p 5-75. In DworkinM(ed), Procaryotes, vol 4. Springer, New York, NY.
    • (2006) Procaryotes , vol.4 , pp. 5-75
    • Götz, F.1    Bannerman, T.2    Schleifer, K.H.3
  • 3
    • 0033973454 scopus 로고    scopus 로고
    • Crucial role of the membrane potential for ATP synthesis by F(1)F(o) ATP synthases
    • Dimroth P, Kaim G, Matthey U. 2000. Crucial role of the membrane potential for ATP synthesis by F(1)F(o) ATP synthases. J Exp Biol 203:51-59.
    • (2000) J Exp Biol , vol.203 , pp. 51-59
    • Dimroth, P.1    Kaim, G.2    Matthey, U.3
  • 4
    • 0026484793 scopus 로고
    • Conservation of sequences of subunits of mitochondrial complex I and their relationships with other proteins
    • Fearnley IM, Walker JE. 1992. Conservation of sequences of subunits of mitochondrial complex I and their relationships with other proteins. Biochim Biophys Acta 1140:105-134. http://dx.doi.org/10.1016/0005 -2728(92)90001-I.
    • (1992) Biochim Biophys Acta , vol.1140 , pp. 105-134
    • Fearnley, I.M.1    Walker, J.E.2
  • 5
    • 0025752593 scopus 로고
    • Bacterial NADH-quinone oxidoreductases
    • Yagi T. 1991. Bacterial NADH-quinone oxidoreductases. J Bioenerg Biomembr 23:211-225. http://dx.doi.org/10.1007/BF00762218.
    • (1991) J Bioenerg Biomembr , vol.23 , pp. 211-225
    • Yagi, T.1
  • 7
    • 33746329868 scopus 로고    scopus 로고
    • Energy converting NADH:quinone oxidoreductase (complex I)
    • Brandt U. 2006. Energy converting NADH:quinone oxidoreductase (complex I). Annu Rev Biochem 75:69-92. http://dx.doi.org/10.1146 /annurev.biochem.75.103004.142539.
    • (2006) Annu Rev Biochem , vol.75 , pp. 69-92
    • Brandt, U.1
  • 8
    • 0027104114 scopus 로고
    • The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains
    • Walker JE. 1992. The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains. Q Rev Biophys 25:253-324. http://dx.doi.org/10.1017 /S003358350000425X.
    • (1992) Q Rev Biophys , vol.25 , pp. 253-324
    • Walker, J.E.1
  • 9
    • 0037418550 scopus 로고    scopus 로고
    • The proton-translocating NADHquinone oxidoreductase in the respiratory chain: the secret unlocked
    • Yagi T, Matsuno-Yagi A. 2003. The proton-translocating NADHquinone oxidoreductase in the respiratory chain: the secret unlocked. Biochemistry 42:2266-2274. http://dx.doi.org/10.1021/bi027158b.
    • (2003) Biochemistry , vol.42 , pp. 2266-2274
    • Yagi, T.1    Matsuno-Yagi, A.2
  • 10
    • 66449105882 scopus 로고    scopus 로고
    • Architecture of complex I and its implications for electron transfer and proton pumping
    • Zickermann V, Kerscher S, Zwicker K, Tocilescu MA, Radermacher M, Brandt U. 2009. Architecture of complex I and its implications for electron transfer and proton pumping. Biochim Biophys Acta 1787:574-583. http://dx.doi.org/10.1016/j.bbabio.2009.01.012.
    • (2009) Biochim Biophys Acta , vol.1787 , pp. 574-583
    • Zickermann, V.1    Kerscher, S.2    Zwicker, K.3    Tocilescu, M.A.4    Radermacher, M.5    Brandt, U.6
  • 11
    • 0033955767 scopus 로고    scopus 로고
    • + translocation by complex I (NADH:quinone oxidoreductase) of Escherichia coli
    • + translocation by complex I (NADH:quinone oxidoreductase) of Escherichia coli. Mol Microbiol 35:428-434. http://dx.doi.org/10.1046/j.1365-2958.2000 .01712.x.
    • (2000) Mol Microbiol , vol.35 , pp. 428-434
    • Steuber, J.1    Schmid, C.2    Rufibach, M.3    Dimroth, P.4
  • 12
    • 84884614877 scopus 로고    scopus 로고
    • Cation transport by the respiratory NADH: quinone oxidoreductase (complex I): facts and hypotheses
    • Steffen W, Steuber J. 2013. Cation transport by the respiratory NADH: quinone oxidoreductase (complex I): facts and hypotheses. Biochem Soc Trans 41:1280-1287. http://dx.doi.org/10.1042/BST20130024.
