메뉴 건너뛰기




Volumn 89, Issue 2, 2013, Pages 288-303

Molecular and structural basis of glutathione import in Gram-positive bacteria via GshT and the cystine ABC importer TcyBC of Streptococcus mutans

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; BINDING PROTEIN; CARBOXYLIC ACID; CYSTEINE; GLUTATHIONE; GLUTATHIONE DISULFIDE; GLYCINE; PROTEIN GSHT; PROTEIN TCYBC; SULFUR; UNCLASSIFIED DRUG;

EID: 84880136182     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/mmi.12274     Document Type: Article
Times cited : (37)

References (68)
  • 3
    • 65049090568 scopus 로고    scopus 로고
    • Plasma membrane glutathione transporters and their roles in cell physiology and pathophysiology
    • Ballatori, N., Krance, S.M., Marchan, R., and Hammond, C.L. (2009) Plasma membrane glutathione transporters and their roles in cell physiology and pathophysiology. Mol Aspects Med 30: 13-28.
    • (2009) Mol Aspects Med , vol.30 , pp. 13-28
    • Ballatori, N.1    Krance, S.M.2    Marchan, R.3    Hammond, C.L.4
  • 4
    • 2442715491 scopus 로고    scopus 로고
    • Virulence properties of Streptococcus mutans
    • Banas, J.A. (2004) Virulence properties of Streptococcus mutans. Front Biosci 9: 1267-1277.
    • (2004) Front Biosci , vol.9 , pp. 1267-1277
    • Banas, J.A.1
  • 5
    • 84872769080 scopus 로고    scopus 로고
    • The effects of methionine acquisition and synthesis on Streptococcus pneumoniae growth and virulence
    • Basavanna, S., Chimalapati, S., Maqbool, A., Rubbo, B., Yuste, J., Wilson, R.J., etal. (2013) The effects of methionine acquisition and synthesis on Streptococcus pneumoniae growth and virulence. PloS ONE 8: e49638.
    • (2013) PloS ONE , vol.8
    • Basavanna, S.1    Chimalapati, S.2    Maqbool, A.3    Rubbo, B.4    Yuste, J.5    Wilson, R.J.6
  • 7
    • 0346251029 scopus 로고    scopus 로고
    • Contribution of glutathione peroxidase to the virulence of Streptococcus pyogenes
    • Brenot, A., King, K.Y., Janowiak, B., Griffith, O., and Caparon, M.G. (2004) Contribution of glutathione peroxidase to the virulence of Streptococcus pyogenes. Infect Immun 72: 408-413.
    • (2004) Infect Immun , vol.72 , pp. 408-413
    • Brenot, A.1    King, K.Y.2    Janowiak, B.3    Griffith, O.4    Caparon, M.G.5
  • 8
    • 0016088102 scopus 로고
    • Compounds affecting Streptococcus agalactiae growth in milk
    • Brown, R.W. (1974) Compounds affecting Streptococcus agalactiae growth in milk. J Dairy Sci 57: 797-802.
    • (1974) J Dairy Sci , vol.57 , pp. 797-802
    • Brown, R.W.1
  • 9
    • 84855826252 scopus 로고    scopus 로고
    • Crystal structures of two solute receptors for L-cystine and L-cysteine, respectively, of the human pathogen Neisseria gonorrhoeae
    • Bulut, H., Moniot, S., Licht, A., Scheffel, F., Gathmann, S., Saenger, W., and Schneider, E. (2012) Crystal structures of two solute receptors for L-cystine and L-cysteine, respectively, of the human pathogen Neisseria gonorrhoeae. J Mol Biol 415: 560-572.
