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Volumn 94, Issue 6, 2014, Pages 1343-1360

The CsoR-like sulfurtransferase repressor (CstR) is a persulfide sensor in Staphylococcus aureus

Author keywords

[No Author keywords available]

Indexed keywords

COPPER ION; COPPER SENSING OPERON REPRESSOR LIKE SULFURTRANSFERASE REPRESSOR; CYSTINE; GLUTATHIONE DISULFIDE; HYDROGEN SULFIDE; ORGANIC PERSULFIDE; ORGANOSULFUR DERIVATIVE; PERSULFIDE; REPRESSOR PROTEIN; SULFIDE; SULFUR; THIOSULFATE; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; COPPER; CULTURE MEDIUM; PERSULFIDES;

EID: 84915735116     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/mmi.12835     Document Type: Article
Times cited : (96)

References (61)
  • 1
    • 29144482705 scopus 로고    scopus 로고
    • Allelic replacement in Staphylococcus aureus with inducible counter-selection
    • Bae, T., and Schneewind, O. (2006) Allelic replacement in Staphylococcus aureus with inducible counter-selection. Plasmid 55: 58-63.
    • (2006) Plasmid , vol.55 , pp. 58-63
    • Bae, T.1    Schneewind, O.2
  • 2
    • 84905281134 scopus 로고    scopus 로고
    • Understanding hydrogen sulfide storage: probing conditions for sulfide release from hydrodisulfides
    • Bailey, T.S., Zakharov, L.N., and Pluth, M.D. (2014) Understanding hydrogen sulfide storage: probing conditions for sulfide release from hydrodisulfides. J Am Chem Soc 136: 10573-10576.
    • (2014) J Am Chem Soc , vol.136 , pp. 10573-10576
    • Bailey, T.S.1    Zakharov, L.N.2    Pluth, M.D.3
  • 3
    • 33750479893 scopus 로고    scopus 로고
    • Involvement of nitric oxide in biofilm dispersal of Pseudomonas aeruginosa
    • Barraud, N., Hassett, D.J., Hwang, S.H., Rice, S.A., Kjelleberg, S., and Webb, J.S. (2006) Involvement of nitric oxide in biofilm dispersal of Pseudomonas aeruginosa. J Bacteriol 188: 7344-7353.
    • (2006) J Bacteriol , vol.188 , pp. 7344-7353
    • Barraud, N.1    Hassett, D.J.2    Hwang, S.H.3    Rice, S.A.4    Kjelleberg, S.5    Webb, J.S.6
  • 4
    • 84919781393 scopus 로고    scopus 로고
    • Nitric oxide: a key mediator of biofilm dispersal with applications in infectious diseases
    • Barraud, N., Kelso, M.J., Rice, S.A., and Kjelleberg, S. (2014) Nitric oxide: a key mediator of biofilm dispersal with applications in infectious diseases. Curr Pharm Des. doi: 10.2174/1381612820666140905112822.
    • (2014) Curr Pharm Des
    • Barraud, N.1    Kelso, M.J.2    Rice, S.A.3    Kjelleberg, S.4
  • 5
    • 33748783783 scopus 로고    scopus 로고
    • Host defenses against Staphylococcus aureus infection require recognition of bacterial lipoproteins
    • Bubeck Wardenburg, J., Williams, W.A., and Missiakas, D. (2006) Host defenses against Staphylococcus aureus infection require recognition of bacterial lipoproteins. Proc Natl Acad Sci USA 103: 13831-13836.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 13831-13836
    • Bubeck Wardenburg, J.1    Williams, W.A.2    Missiakas, D.3
  • 6
    • 84903822857 scopus 로고    scopus 로고
    • Cu(I)-mediated allosteric switching in a copper-sensing operon repressor (CsoR)
    • Chang, F.M., Coyne, H.J., Ramirez, C.A., Fleischmann, P.V., Fang, X., Ma, Z., etal. (2014) Cu(I)-mediated allosteric switching in a copper-sensing operon repressor (CsoR). J Biol Chem 289: 19204-19217.