    • (2013) Biochem Soc Trans , vol.41 , pp. 1280-1287
    • Steffen, W.1    Steuber, J.2
  • 13
    • 1842737600 scopus 로고    scopus 로고
    • The origin of the sodium-dependent NADH oxidation by the respiratory chain of Klebsiella pneumoniae
    • Bertsova YV, Bogachev AV. 2004. The origin of the sodium-dependent NADH oxidation by the respiratory chain of Klebsiella pneumoniae. FEBS Lett 563:207-212. http://dx.doi.org/10.1016/S0014-5793(04)00312-6.
    • (2004) FEBS Lett , vol.563 , pp. 207-212
    • Bertsova, Y.V.1    Bogachev, A.V.2
  • 15
    • 84864664396 scopus 로고    scopus 로고
    • +-pumping NADH:quinone oxidoreductase
    • +-pumping NADH:quinone oxidoreductase. Biochim Biophys Acta 1817:1823-1832. http://dx.doi.org /10.1016/j.bbabio.2012.03.017.
    • (2012) Biochim Biophys Acta , vol.1817 , pp. 1823-1832
    • Juárez, O.1    Barquera, B.2
  • 16
    • 77953799863 scopus 로고    scopus 로고
    • Sodium-translocating NADH: quinone oxidoreductase as a redox-driven ion pump
    • Verkhovsky MI, Bogachev AV. 2010. Sodium-translocating NADH: quinone oxidoreductase as a redox-driven ion pump. Biochim Biophys Acta 1797:738-746. http://dx.doi.org/10.1016/j.bbabio.2009.12.020.
    • (2010) Biochim Biophys Acta , vol.1797 , pp. 738-746
    • Verkhovsky, M.I.1    Bogachev, A.V.2
  • 17
    • 84922143729 scopus 로고    scopus 로고
    • +-translocating NADH:quinone oxidoreductase (Na+-NQR) in sodium bioenergetics of Vibrio cholerae
    • +-translocating NADH:quinone oxidoreductase (Na+-NQR) in sodium bioenergetics of Vibrio cholerae. Biol Chem 395: 1389-1399. http://dx.doi.org/10.1515/hsz-2014-0204.
    • (2014) Biol Chem , vol.395 , pp. 1389-1399
    • Steuber, J.1    Halang, P.2    Vorburger, T.3    Steffen, W.4    Vohl, G.5    Fritz, G.6
  • 18
    • 0037072803 scopus 로고    scopus 로고
    • The respiratory complex I (NDH I) from Klebsiella pneumoniae, a sodium pump
    • Gemperli AC, Dimroth P, Steuber J. 2002. The respiratory complex I (NDH I) from Klebsiella pneumoniae, a sodium pump. J Biol Chem 277: 33811-33817. http://dx.doi.org/10.1074/jbc.M204860200.
    • (2002) J Biol Chem , vol.277
    • Gemperli, A.C.1    Dimroth, P.2    Steuber, J.3
  • 19
  • 20
    • 10344231976 scopus 로고    scopus 로고
    • New insights into type II NAD(P)H:quinone oxidoreductases
    • Melo AM, Bandeiras TM, Teixeira M. 2004. New insights into type II NAD(P)H:quinone oxidoreductases. Microbiol Mol Biol Rev 68:603-616. http://dx.doi.org/10.1128/MMBR.68.4.603-616.2004.
    • (2004) Microbiol Mol Biol Rev , vol.68 , pp. 603-616
    • Melo, A.M.1    Bandeiras, T.M.2    Teixeira, M.3
  • 21
    • 0019490792 scopus 로고
    • Distribution of isoprenoid quinone structural types in bacteria and their taxonomic implication
    • Collins MD, Jones D. 1981. Distribution of isoprenoid quinone structural types in bacteria and their taxonomic implication. Microbiol Rev 45:316-354.
    • (1981) Microbiol Rev , vol.45 , pp. 316-354
    • Collins, M.D.1    Jones, D.2
  • 22
    • 77951059306 scopus 로고    scopus 로고
    • Advantage of upregulation of succinate dehydrogenase in Staphylococcus aureus biofilms
    • Gaupp R, Schlag S, Liebeke M, Lalk M, Götz F. 2010. Advantage of upregulation of succinate dehydrogenase in Staphylococcus aureus biofilms. J Bacteriol 192:2385-2394. http://dx.doi.org/10.1128/JB.01472-09.