    • (2012) J Mol Biol , vol.415 , pp. 560-572
    • Bulut, H.1    Moniot, S.2    Licht, A.3    Scheffel, F.4    Gathmann, S.5    Saenger, W.6    Schneider, E.7
  • 11
    • 82355184471 scopus 로고    scopus 로고
    • Glutathione utilization by Candida albicans requires a functional glutathione degradation (DUG) pathway and OPT7, an unusual member of the oligopeptide transporter family
    • Desai, P.R., Thakur, A., Ganguli, D., Paul, S., Morschhauser, J., and Bachhawat, A.K. (2011) Glutathione utilization by Candida albicans requires a functional glutathione degradation (DUG) pathway and OPT7, an unusual member of the oligopeptide transporter family. J Biol Chem 286: 41183-41194.
    • (2011) J Biol Chem , vol.286 , pp. 41183-41194
    • Desai, P.R.1    Thakur, A.2    Ganguli, D.3    Paul, S.4    Morschhauser, J.5    Bachhawat, A.K.6
  • 12
    • 77956632119 scopus 로고    scopus 로고
    • Canonical and ECF-type ATP-binding cassette importers in prokaryotes: diversity in modular organization and cellular functions
    • Eitinger, T., Rodionov, D.A., Grote, M., and Schneider, E. (2011) Canonical and ECF-type ATP-binding cassette importers in prokaryotes: diversity in modular organization and cellular functions. FEMS Microbiol Rev 35: 3-67.
    • (2011) FEMS Microbiol Rev , vol.35 , pp. 3-67
    • Eitinger, T.1    Rodionov, D.A.2    Grote, M.3    Schneider, E.4
  • 13
    • 0025963834 scopus 로고
    • Glutathione as an endogenous sulphur source in the yeast Saccharomyces cerevisiae
    • Elskens, M.T., Jaspers, C.J., and Penninckx, M.J. (1991) Glutathione as an endogenous sulphur source in the yeast Saccharomyces cerevisiae. J Gen Microbiol 137: 637-644.
    • (1991) J Gen Microbiol , vol.137 , pp. 637-644
    • Elskens, M.T.1    Jaspers, C.J.2    Penninckx, M.J.3
  • 15
    • 84875715041 scopus 로고    scopus 로고
    • Glutathione analogs in prokaryotes
    • Fahey, R.C. (2013) Glutathione analogs in prokaryotes. Biochim Biophys Acta 1830: 3182-3198.
    • (2013) Biochim Biophys Acta , vol.1830 , pp. 3182-3198
    • Fahey, R.C.1
  • 17
    • 33544461370 scopus 로고    scopus 로고
    • The Venus flytrap of periplasmic binding proteins: an ancient protein module present in multiple drug receptors
    • Felder, C.B., Graul, R.C., Lee, A.Y., Merkle, H., and Sadee, W. (1999) The Venus flytrap of periplasmic binding proteins: an ancient protein module present in multiple drug receptors. AAPS PharmSci 1: E2.
    • (1999) AAPS PharmSci , vol.1
    • Felder, C.B.1    Graul, R.C.2    Lee, A.Y.3    Merkle, H.4    Sadee, W.5
  • 18
    • 84867709011 scopus 로고    scopus 로고
    • Glutathione efflux and cell death
    • Franco, R., and Cidlowski, J.A. (2012) Glutathione efflux and cell death. Antioxid Redox Signal 17: 1694-1713.
    • (2012) Antioxid Redox Signal , vol.17 , pp. 1694-1713
    • Franco, R.1    Cidlowski, J.A.2
  • 19
    • 37549023835 scopus 로고    scopus 로고
    • The central role of glutathione in the pathophysiology of human diseases
    • Franco, R., Schoneveld, O.J., Pappa, A., and Panayiotidis, M.I. (2007) The central role of glutathione in the pathophysiology of human diseases. Arch Physiol Biochem 113: 234-258.
    • (2007) Arch Physiol Biochem , vol.113 , pp. 234-258
    • Franco, R.1    Schoneveld, O.J.2    Pappa, A.3    Panayiotidis, M.I.4
  • 20
    • 52049123291 scopus 로고    scopus 로고
    • Do enthalpy and entropy distinguish first in class from best in class?