    • (2014) J Biol Chem , vol.289 , pp. 19204-19217
    • Chang, F.M.1    Coyne, H.J.2    Ramirez, C.A.3    Fleischmann, P.V.4    Fang, X.5    Ma, Z.6
  • 7
    • 35948992186 scopus 로고    scopus 로고
    • Toxicogenomic response to chlorination includes induction of major virulence genes in Staphylococcus aureus
    • Chang, M.W., Toghrol, F., and Bentley, W.E. (2007) Toxicogenomic response to chlorination includes induction of major virulence genes in Staphylococcus aureus. Environ Sci Technol 41: 7570-7575.
    • (2007) Environ Sci Technol , vol.41 , pp. 7570-7575
    • Chang, M.W.1    Toghrol, F.2    Bentley, W.E.3
  • 8
    • 66449109703 scopus 로고    scopus 로고
    • 2S biogenesis by human cystathionine γ-lyase leads to the novel sulfur metabolites lanthionine and homolanthionine and is responsive to the grade of hyperhomocysteinemia
    • 2S biogenesis by human cystathionine γ-lyase leads to the novel sulfur metabolites lanthionine and homolanthionine and is responsive to the grade of hyperhomocysteinemia. J Biol Chem 284: 11601-11612.
    • (2009) J Biol Chem , vol.284 , pp. 11601-11612
    • Chiku, T.1    Padovani, D.2    Zhu, W.3    Singh, S.4    Vitvitsky, V.5    Banerjee, R.6
  • 9
    • 34047225116 scopus 로고    scopus 로고
    • Common themes and variations in the rhodanese superfamily
    • Cipollone, R., Ascenzi, P., and Visca, P. (2007) Common themes and variations in the rhodanese superfamily. IUBMB Life 59: 51-59.
    • (2007) IUBMB Life , vol.59 , pp. 51-59
    • Cipollone, R.1    Ascenzi, P.2    Visca, P.3
  • 10
    • 84862803226 scopus 로고    scopus 로고
    • Identification and characterization of a bacterial hydrosulphide ion channel
    • Czyzewski, B.K., and Wang, D.N. (2012) Identification and characterization of a bacterial hydrosulphide ion channel. Nature 483: 494-497.
    • (2012) Nature , vol.483 , pp. 494-497
    • Czyzewski, B.K.1    Wang, D.N.2
  • 11
    • 84874322079 scopus 로고    scopus 로고
    • The sulfur carrier protein TusA has a pleiotropic role in Escherichia coli that also affects molybdenum cofactor biosynthesis
    • Dahl, J.-U., Radon, C., Bühning, M., Nimtz, M., Leichert, L.I., Denis, Y., etal. (2013) The sulfur carrier protein TusA has a pleiotropic role in Escherichia coli that also affects molybdenum cofactor biosynthesis. J Biol Chem 288: 5426-5442.
    • (2013) J Biol Chem , vol.288 , pp. 5426-5442
    • Dahl, J.-U.1    Radon, C.2    Bühning, M.3    Nimtz, M.4    Leichert, L.I.5    Denis, Y.6
  • 12
    • 80053905923 scopus 로고    scopus 로고
    • The identification of a novel protein involved in molybdenum cofactor biosynthesis in Escherichia coli
    • Dahl, J.U., Urban, A., Bolte, A., Sriyabhaya, P., Donahue, J.L., Nimtz, M., etal. (2011) The identification of a novel protein involved in molybdenum cofactor biosynthesis in Escherichia coli. J Biol Chem 286: 35801-35812.
    • (2011) J Biol Chem , vol.286 , pp. 35801-35812
    • Dahl, J.U.1    Urban, A.2    Bolte, A.3    Sriyabhaya, P.4    Donahue, J.L.5    Nimtz, M.6
  • 13
    • 10044219806 scopus 로고    scopus 로고
    • First evidence of the oxidation and regeneration of polysulfides at a GaAs electrode, under anodic conditions. A study by in situ UV-visible spectroelectrochemistry
    • Debiemme-Chouvy, C., Wartelle, C., and Sauvage, F.-X. (2004) First evidence of the oxidation and regeneration of polysulfides at a GaAs electrode, under anodic conditions. A study by in situ UV-visible spectroelectrochemistry. J Phys Chem B 108: 18291-18296.