    • (2010) J Bacteriol , vol.192 , pp. 2385-2394
    • Gaupp, R.1    Schlag, S.2    Liebeke, M.3    Lalk, M.4    Götz, F.5
  • 24
    • 0014593756 scopus 로고
    • Multiple forms of lactate dehydrogenase in Staphylococcus aureus
    • Stockland AE, San Clemente CL. 1969. Multiple forms of lactate dehydrogenase in Staphylococcus aureus. J Bacteriol 100:347-353.
    • (1969) J Bacteriol , vol.100 , pp. 347-353
    • Stockland, A.E.1    San Clemente, C.L.2
  • 25
    • 0019472432 scopus 로고
    • Modified oxidase and benzidine tests for separation of staphylococci from micrococci
    • Faller A, Schleifer KH. 1981. Modified oxidase and benzidine tests for separation of staphylococci from micrococci. J Clin Microbiol 13:1031- 1035.
    • (1981) J Clin Microbiol , vol.13 , pp. 1031- 1035
    • Faller, A.1    Schleifer, K.H.2
  • 26
    • 0019271384 scopus 로고
    • Cytochrome patterns of staphylococci and micrococci and their taxonomic implications
    • Faller AH, Götz F, Schleifer KH. 1980. Cytochrome patterns of staphylococci and micrococci and their taxonomic implications. Zentralbl Bakteriol Hyg Abt 1 Orig C 1:26-39.
    • (1980) Zentralbl Bakteriol Hyg Abt 1 Orig C , vol.1 , pp. 26-39
    • Faller, A.H.1    Götz, F.2    Schleifer, K.H.3
  • 27
    • 0037990786 scopus 로고    scopus 로고
    • Biogenesis of respiratory cytochromes in bacteria
    • Thöny-Meyer L. 1997. Biogenesis of respiratory cytochromes in bacteria. Microbiol Mol Biol Rev 61:337-376.
    • (1997) Microbiol Mol Biol Rev , vol.61 , pp. 337-376
    • Thöny-Meyer, L.1
  • 28
    • 0032899044 scopus 로고    scopus 로고
    • CtaA of Staphylococcus aureus is required for starvation survival, recovery, and cytochrome biosynthesis
    • Clements MO, Watson SP, Poole RK, Foster SJ. 1999. CtaA of Staphylococcus aureus is required for starvation survival, recovery, and cytochrome biosynthesis. J Bacteriol 181:501-507.
    • (1999) J Bacteriol , vol.181 , pp. 501-507
    • Clements, M.O.1    Watson, S.P.2    Poole, R.K.3    Foster, S.J.4
  • 29
    • 84883316268 scopus 로고    scopus 로고
    • Two heme-dependent terminal oxidases power Staphylococcus aureus organ-specific colonization of the vertebrate host
    • Hammer ND, Reniere ML, Cassat JE, Zhang Y, Hirsch AO, Indriati Hood M, Skaar EP. 2013. Two heme-dependent terminal oxidases power Staphylococcus aureus organ-specific colonization of the vertebrate host. mBio 4(4):e00241-13. http://dx.doi.org/10.1128/mBio.00241-13.
    • (2013) mBio , vol.4 , Issue.4
    • Hammer, N.D.1    Reniere, M.L.2    Cassat, J.E.3    Zhang, Y.4    Hirsch, A.O.5    Indriati Hood, M.6    Skaar, E.P.7
  • 30
    • 33751585830 scopus 로고    scopus 로고
    • Microevolution of cytochrome bd oxidase in staphylococci and its implication in resistance to respiratory toxins released by Pseudomonas
    • Voggu L, Schlag S, Biswas R, Rosenstein R, Rausch C, Götz F. 2006. Microevolution of cytochrome bd oxidase in staphylococci and its implication in resistance to respiratory toxins released by Pseudomonas. J Bacteriol 188:8079-8086. http://dx.doi.org/10.1128/JB.00858-06.
    • (2006) J Bacteriol , vol.188 , pp. 8079-8086
    • Voggu, L.1    Schlag, S.2    Biswas, R.3    Rosenstein, R.4    Rausch, C.5    Götz, F.6
  • 31
    • 0030764901 scopus 로고    scopus 로고
    • Aerobic regulation of cytochrome d oxidase (cydAB) operon expression in Escherichia coli: roles of Fnr and ArcA in repression and activation
    • Cotter PA, Melville SB, Albrecht JA, Gunsalus RP. 1997. Aerobic regulation of cytochrome d oxidase (cydAB) operon expression in Escherichia coli: roles of Fnr and ArcA in repression and activation. Mol Microbiol 25:605-615. http://dx.doi.org/10.1046/j.1365-2958.1997.5031860.x.