    • Freire, E. (2008) Do enthalpy and entropy distinguish first in class from best in class? Drug Discov Today 13: 869-874.
    • (2008) Drug Discov Today , vol.13 , pp. 869-874
    • Freire, E.1
  • 21
    • 18944397128 scopus 로고    scopus 로고
    • A multidomain fusion protein in Listeria monocytogenes catalyzes the two primary activities for glutathione biosynthesis
    • Gopal, S., Borovok, I., Ofer, A., Yanku, M., Cohen, G., Goebel, W., etal. (2005) A multidomain fusion protein in Listeria monocytogenes catalyzes the two primary activities for glutathione biosynthesis. J Bacteriol 187: 3839-3847.
    • (2005) J Bacteriol , vol.187 , pp. 3839-3847
    • Gopal, S.1    Borovok, I.2    Ofer, A.3    Yanku, M.4    Cohen, G.5    Goebel, W.6
  • 22
    • 0027360468 scopus 로고
    • Functional exchangeability of the ABC proteins of the periplasmic binding protein-dependent transport systems Ugp and Mal of Escherichia coli
    • Hekstra, D., and Tommassen, J. (1993) Functional exchangeability of the ABC proteins of the periplasmic binding protein-dependent transport systems Ugp and Mal of Escherichia coli. J Bacteriol 175: 6546-6552.
    • (1993) J Bacteriol , vol.175 , pp. 6546-6552
    • Hekstra, D.1    Tommassen, J.2
  • 23
    • 33745861648 scopus 로고    scopus 로고
    • Analysis of glutathione and glutathione disulfide in human saliva using hydrophilic interaction chromatography with mass spectrometry
    • Iwasaki, Y., Hoshi, M., Ito, R., Saito, K., and Nakazawa, H. (2006) Analysis of glutathione and glutathione disulfide in human saliva using hydrophilic interaction chromatography with mass spectrometry. J Chromatogr B Analyt Technol Biomed Life Sci 839: 74-79.
    • (2006) J Chromatogr B Analyt Technol Biomed Life Sci , vol.839 , pp. 74-79
    • Iwasaki, Y.1    Hoshi, M.2    Ito, R.3    Saito, K.4    Nakazawa, H.5
  • 24
    • 15744398210 scopus 로고    scopus 로고
    • Glutathione synthesis in Streptococcus agalactiae. One protein accounts for gamma-glutamylcysteine synthetase and glutathione synthetase activities
    • Janowiak, B.E., and Griffith, O.W. (2005) Glutathione synthesis in Streptococcus agalactiae. One protein accounts for gamma-glutamylcysteine synthetase and glutathione synthetase activities. J Biol Chem 280: 11829-11839.
    • (2005) J Biol Chem , vol.280 , pp. 11829-11839
    • Janowiak, B.E.1    Griffith, O.W.2
  • 25
    • 0033230779 scopus 로고    scopus 로고
    • Export pumps for glutathione S-conjugates
    • Keppler, D. (1999) Export pumps for glutathione S-conjugates. Free Radic Biol Med 27: 985-991.
    • (1999) Free Radic Biol Med , vol.27 , pp. 985-991
    • Keppler, D.1
  • 26
    • 84862794226 scopus 로고    scopus 로고
    • TcyR regulates L-cystine uptake via the TcyABC transporter in Streptococcus mutans
    • Kim, J., Senadheera, D.B., Levesque, C.M., and Cvitkovitch, D.G. (2012) TcyR regulates L-cystine uptake via the TcyABC transporter in Streptococcus mutans. FEMS Microbiol Lett 328: 114-121.