    • (2004) J Phys Chem B , vol.108 , pp. 18291-18296
    • Debiemme-Chouvy, C.1    Wartelle, C.2    Sauvage, F.-X.3
  • 14
    • 34548571932 scopus 로고    scopus 로고
    • Unbiased identification of cysteine S-nitrosylation sites on proteins
    • Derakhshan, B., Wille, P.C., and Gross, S.S. (2007) Unbiased identification of cysteine S-nitrosylation sites on proteins. Nat Protoc 2: 1685-1691.
    • (2007) Nat Protoc , vol.2 , pp. 1685-1691
    • Derakhshan, B.1    Wille, P.C.2    Gross, S.S.3
  • 15
    • 84861206687 scopus 로고    scopus 로고
    • Response to copper stress in Streptomyces lividans extends beyond genes under direct control of a copper-sensitive operon repressor protein (CsoR)
    • Dwarakanath, S., Chaplin, A.K., Hough, M.A., Rigali, S., Vijgenboom, E., and Worrall, J.A. (2012) Response to copper stress in Streptomyces lividans extends beyond genes under direct control of a copper-sensitive operon repressor protein (CsoR). J Biol Chem 287: 17833-17847.
    • (2012) J Biol Chem , vol.287 , pp. 17833-17847
    • Dwarakanath, S.1    Chaplin, A.K.2    Hough, M.A.3    Rigali, S.4    Vijgenboom, E.5    Worrall, J.A.6
  • 16
    • 84904490728 scopus 로고    scopus 로고
    • H2S and NO cooperatively regulate vascular tone by activating a neuroendocrine HNO-TRPA1-CGRP signalling pathway
    • Eberhardt, M., Dux, M., Namer, B., Miljkovic, J., Cordasic, N., Will, C., etal. (2014) H2S and NO cooperatively regulate vascular tone by activating a neuroendocrine HNO-TRPA1-CGRP signalling pathway. Nat Commun 5: 4381.
    • (2014) Nat Commun , vol.5 , pp. 4381
    • Eberhardt, M.1    Dux, M.2    Namer, B.3    Miljkovic, J.4    Cordasic, N.5    Will, C.6
  • 17
    • 0023084955 scopus 로고
    • Determination of low-molecular-weight thiols using monobromobimane fluorescent labeling and high-performance liquid chromatography
    • Fahey, R.C., and Newton, G.L. (1987) Determination of low-molecular-weight thiols using monobromobimane fluorescent labeling and high-performance liquid chromatography. Methods Enzymol 143: 85-96.
    • (1987) Methods Enzymol , vol.143 , pp. 85-96
    • Fahey, R.C.1    Newton, G.L.2
  • 20
    • 84874104763 scopus 로고    scopus 로고
    • A new structural paradigm in copper resistance in Streptococcus pneumoniae
    • Fu, Y., Tsui, H.C., Bruce, K.E., Sham, L.T., Higgins, K.A., Lisher, J.P., etal. (2013) A new structural paradigm in copper resistance in Streptococcus pneumoniae. Nat Chem Biol 9: 177-183.
    • (2013) Nat Chem Biol , vol.9 , pp. 177-183
    • Fu, Y.1    Tsui, H.C.2    Bruce, K.E.3    Sham, L.T.4    Higgins, K.A.5    Lisher, J.P.6
  • 21
    • 84881517255 scopus 로고    scopus 로고
    • Aureolib - a proteome signature library: towards an understanding of Staphylococcus aureus pathophysiology
    • Fuchs, S., Zuhlke, D., Pane-Farre, J., Kusch, H., Wolf, C., Reiss, S., etal. (2013) Aureolib - a proteome signature library: towards an understanding of Staphylococcus aureus pathophysiology. PLoS ONE 8: e70669.