    • (1997) Mol Microbiol , vol.25 , pp. 605-615
    • Cotter, P.A.1    Melville, S.B.2    Albrecht, J.A.3    Gunsalus, R.P.4
  • 32
    • 0032415869 scopus 로고    scopus 로고
    • Cytochrome bd biosynthesis in Bacillus subtilis: characterization of the cydABCD operon
    • Winstedt L, Yoshida K, Fujita Y, von Wachenfeldt C. 1998. Cytochrome bd biosynthesis in Bacillus subtilis: characterization of the cydABCD operon. J Bacteriol 180:6571-6580.
    • (1998) J Bacteriol , vol.180 , pp. 6571-6580
    • Winstedt, L.1    Yoshida, K.2    Fujita, Y.3    von Wachenfeldt, C.4
  • 33
    • 0004510881 scopus 로고
    • Electron transport in staphylococci: properties of a particle preparation from exponential phase Staphylococcus aureus
    • Taber HW, Morrison M. 1964. Electron transport in staphylococci: properties of a particle preparation from exponential phase Staphylococcus aureus. Arch Biochem Biophys 105:367-379. http://dx.doi.org/10.1016/0003 -9861(64)90021-9.
    • (1964) Arch Biochem Biophys , vol.105 , pp. 367-379
    • Taber, H.W.1    Morrison, M.2
  • 34
    • 0014185038 scopus 로고
    • Membrane lipid changes during formation of a functional electron transport system in Staphylococcus aureus
    • Frerman FE, White DC. 1967. Membrane lipid changes during formation of a functional electron transport system in Staphylococcus aureus. J Bacteriol 94:1868-1874.
    • (1967) J Bacteriol , vol.94 , pp. 1868-1874
    • Frerman, F.E.1    White, D.C.2
  • 35
    • 0025326656 scopus 로고
    • Branched respiratory chain in aerobically grown Staphylococcus aureus-oxidation of ethanol by cells and protoplasts
    • Artzatbanov VY, Petrov VV. 1990. Branched respiratory chain in aerobically grown Staphylococcus aureus-oxidation of ethanol by cells and protoplasts. Arch Microbiol 153:580 -584. http://dx.doi.org/10.1007 /BF00245268.
    • (1990) Arch Microbiol , vol.153 , pp. 580 -584
    • Artzatbanov, V.Y.1    Petrov, V.V.2
  • 36
    • 84891604619 scopus 로고    scopus 로고
    • Both terminal oxidases contribute to fitness and virulence during organ-specific Staphylococcus aureus colonization
    • Götz F, Mayer S. 2013. Both terminal oxidases contribute to fitness and virulence during organ-specific Staphylococcus aureus colonization. mBio 4(6):e00976 -13. http://dx.doi.org/10.1128/mBio.00976-13.
    • (2013) mBio , vol.4 , Issue.6
    • Götz, F.1    Mayer, S.2
  • 38
    • 0037010862 scopus 로고    scopus 로고
    • Transmembrane topology of the NuoL, M and N subunits of NADH:quinone oxidoreductase and their homologues among membrane-bound hydrogenases and bona fide antiporters
    • Mathiesen C, Hagerhall C. 2002. Transmembrane topology of the NuoL, M and N subunits of NADH:quinone oxidoreductase and their homologues among membrane-bound hydrogenases and bona fide antiporters. Biochim Biophys Acta 1556:121-132. http://dx.doi.org/10.1016/S0005 -2728(02)00343-2.
    • (2002) Biochim Biophys Acta , vol.1556 , pp. 121-132
    • Mathiesen, C.1    Hagerhall, C.2
  • 39
    • 33644890219 scopus 로고    scopus 로고
    • Transposon disruption of the complex I NADH oxidoreductase gene (snoD) in Staphylococcus aureus is associated with reduced susceptibility to the microbicidal activity of thrombininduced platelet microbicidal protein 1
    • Bayer AS, McNamara P, Yeaman MR, Lucindo N, Jones T, Cheung AL, Sahl HG, Proctor RA. 2006. Transposon disruption of the complex I NADH oxidoreductase gene (snoD) in Staphylococcus aureus is associated with reduced susceptibility to the microbicidal activity of thrombininduced platelet microbicidal protein 1. J Bacteriol 188:211-222. http://dx .doi.org/10.1128/JB.188.1.211-222.2006.