    • (2012) FEMS Microbiol Lett , vol.328 , pp. 114-121
    • Kim, J.1    Senadheera, D.B.2    Levesque, C.M.3    Cvitkovitch, D.G.4
  • 27
    • 35648957713 scopus 로고    scopus 로고
    • Involvement of the detoxifying enzyme lactoylglutathione lyase in Streptococcus mutans aciduricity
    • Korithoski, B., Levesque, C.M., and Cvitkovitch, D.G. (2007) Involvement of the detoxifying enzyme lactoylglutathione lyase in Streptococcus mutans aciduricity. J Bacteriol 189: 7586-7592.
    • (2007) J Bacteriol , vol.189 , pp. 7586-7592
    • Korithoski, B.1    Levesque, C.M.2    Cvitkovitch, D.G.3
  • 29
    • 16344382388 scopus 로고    scopus 로고
    • Thermodynamic stability of carbonic anhydrase: measurements of binding affinity and stoichiometry using ThermoFluor
    • Matulis, D., Kranz, J.K., Salemme, F.R., and Todd, M.J. (2005) Thermodynamic stability of carbonic anhydrase: measurements of binding affinity and stoichiometry using ThermoFluor. Biochemistry 44: 5258-5266.
    • (2005) Biochemistry , vol.44 , pp. 5258-5266
    • Matulis, D.1    Kranz, J.K.2    Salemme, F.R.3    Todd, M.J.4
  • 30
    • 34347400474 scopus 로고    scopus 로고
    • The oligopeptide (opp) gene cluster of Streptococcus mutans: identification, prevalence, and characterization
    • Nepomuceno, R.S., Tavares, M.B., Lemos, J.A., Griswold, A.R., Ribeiro, J.L., Balan, A., etal. (2007) The oligopeptide (opp) gene cluster of Streptococcus mutans: identification, prevalence, and characterization. Oral Microbiol Immunol 22: 277-284.
    • (2007) Oral Microbiol Immunol , vol.22 , pp. 277-284
    • Nepomuceno, R.S.1    Tavares, M.B.2    Lemos, J.A.3    Griswold, A.R.4    Ribeiro, J.L.5    Balan, A.6
  • 31
    • 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
  • 32
    • 0028067178 scopus 로고
    • The bacterial periplasmic histidine-binding protein. structure/function analysis of the ligand-binding site and comparison with related proteins
    • Oh, B.H., Kang, C.H., De Bondt, H., Kim, S.H., Nikaido, K., Joshi, A.K., and Ames, G.F. (1994) The bacterial periplasmic histidine-binding protein. structure/function analysis of the ligand-binding site and comparison with related proteins. J Biol Chem 269: 4135-4143.
    • (1994) J Biol Chem , vol.269 , pp. 4135-4143
    • Oh, B.H.1    Kang, C.H.2    De Bondt, H.3    Kim, S.H.4    Nikaido, K.5    Joshi, A.K.6    Ames, G.F.7
  • 33
    • 77952905782 scopus 로고    scopus 로고
    • The L-cysteine/L-cystine shuttle system provides reducing equivalents to the periplasm in Escherichia coli
    • Ohtsu, I., Wiriyathanawudhiwong, N., Morigasaki, S., Nakatani, T., Kadokura, H., and Takagi, H. (2010) The L-cysteine/L-cystine shuttle system provides reducing equivalents to the periplasm in Escherichia coli. J Biol Chem 285: 17479-17487.
    • (2010) J Biol Chem , vol.285 , pp. 17479-17487
    • Ohtsu, I.1    Wiriyathanawudhiwong, N.2    Morigasaki, S.3    Nakatani, T.4    Kadokura, H.5    Takagi, H.6
  • 34
    • 84865293921 scopus 로고    scopus 로고
    • Current status and emerging role of glutathione in food grade lactic acid bacteria
    • Pophaly, S.D., Singh, R., Pophaly, S.D., Kaushik, J.K., and Tomar, S.K. (2012) Current status and emerging role of glutathione in food grade lactic acid bacteria. Microb Cell Fact 11: 1-14.