    • (2013) PLoS ONE , vol.8 , pp. e70669
    • Fuchs, S.1    Zuhlke, D.2    Pane-Farre, J.3    Kusch, H.4    Wolf, C.5    Reiss, S.6
  • 23
    • 79953892242 scopus 로고    scopus 로고
    • Control of copper resistance and inorganic sulfur metabolism by paralogous regulators in Staphylococcus aureus
    • Grossoehme, N., Kehl-Fie, T.E., Ma, Z., Adams, K.W., Cowart, D.M., Scott, R.A., etal. (2011) Control of copper resistance and inorganic sulfur metabolism by paralogous regulators in Staphylococcus aureus. J Biol Chem 286: 13522-13531.
    • (2011) J Biol Chem , vol.286 , pp. 13522-13531
    • Grossoehme, N.1    Kehl-Fie, T.E.2    Ma, Z.3    Adams, K.W.4    Cowart, D.M.5    Scott, R.A.6
  • 24
    • 79960423857 scopus 로고    scopus 로고
    • Plant pathogenic bacteria utilize biofilm growth-associated repressor (BigR), a novel winged-helix redox switch, to control hydrogen sulfide detoxification under hypoxia
    • Guimaraes, B.G., Barbosa, R.L., Soprano, A.S., Campos, B.M., de Souza, T.A., Tonoli, C.C., etal. (2011) Plant pathogenic bacteria utilize biofilm growth-associated repressor (BigR), a novel winged-helix redox switch, to control hydrogen sulfide detoxification under hypoxia. J Biol Chem 286: 26148-26157.
    • (2011) J Biol Chem , vol.286 , pp. 26148-26157
    • Guimaraes, B.G.1    Barbosa, R.L.2    Soprano, A.S.3    Campos, B.M.4    de Souza, T.A.5    Tonoli, C.C.6
  • 25
    • 84891810747 scopus 로고    scopus 로고
    • Insights into protein allostery in the CsoR/RcnR Family of transcriptional repressors
    • Higgins, K.A., and Giedroc, D. (2014) Insights into protein allostery in the CsoR/RcnR Family of transcriptional repressors. Chem Lett 43: 20-25.
    • (2014) Chem Lett , vol.43 , pp. 20-25
    • Higgins, K.A.1    Giedroc, D.2
  • 26
    • 44949214775 scopus 로고    scopus 로고
    • Three enzymatic activities catalyze the oxidation of sulfide to thiosulfate in mammalian and invertebrate mitochondria
    • Hildebrandt, T.M., and Grieshaber, M.K. (2008) Three enzymatic activities catalyze the oxidation of sulfide to thiosulfate in mammalian and invertebrate mitochondria. FEBS J 275: 3352-3361.
    • (2008) FEBS J , vol.275 , pp. 3352-3361
    • Hildebrandt, T.M.1    Grieshaber, M.K.2
  • 27
    • 84881530220 scopus 로고    scopus 로고
    • Proteome adaptations in Ethe1-deficient mice indicate a role in lipid catabolism and cytoskeleton organization via post-translational protein modifications
    • Hildebrandt, T.M., Di Meo, I., Zeviani, M., Viscomi, C., and Braun, H.P. (2013) Proteome adaptations in Ethe1-deficient mice indicate a role in lipid catabolism and cytoskeleton organization via post-translational protein modifications. Biosci Rep 33: e00052.
    • (2013) Biosci Rep , vol.33 , pp. e00052
    • Hildebrandt, T.M.1    Di Meo, I.2    Zeviani, M.3    Viscomi, C.4    Braun, H.P.5
  • 28
    • 47249088762 scopus 로고    scopus 로고
    • Nitric oxide stress induces different responses but mediates comparable protein thiol protection in Bacillus subtilis and Staphylococcus aureus
    • Hochgräfe, F., Wolf, C., Fuchs, S., Liebeke, M., Lalk, M., Engelmann, S., etal. (2008) Nitric oxide stress induces different responses but mediates comparable protein thiol protection in Bacillus subtilis and Staphylococcus aureus. J Bacteriol 190: 4997-5008.