    • (2006) J Bacteriol , vol.188 , pp. 211-222
    • Bayer, A.S.1    McNamara, P.2    Yeaman, M.R.3    Lucindo, N.4    Jones, T.5    Cheung, A.L.6    Sahl, H.G.7    Proctor, R.A.8
  • 40
    • 34247874630 scopus 로고    scopus 로고
    • Catalytic properties of Staphylococcus aureus and Bacillus members of the secondary cation/proton antiporter-3 (Mrp) family are revealed by an optimized assay in an Escherichia coli host
    • Swartz TH, Ito M, Ohira T, Natsui S, Hicks DB, Krulwich TA. 2007. Catalytic properties of Staphylococcus aureus and Bacillus members of the secondary cation/proton antiporter-3 (Mrp) family are revealed by an optimized assay in an Escherichia coli host. J Bacteriol 189:3081-3090. http://dx.doi.org/10.1128/JB.00021-07.
    • (2007) J Bacteriol , vol.189 , pp. 3081-3090
    • Swartz, T.H.1    Ito, M.2    Ohira, T.3    Natsui, S.4    Hicks, D.B.5    Krulwich, T.A.6
  • 41
    • 77649311467 scopus 로고    scopus 로고
    • A novel fed-batch based cultivation method provides high cell-density and improves yield of soluble recombinant proteins in shaken cultures
    • Krause M, Ukkonen K, Haataja T, Ruottinen M, Glumoff T, Neubauer A, Neubauer P, Vasala A. 2010. A novel fed-batch based cultivation method provides high cell-density and improves yield of soluble recombinant proteins in shaken cultures. Microb Cell Fact 9:11. http://dx.doi .org/10.1186/1475-2859-9-11.
    • (2010) Microb Cell Fact , vol.9 , pp. 11
    • Krause, M.1    Ukkonen, K.2    Haataja, T.3    Ruottinen, M.4    Glumoff, T.5    Neubauer, A.6    Neubauer, P.7    Vasala, A.8
  • 42
    • 29144482705 scopus 로고    scopus 로고
    • Allelic replacement in Staphylococcus aureus with inducible counter-selection
    • Bae T, Schneewind O. 2005. Allelic replacement in Staphylococcus aureus with inducible counter-selection. Plasmid 55:58-63. http://dx.doi.org/10 .1016/j.plasmid.2005.05.005.
    • (2005) Plasmid , vol.55 , pp. 58-63
    • Bae, T.1    Schneewind, O.2
  • 43
    • 0025079412 scopus 로고
    • Transformation of Staphylococcus epidermidis and other staphylococcal species with plasmid DNA by electroporation
    • Augustin J, Götz F. 1990. Transformation of Staphylococcus epidermidis and other staphylococcal species with plasmid DNA by electroporation. FEMS Microbiol Lett 54:203-207.
    • (1990) FEMS Microbiol Lett , vol.54 , pp. 203-207
    • Augustin, J.1    Götz, F.2
  • 44
    • 0026495787 scopus 로고
    • A series of shuttle vectors for Bacillus subtilis and Escherichiacoli.
    • Brückner R. 1992. A series of shuttle vectors for Bacillus subtilis and Escherichiacoli.Gene122:187-192.http://dx.doi.org/10.1016/0378-1119 (92)90048-T.
    • (1992) Gene , vol.122 , pp. 187-192
    • Brückner, R.1
  • 45
    • 84860524445 scopus 로고    scopus 로고
    • Transforming the untransformable: application of direct transformation to manipulate genetically Staphylococcus aureus and Staphylococcus epidermidis
    • Monk IR, Shah IM, Xu M, Tan MW, Foster TJ. 2012. Transforming the untransformable: application of direct transformation to manipulate genetically Staphylococcus aureus and Staphylococcus epidermidis. mBio 3(2):e00277-11. http://dx.doi.org/10.1128/mBio.00277-11.
    • (2012) mBio , vol.3 , Issue.2
    • Monk, I.R.1    Shah, I.M.2    Xu, M.3    Tan, M.W.4    Foster, T.J.5
  • 48
    • 0002051540 scopus 로고    scopus 로고
    • BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT
    • Hall TA. 1999. BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT. Nucleic Acids Symp Ser 41:95-98.
    • (1999) Nucleic Acids Symp Ser , vol.41 , pp. 95-98
    • Hall, T.A.1
  • 49
    • 23144452044 scopus 로고    scopus 로고
    • The HHpred interactive server for protein homology detection and structure prediction
    • Söding J, Biegert A, Lupas AN. 2005. The HHpred interactive server for protein homology detection and structure prediction. Nucleic Acids Res 33:W244-W248. http://dx.doi.org/10.1093/nar/gki408.