    • (2012) Microb Cell Fact , vol.11 , pp. 1-14
    • Pophaly, S.D.1    Singh, R.2    Pophaly, S.D.3    Kaushik, J.K.4    Tomar, S.K.5
  • 35
    • 84869105723 scopus 로고    scopus 로고
    • Streptococcus pneumoniae uses glutathione to defend against oxidative stress and metal ion toxicity
    • Potter, A.J., Trappetti, C., and Paton, J.C. (2012) Streptococcus pneumoniae uses glutathione to defend against oxidative stress and metal ion toxicity. J Bacteriol 194: 6248-6254.
    • (2012) J Bacteriol , vol.194 , pp. 6248-6254
    • Potter, A.J.1    Trappetti, C.2    Paton, J.C.3
  • 36
    • 73049125364 scopus 로고
    • Utilization of sulfur compounds by Streptococcus bovis
    • Prescott, J.M. (1961) Utilization of sulfur compounds by Streptococcus bovis. J Bacteriol 82: 724-728.
    • (1961) J Bacteriol , vol.82 , pp. 724-728
    • Prescott, J.M.1
  • 37
  • 38
    • 33846896349 scopus 로고    scopus 로고
    • The Streptococcus mutans vicX gene product modulates gtfB/C expression, biofilm formation, genetic competence, and oxidative stress tolerance
    • Senadheera, M.D., Lee, A.W., Hung, D.C., Spatafora, G.A., Goodman, S.D., and Cvitkovitch, D.G. (2007) The Streptococcus mutans vicX gene product modulates gtfB/C expression, biofilm formation, genetic competence, and oxidative stress tolerance. J Bacteriol 189: 1451-1458.
    • (2007) J Bacteriol , vol.189 , pp. 1451-1458
    • Senadheera, M.D.1    Lee, A.W.2    Hung, D.C.3    Spatafora, G.A.4    Goodman, S.D.5    Cvitkovitch, D.G.6
  • 39
    • 0034574721 scopus 로고    scopus 로고
    • Transport of glutathione-conjugates in human erythrocytes
    • Sharma, R., Awasthi, S., Zimniak, P., and Awasthi, Y.C. (2000) Transport of glutathione-conjugates in human erythrocytes. Acta Biochim Pol 47: 751-762.
    • (2000) Acta Biochim Pol , vol.47 , pp. 751-762
    • Sharma, R.1    Awasthi, S.2    Zimniak, P.3    Awasthi, Y.C.4
  • 40
    • 0031894921 scopus 로고    scopus 로고
    • Import and metabolism of glutathione by Streptococcus mutans
    • Sherrill, C., and Fahey, R.C. (1998) Import and metabolism of glutathione by Streptococcus mutans. J Bacteriol 180: 1454-1459.
    • (1998) J Bacteriol , vol.180 , pp. 1454-1459
    • Sherrill, C.1    Fahey, R.C.2
  • 41
    • 0029017142 scopus 로고
    • Sulfate and thiosulfate transport in Escherichia coli K-12: evidence for a functional overlapping of sulfate- and thiosulfate-binding proteins
    • Sirko, A., Zatyka, M., Sadowy, E., and Hulanicka, D. (1995) Sulfate and thiosulfate transport in Escherichia coli K-12: evidence for a functional overlapping of sulfate- and thiosulfate-binding proteins. J Bacteriol 177: 4134-4136.
    • (1995) J Bacteriol , vol.177 , pp. 4134-4136
    • Sirko, A.1    Zatyka, M.2    Sadowy, E.3    Hulanicka, D.4
  • 42
    • 76949138686 scopus 로고
    • The amino acid nutrition of group A hemolytic Streptococci, with reference to the effect of glutathione on the cystine requirement
    • Slade, H.D., Knox, G.A., and Slamp, W.C. (1951) The amino acid nutrition of group A hemolytic Streptococci, with reference to the effect of glutathione on the cystine requirement. J Bacteriol 62: 669-675.