    • (2008) J Bacteriol , vol.190 , pp. 4997-5008
    • Hochgräfe, F.1    Wolf, C.2    Fuchs, S.3    Liebeke, M.4    Lalk, M.5    Engelmann, S.6
  • 29
    • 48849106057 scopus 로고    scopus 로고
    • Spectroscopic studies on Arabidopsis ETHE1, a glyoxalase II-like protein
    • Holdorf, M.M., Bennett, B., Crowder, M.W., and Markaroff, C.A. (2008) Spectroscopic studies on Arabidopsis ETHE1, a glyoxalase II-like protein. J Inorg Biochem 102: 1825-1830.
    • (2008) J Inorg Biochem , vol.102 , pp. 1825-1830
    • Holdorf, M.M.1    Bennett, B.2    Crowder, M.W.3    Markaroff, C.A.4
  • 30
    • 0025975149 scopus 로고
    • A chemically defined medium for slime production by coagulase-negative staphylococci
    • Hussain, M., Hastings, J.G.M., and White, P.J. (1991) A chemically defined medium for slime production by coagulase-negative staphylococci. J Med Microbiol 34: 143-147.
    • (1991) J Med Microbiol , vol.34 , pp. 143-147
    • Hussain, M.1    Hastings, J.G.M.2    White, P.J.3
  • 31
    • 84901659489 scopus 로고    scopus 로고
    • Reactive cysteine persulfides and S-polythiolation regulate oxidative stress and redox signaling
    • Ida, T., Sawa, T., Ihara, H., Tsuchiya, Y., Watanabe, Y., Kumagai, Y., etal. (2014) Reactive cysteine persulfides and S-polythiolation regulate oxidative stress and redox signaling. Proc Natl Acad Sci USA 111: 7606-7611.
    • (2014) Proc Natl Acad Sci USA , vol.111 , pp. 7606-7611
    • Ida, T.1    Sawa, T.2    Ihara, H.3    Tsuchiya, Y.4    Watanabe, Y.5    Kumagai, Y.6
  • 32
    • 29544452864 scopus 로고    scopus 로고
    • Mechanistic insights into sulfur relay by multiple sulfur mediators involved in thiouridine biosynthesis at tRNA wobble positions
    • Ikeuchi, Y., Shigi, N., Kato, J., Nishimura, A., and Suzuki, T. (2006) Mechanistic insights into sulfur relay by multiple sulfur mediators involved in thiouridine biosynthesis at tRNA wobble positions. Mol Cell 21: 97-108.
    • (2006) Mol Cell , vol.21 , pp. 97-108
    • Ikeuchi, Y.1    Shigi, N.2    Kato, J.3    Nishimura, A.4    Suzuki, T.5
  • 33
    • 77954579286 scopus 로고    scopus 로고
    • Redox biochemistry of hydrogen sulfide
    • Kabil, O., and Banerjee, R. (2010) Redox biochemistry of hydrogen sulfide. J Biol Chem 285: 21903-21907.
    • (2010) J Biol Chem , vol.285 , pp. 21903-21907
    • Kabil, O.1    Banerjee, R.2
  • 34
    • 84902255282 scopus 로고    scopus 로고
    • HS and its role in redox signaling
    • Kabil, O., Motl, N., and Banerjee, R. (2014) HS and its role in redox signaling. Biochim Biophys Acta 1844: 1355-1366.
    • (2014) Biochim Biophys Acta , vol.1844 , pp. 1355-1366
    • Kabil, O.1    Motl, N.2    Banerjee, R.3
  • 35
    • 33947297662 scopus 로고
    • Cyanolysis and spectrophotometric estimation of trithionate in mixture with thiosulfate and tetrathionate
    • Kelly, D.P., Chambers, L.A., and Trudinger, P.A. (1969) Cyanolysis and spectrophotometric estimation of trithionate in mixture with thiosulfate and tetrathionate. Anal Chem 41: 898-901.
    • (1969) Anal Chem , vol.41 , pp. 898-901
    • Kelly, D.P.1    Chambers, L.A.2    Trudinger, P.A.3
  • 36
    • 77950851571 scopus 로고    scopus 로고
    • Hydrogen sulfide: from brain to gut
    • Kimura, H. (2010) Hydrogen sulfide: from brain to gut. Antioxid Redox Signal 12: 1111-1123.