    • (2005) Nucleic Acids Res , vol.33 , pp. W244-W248
    • Söding, J.1    Biegert, A.2    Lupas, A.N.3
  • 50
    • 80052068980 scopus 로고    scopus 로고
    • Structure of the membrane domain of respiratory complex I
    • Efremov RG, Sazanov LA. 2011. Structure of the membrane domain of respiratory complex I. Nature 476:414-420. http://dx.doi.org/10.1038 /nature10330.
    • (2011) Nature , vol.476 , pp. 414-420
    • Efremov, R.G.1    Sazanov, L.A.2
  • 51
    • 0041744003 scopus 로고    scopus 로고
    • Correlation of acetate catabolism and growth yield in Staphylococcus aureus: implications for host-pathogen interactions
    • Somerville GA, Said-Salim B, Wickman JM, Raffel SJ, Kreiswirth BN, Musser JM. 2003. Correlation of acetate catabolism and growth yield in Staphylococcus aureus: implications for host-pathogen interactions. Infect Immun 71:4724-4732. http://dx.doi.org/10.1128/IAI.71.8.4724-4732.2003.
    • (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    Musser, J.M.6
  • 52
    • 0030872427 scopus 로고    scopus 로고
    • A site-directed Staphylococcus aureus hemB mutant is a small-colony variant which persists intracellularly
    • von Eiff C, Heilmann C, Proctor RA, Woltz C, Peters G, Götz F. 1997. A site-directed Staphylococcus aureus hemB mutant is a small-colony variant which persists intracellularly. J Bacteriol 179:4706-4712.
    • (1997) J Bacteriol , vol.179 , pp. 4706-4712
    • von Eiff, C.1    Heilmann, C.2    Proctor, R.A.3    Woltz, C.4    Peters, G.5    Götz, F.6
  • 53
    • 84874638650 scopus 로고    scopus 로고
    • A genetic resource for rapid and comprehensive phenotype screening of nonessential Staphylococcus aureus genes
    • Fey PD, Endres JL, Yajjala VK, Widhelm TJ, Boissy RJ, Bose JL, Bayles KW. 2013. A genetic resource for rapid and comprehensive phenotype screening of nonessential Staphylococcus aureus genes. mBio 4(1):e00537-12. http://dx.doi.org/10.1128/mBio.00537-12.
    • (2013) mBio , vol.4 , Issue.1
    • 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
  • 54
    • 0020676737 scopus 로고
    • Membrane potential in anaerobically growing Staphylococcus aureus and its relationship to gentamicin uptake
    • Mates SM, Patel L, Kaback HR, Miller MH. 1983. Membrane potential in anaerobically growing Staphylococcus aureus and its relationship to gentamicin uptake. Antimicrob Agents Chemother 23:526-530. http://dx.doi .org/10.1128/AAC.23.4.526.
    • (1983) Antimicrob Agents Chemother , vol.23 , pp. 526-530
    • Mates, S.M.1    Patel, L.2    Kaback, H.R.3    Miller, M.H.4
  • 56
    • 0003711342 scopus 로고
    • Antibiotics: origin, nature, and properties.
    • American Society for Microbiology, Washington, DC.
    • Korzybski T, Kowskyk-Gindifer Z, Kurylowicz W. 1978. Antibiotics: origin, nature, and properties. American Society for Microbiology, Washington, DC.
    • (1978)
    • Korzybski, T.1    Kowskyk-Gindifer, Z.2    Kurylowicz, W.3
  • 58
    • 0023463947 scopus 로고
    • NADH-ubiquinone oxidoreductases of the Escherichia coli aerobic respiratory chain
    • Matsushita K, Ohnishi T, Kaback HR. 1987. NADH-ubiquinone oxidoreductases of the Escherichia coli aerobic respiratory chain. Biochemistry 26:7732-7737. http://dx.doi.org/10.1021/bi00398a029.
    • (1987) Biochemistry , vol.26 , pp. 7732-7737
    • Matsushita, K.1    Ohnishi, T.2    Kaback, H.R.3
  • 59
    • 0034017033 scopus 로고    scopus 로고
    • Staphylococcus aureus small colony variants, electron transport and persistent infections
    • McNamara PJ, Proctor RA. 2000. Staphylococcus aureus small colony variants, electron transport and persistent infections. Int J Antimicrob Agents 14:117-122. http://dx.doi.org/10.1016/S0924-8579(99)00170-3.
    • (2000) Int J Antimicrob Agents , vol.14 , pp. 117-122
    • McNamara, P.J.1    Proctor, R.A.2
  • 60
    • 0031715560 scopus 로고    scopus 로고
    • Small colony variants in staphylococcal infections: diagnostic and therapeutic implications
    • Proctor RA, Peters G. 1998. Small colony variants in staphylococcal infections: diagnostic and therapeutic implications. Clin Infect Dis 27: 419-423. http://dx.doi.org/10.1086/514706.
    • (1998) Clin Infect Dis , vol.27 , pp. 419-423
    • Proctor, R.A.1    Peters, G.2
  • 61
    • 0036840950 scopus 로고    scopus 로고
    • Staphylococcus aureus aconitase inactivation unexpectedly inhibits post-exponential-phase growth and enhances stationary- phase survival
    • Somerville GA, Chaussee MS, Morgan CI, Fitzgerald JR, Dorward DW, Reitzer LJ, Musser JM. 2002. Staphylococcus aureus aconitase inactivation unexpectedly inhibits post-exponential-phase growth and enhances stationary- phase survival. Infect Immun 70:6373-6382. http://dx.doi.org/10 .1128/IAI.70.11.6373-6382.2002.
    • (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    Reitzer, L.J.6    Musser, J.M.7
  • 62
    • 0037046271 scopus 로고    scopus 로고
    • Carbon catabolite repression in bacteria: choice of the carbon source and autoregulatory limitation of sugar utilization
    • Brückner R, Titgemeyer F. 2002. Carbon catabolite repression in bacteria: choice of the carbon source and autoregulatory limitation of sugar utilization. FEMS Microbiol Lett 209:141-148. http://dx.doi.org/10.1111 /j.1574-6968.2002.tb11123.x.
    • (2002) FEMS Microbiol Lett , vol.209 , pp. 141-148
    • Brückner, R.1    Titgemeyer, F.2
  • 63
    • 0029745668 scopus 로고    scopus 로고
    • Catabolite repression mediated by the catabolite control protein CcpA in Staphylococcus xylosus
    • Egeter O, Brückner R. 1996. Catabolite repression mediated by the catabolite control protein CcpA in Staphylococcus xylosus. Mol Microbiol 21:739-749. http://dx.doi.org/10.1046/j.1365-2958.1996.301398.x.
    • (1996) Mol Microbiol , vol.21 , pp. 739-749
    • Egeter, O.1    Brückner, R.2
  • 64
    • 0036198739 scopus 로고    scopus 로고
    • Carbon catabolite repression by the catabolite control protein CcpA in Staphylococcus xylosus
    • Jankovic I, Brückner R. 2002. Carbon catabolite repression by the catabolite control protein CcpA in Staphylococcus xylosus. J Mol Microbiol Biotechnol 4:309-314.
    • (2002) J Mol Microbiol Biotechnol , vol.4 , pp. 309-314
    • Jankovic, I.1    Brückner, R.2
  • 65
    • 84888586216 scopus 로고    scopus 로고
    • Lactose autoinduction with enzymatic glucose release: characterization of the cultivation system in bioreactor
    • Mayer S, Junne S, Ukkonen K, Glazyrina J, Glauche F, Neubauer P, Vasala A. 2014. Lactose autoinduction with enzymatic glucose release: characterization of the cultivation system in bioreactor. Protein Expr Purif 94:67-72. http://dx.doi.org/10.1016/j.pep.2013.10.024.
    • (2014) Protein Expr Purif , vol.94 , pp. 67-72
    • Mayer, S.1    Junne, S.2    Ukkonen, K.3    Glazyrina, J.4    Glauche, F.5    Neubauer, P.6    Vasala, A.7
  • 66
    • 0017208520 scopus 로고
    • Effect of specific growth rate and glucose concentration on growth and glucose metabolism of Escherichia coli K-12
    • Hollywood N, Doelle HW. 1976. Effect of specific growth rate and glucose concentration on growth and glucose metabolism of Escherichia coli K-12. Microbios 17:23-33.
    • (1976) Microbios , vol.17 , pp. 23-33
    • Hollywood, N.1    Doelle, H.W.2
  • 67
    • 0011063907 scopus 로고
    • Quantitative observations on the chemical activity of "resting" Staphylococcus aureus
    • Kendall AI, Friedemann TE, Ishikawa M. 1930. Quantitative observations on the chemical activity of "resting" Staphylococcus aureus. J Infect Dis 47:223-228. http://dx.doi.org/10.1093/infdis/47.3.223.