    • (2010) Antioxid Redox Signal , vol.12 , pp. 1111-1123
    • Kimura, H.1
  • 37
    • 84881191992 scopus 로고    scopus 로고
    • Hydrogen sulfide chemical biology: pathophysiological roles and detection
    • Kolluru, G.K., Shen, X., Bir, S.C., and Kevil, C.G. (2013) Hydrogen sulfide chemical biology: pathophysiological roles and detection. Nitric Oxide 35: 5-20.
    • (2013) Nitric Oxide , vol.35 , pp. 5-20
    • Kolluru, G.K.1    Shen, X.2    Bir, S.C.3    Kevil, C.G.4
  • 38
    • 0029902679 scopus 로고    scopus 로고
    • Program DYNAFIT for the analysis of enzyme kinetic data: application to HIV proteinase
    • Kuzmic, P. (1996) Program DYNAFIT for the analysis of enzyme kinetic data: application to HIV proteinase. Anal Biochem 237: 260-273.
    • (1996) Anal Biochem , vol.237 , pp. 260-273
    • Kuzmic, P.1
  • 39
    • 33845736364 scopus 로고    scopus 로고
    • CsoR is a novel Mycobacterium tuberculosis copper-sensing transcriptional regulator
    • Liu, T., Ramesh, A., Ma, Z., Ward, S.K., Zhang, L., George, G.N., etal. (2007) CsoR is a novel Mycobacterium tuberculosis copper-sensing transcriptional regulator. Nat Chem Biol 3: 60-68.
    • (2007) Nat Chem Biol , vol.3 , pp. 60-68
    • Liu, T.1    Ramesh, A.2    Ma, Z.3    Ward, S.K.4    Zhang, L.5    George, G.N.6
  • 40
    • 84879565056 scopus 로고    scopus 로고
    • Selenite and tellurite form mixed seleno- and tellurotrisulfides with CstR from Staphylococcus aureus
    • Luebke, J.L., Arnold, R.J., and Giedroc, D.P. (2013) Selenite and tellurite form mixed seleno- and tellurotrisulfides with CstR from Staphylococcus aureus. Metallomics 5: 335-342.
    • (2013) Metallomics , vol.5 , pp. 335-342
    • Luebke, J.L.1    Arnold, R.J.2    Giedroc, D.P.3
  • 41
    • 65249102750 scopus 로고    scopus 로고
    • Molecular insights into the metal selectivity of the copper(I)-sensing repressor CsoR from Bacillus subtilis
    • Ma, Z., Cowart, D.M., Scott, R.A., and Giedroc, D.P. (2009a) Molecular insights into the metal selectivity of the copper(I)-sensing repressor CsoR from Bacillus subtilis. Biochemistry 48: 3325-3334.
    • (2009) Biochemistry , vol.48 , pp. 3325-3334
    • Ma, Z.1    Cowart, D.M.2    Scott, R.A.3    Giedroc, D.P.4
  • 42
    • 72449153406 scopus 로고    scopus 로고
    • Unnatural amino acid substitution as a probe of the allosteric coupling pathway in a mycobacterial Cu(I) sensor
    • Ma, Z., Cowart, D.M., Ward, B.P., Arnold, R.J., DiMarchi, R.D., Zhang, L., etal. (2009b) Unnatural amino acid substitution as a probe of the allosteric coupling pathway in a mycobacterial Cu(I) sensor. J Am Chem Soc 131: 18044-18045.
    • (2009) J Am Chem Soc , vol.131 , pp. 18044-18045
    • Ma, Z.1    Cowart, D.M.2    Ward, B.P.3    Arnold, R.J.4    DiMarchi, R.D.5    Zhang, L.6
  • 43
    • 67649872642 scopus 로고    scopus 로고
    • The structure of Aquifex aeolicus sulfide:quinone oxidoreductase, a basis to understand sulfide detoxification and respiration
    • Marcia, M., Ermler, U., Peng, G., and Michel, H. (2009) The structure of Aquifex aeolicus sulfide:quinone oxidoreductase, a basis to understand sulfide detoxification and respiration. Proc Natl Acad Sci USA 106: 9625-9630.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 9625-9630
    • Marcia, M.1    Ermler, U.2    Peng, G.3    Michel, H.4
  • 44
    • 33646349748 scopus 로고    scopus 로고
    • Trafficking in persulfides: delivering sulfur in biosynthetic pathways
    • Mueller, E.G. (2006) Trafficking in persulfides: delivering sulfur in biosynthetic pathways. Nat Chem Biol 2: 185-194.
    • (2006) Nat Chem Biol , vol.2 , pp. 185-194
    • Mueller, E.G.1
  • 45
    • 9244225687 scopus 로고    scopus 로고
    • Distribution of thiols in microorganisms: mycothiol is a major thiol in most actinomycetes
    • Newton, G.L., Arnold, K., Price, M.S., Sherrill, C., Delcardayre, S.B., Aharonowitz, Y., etal. (1996) Distribution of thiols in microorganisms: mycothiol is a major thiol in most actinomycetes. J Bacteriol 178: 1990-1995.
    • (1996) J Bacteriol , vol.178 , pp. 1990-1995
    • Newton, G.L.1    Arnold, K.2    Price, M.S.3    Sherrill, C.4    Delcardayre, S.B.5    Aharonowitz, Y.6
  • 46
    • 84879776406 scopus 로고    scopus 로고
    • Persulfide reactivity in the detection of protein S-sulfhydration
    • Pan, J., and Carroll, K.S. (2013) Persulfide reactivity in the detection of protein S-sulfhydration. ACS Chem Biol 8: 1110-1116.
    • (2013) ACS Chem Biol , vol.8 , pp. 1110-1116
    • Pan, J.1    Carroll, K.S.2
  • 47
    • 84864285556 scopus 로고    scopus 로고
    • 2S signalling through protein sulfhydration and beyond
    • 2S signalling through protein sulfhydration and beyond. Nat Rev Mol Cell Biol 13: 499-507.
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 499-507
    • Paul, B.D.1    Snyder, S.H.2
  • 48
    • 72449174430 scopus 로고    scopus 로고
    • Diamide triggers mainly S-thiolations in the cytoplasmic proteomes of Bacillus subtilis and Staphylococcus aureus
    • Pother, D.C., Liebeke, M., Hochgrafe, F., Antelmann, H., Becher, D., Lalk, M., etal. (2009) Diamide triggers mainly S-thiolations in the cytoplasmic proteomes of Bacillus subtilis and Staphylococcus aureus. J Bacteriol 191: 7520-7530.
    • (2009) J Bacteriol , vol.191 , pp. 7520-7530
    • Pother, D.C.1    Liebeke, M.2    Hochgrafe, F.3    Antelmann, H.4    Becher, D.5    Lalk, M.6
  • 49
    • 79956065205 scopus 로고    scopus 로고
    • Metalloregulatory proteins: metal selectivity and allosteric switching
    • Reyes-Caballero, H., Campanello, G.C., and Giedroc, D.P. (2011) Metalloregulatory proteins: metal selectivity and allosteric switching. Biophys Chem 156: 103-114.
    • (2011) Biophys Chem , vol.156 , pp. 103-114
    • Reyes-Caballero, H.1    Campanello, G.C.2    Giedroc, D.P.3
  • 51
    • 84860176878 scopus 로고    scopus 로고
    • Endogenous protein S-nitrosylation in E. coli: regulation by OxyR
    • Seth, D., Hausladen, A., Wang, Y.J., and Stamler, J.S. (2012) Endogenous protein S-nitrosylation in E. coli: regulation by OxyR. Science 336: 470-473.
    • (2012) Science , vol.336 , pp. 470-473
    • Seth, D.1    Hausladen, A.2    Wang, Y.J.3    Stamler, J.S.4
  • 54
    • 67650462310 scopus 로고    scopus 로고
    • CymR, the master regulator of cysteine metabolism in Staphylococcus aureus, controls host sulphur source utilization and plays a role in biofilm formation
    • Soutourina, O., Poupel, O., Coppee, J.Y., Danchin, A., Msadek, T., and Martin-Verstraete, I. (2009) CymR, the master regulator of cysteine metabolism in Staphylococcus aureus, controls host sulphur source utilization and plays a role in biofilm formation. Mol Microbiol 73: 194-211.