    • (1930) J Infect Dis , vol.47 , pp. 223-228
    • Kendall, A.I.1    Friedemann, T.E.2    Ishikawa, M.3
  • 68
    • 0011093548 scopus 로고
    • Dismutation of pyruvic acid in Gonococcus and Staphylococcus
    • Krebs HA. 1937. Dismutation of pyruvic acid in Gonococcus and Staphylococcus. Biochem J 31:661-671.
    • (1937) Biochem J , vol.31 , pp. 661-671
    • Krebs, H.A.1
  • 69
    • 0020585526 scopus 로고
    • Roles of ribosomal binding, membrane potential, and electron transport in bacterial uptake of streptomycin and gentamicin
    • Bryan LE, Kwan S. 1983. Roles of ribosomal binding, membrane potential, and electron transport in bacterial uptake of streptomycin and gentamicin. Antimicrob Agents Chemother 23:835-845. http://dx.doi.org/10 .1128/AAC.23.6.835.
    • (1983) Antimicrob Agents Chemother , vol.23 , pp. 835-845
    • Bryan, L.E.1    Kwan, S.2
  • 70
    • 0021337265 scopus 로고
    • Quantitative association between electrical potential across the cytoplasmic membrane and early gentamicin uptake and killing in Staphylococcus aureus
    • Eisenberg ES, Mandel LJ, Kaback HR, Miller MH. 1984. Quantitative association between electrical potential across the cytoplasmic membrane and early gentamicin uptake and killing in Staphylococcus aureus. J Bacteriol 157:863-867.
    • (1984) J Bacteriol , vol.157 , pp. 863-867
    • Eisenberg, E.S.1    Mandel, L.J.2    Kaback, H.R.3    Miller, M.H.4
  • 71
    • 0031926775 scopus 로고    scopus 로고
    • Staphylococcal small colony variants have novel mechanisms for antibiotic resistance
    • Proctor RA, Kahl B, von Eiff C, Vaudaux PE, Lew DP, Peters G. 1998. Staphylococcal small colony variants have novel mechanisms for antibiotic resistance. Clin Infect Dis 27:S68 -S74. http://dx.doi.org/10.1086 /514906.
    • (1998) Clin Infect Dis , vol.27 , pp. S68 -S74
    • Proctor, R.A.1    Kahl, B.2    von Eiff, C.3    Vaudaux, P.E.4    Lew, D.P.5    Peters, G.6
  • 72
    • 0038712412 scopus 로고    scopus 로고
    • +
    • +. J Biol Chem 278:26817-26822. http://dx.doi.org/10.1074/jbc .M301682200.
    • (2003) J Biol Chem , vol.278
    • Steuber, J.1
  • 73
    • 0000182975 scopus 로고
    • XL1-Blue: a high efficiency plasmid transforming recA Escherichia coli strain with beta-galactosidase selection
    • Bullock WO, Fernandez JM, Short JM. 1987. XL1-Blue: a high efficiency plasmid transforming recA Escherichia coli strain with beta-galactosidase selection. Biotechniques 5:376-382.
    • (1987) Biotechniques , vol.5 , pp. 376-382
    • Bullock, W.O.1    Fernandez, J.M.2    Short, J.M.3
  • 74
    • 0017103409 scopus 로고
    • Two restriction and modification systems in Staphylococcus aureus NCTC8325
    • Iordanescu S, Surdeanu M. 1976. Two restriction and modification systems in Staphylococcus aureus NCTC8325. J Gen Microbiol 96:277-281. http://dx.doi.org/10.1099/00221287-96-2-277.
    • (1976) J Gen Microbiol , vol.96 , pp. 277-281
    • Iordanescu, S.1    Surdeanu, M.2
  • 75
    • 77952700194 scopus 로고    scopus 로고
    • Repair of global regulators in Staphylococcus aureus 8325 and comparative analysis with other clinical isolates.
    • Herbert S, Ziebandt AK, Ohlsen K, Schafer T, Hecker M, Albrecht D, Novick R, Götz F. 2010. Repair of global regulators in Staphylococcus aureus 8325 and comparative analysis with other clinical isolates. Infect Immun 78:2877-2889. http://dx.doi.org/10.1128/IAI.00088-10.
    • (2010) Infect Immun , vol.78 , pp. 2877-2889
    • Herbert, S.1    Ziebandt, A.K.2    Ohlsen, K.3    Schafer, T.4    Hecker, M.5    Albrecht, D.6    Novick, R.7    Götz, F.8


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