    • (2009) Mol Microbiol , vol.73 , pp. 194-211
    • Soutourina, O.1    Poupel, O.2    Coppee, J.Y.3    Danchin, A.4    Msadek, T.5    Martin-Verstraete, I.6
  • 55
    • 58149089691 scopus 로고    scopus 로고
    • The CymR regulator in complex with the enzyme CysK controls cysteine metabolism in Bacillus subtilis
    • Tanous, C., Soutourina, O., Raynal, B., Hullo, M.F., Mervelet, P., Gilles, A.M., etal. (2008) The CymR regulator in complex with the enzyme CysK controls cysteine metabolism in Bacillus subtilis. J Biol Chem 283: 35551-35560.
    • (2008) J Biol Chem , vol.283 , pp. 35551-35560
    • Tanous, C.1    Soutourina, O.2    Raynal, B.3    Hullo, M.F.4    Mervelet, P.5    Gilles, A.M.6
  • 56
    • 59649121556 scopus 로고    scopus 로고
    • Loss of ETHE1, a mitochondrial dioxygenase, causes fatal sulfide toxicity in ethylmalonic encephalopathy
    • Tiranti, V., Viscomi, C., Hildebrandt, T., Di Meo, I., Mineri, R., Tiveron, C., etal. (2009) Loss of ETHE1, a mitochondrial dioxygenase, causes fatal sulfide toxicity in ethylmalonic encephalopathy. Nat Med 15: 200-205.
    • (2009) Nat Med , vol.15 , pp. 200-205
    • Tiranti, V.1    Viscomi, C.2    Hildebrandt, T.3    Di Meo, I.4    Mineri, R.5    Tiveron, C.6
  • 57
    • 22544456543 scopus 로고    scopus 로고
    • Staphylococcus aureus develops an alternative, ica-independent biofilm in the absence of the arlRS two-component system
    • Toledo-Arana, A., Merino, N., Vergara-Irigaray, M., Debarbouille, M., Penades, J.R., and Lasa, I. (2005) Staphylococcus aureus develops an alternative, ica-independent biofilm in the absence of the arlRS two-component system. J Bacteriol 187: 5318-5329.
    • (2005) J Bacteriol , vol.187 , pp. 5318-5329
    • Toledo-Arana, A.1    Merino, N.2    Vergara-Irigaray, M.3    Debarbouille, M.4    Penades, J.R.5    Lasa, I.6
  • 59
    • 49749101196 scopus 로고    scopus 로고
    • Proteomic analysis of antioxidant strategies of Staphylococcus aureus: diverse responses to different oxidants
    • Wolf, C., Hochgräfe, F., Kusch, H., Albrecht, D., Hecker, M., and Engelmann, S. (2008) Proteomic analysis of antioxidant strategies of Staphylococcus aureus: diverse responses to different oxidants. Proteomics 8: 3139-3153.
    • (2008) Proteomics , vol.8 , pp. 3139-3153
    • Wolf, C.1    Hochgräfe, F.2    Kusch, H.3    Albrecht, D.4    Hecker, M.5    Engelmann, S.6
  • 60
    • 79953211568 scopus 로고    scopus 로고
    • Unification of the copper(I) binding affinities of the metallo-chaperones Atx1, Atox1, and related proteins: detection probes and affinity standards
    • Xiao, Z., Brose, J., Schimo, S., Ackland, S.M., La Fontaine, S., and Wedd, A.G. (2011) Unification of the copper(I) binding affinities of the metallo-chaperones Atx1, Atox1, and related proteins: detection probes and affinity standards. J Biol Chem 286: 11047-11055.
    • (2011) J Biol Chem , vol.286 , pp. 11047-11055
    • Xiao, Z.1    Brose, J.2    Schimo, S.3    Ackland, S.M.4    La Fontaine, S.5    Wedd, A.G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.