    • (1951) J Bacteriol , vol.62 , pp. 669-675
    • Slade, H.D.1    Knox, G.A.2    Slamp, W.C.3
  • 43
    • 84856370436 scopus 로고    scopus 로고
    • Gene regulation in S.mutans: complex control in a complex environment
    • Smith, E.G., and Spatafora, G.A. (2012) Gene regulation in S.mutans: complex control in a complex environment. J Dent Res 91: 133-141.
    • (2012) J Dent Res , vol.91 , pp. 133-141
    • Smith, E.G.1    Spatafora, G.A.2
  • 45
    • 77954373711 scopus 로고    scopus 로고
    • Three paralogous LysR-type transcriptional regulators control sulfur amino acid supply in Streptococcus mutans
    • Sperandio, B., Gautier, C., Pons, N., Ehrlich, D.S., Renault, P., and Guedon, E. (2010) Three paralogous LysR-type transcriptional regulators control sulfur amino acid supply in Streptococcus mutans. J Bacteriol 192: 3464-3473.
    • (2010) J Bacteriol , vol.192 , pp. 3464-3473
    • Sperandio, B.1    Gautier, C.2    Pons, N.3    Ehrlich, D.S.4    Renault, P.5    Guedon, E.6
  • 46
    • 79958772445 scopus 로고    scopus 로고
    • Crystallographic and microcalorimetric analyses reveal the structural basis for high arginine specificity in the Salmonella enterica serovar Typhimurium periplasmic binding protein STM4351
    • Stamp, A.L., Owen, P., El Omari, K., Lockyer, M., Lamb, H.K., Charles, I.G., etal. (2011) Crystallographic and microcalorimetric analyses reveal the structural basis for high arginine specificity in the Salmonella enterica serovar Typhimurium periplasmic binding protein STM4351. Proteins 79: 2352-2357.
    • (2011) Proteins , vol.79 , pp. 2352-2357
    • Stamp, A.L.1    Owen, P.2    El Omari, K.3    Lockyer, M.4    Lamb, H.K.5    Charles, I.G.6
  • 47
    • 43749083257 scopus 로고    scopus 로고
    • CHAINSAW: a program for mutating pdb files used as templates in molecular replacement
    • Stein, N. (2008) CHAINSAW: a program for mutating pdb files used as templates in molecular replacement. J Appl Crystallogr 41: 641-643.
    • (2008) J Appl Crystallogr , vol.41 , pp. 641-643
    • Stein, N.1
  • 48
    • 84857361072 scopus 로고    scopus 로고
    • Glutathione biosynthesis in bacteria by bifunctional GshF is driven by a modular structure featuring a novel hybrid ATP-grasp fold
    • Stout, J., De Vos, D., Vergauwen, B., and Savvides, S.N. (2012) Glutathione biosynthesis in bacteria by bifunctional GshF is driven by a modular structure featuring a novel hybrid ATP-grasp fold. J Mol Biol 416: 486-494.
    • (2012) J Mol Biol , vol.416 , pp. 486-494
    • Stout, J.1    De Vos, D.2    Vergauwen, B.3    Savvides, S.N.4
  • 49
    • 39149119282 scopus 로고    scopus 로고
    • A pneumococcal MerR-like regulator and S-nitrosoglutathione reductase are required for systemic virulence
    • Stroeher, U.H., Kidd, S.P., Stafford, S.L., Jennings, M.P., Paton, J.C., and McEwan, A.G. (2007) A pneumococcal MerR-like regulator and S-nitrosoglutathione reductase are required for systemic virulence. J Infect Dis 196: 1820-1826.
    • (2007) J Infect Dis , vol.196 , pp. 1820-1826
    • Stroeher, U.H.1    Kidd, S.P.2    Stafford, S.L.3    Jennings, M.P.4    Paton, J.C.5    McEwan, A.G.6
  • 50
    • 0036066456 scopus 로고    scopus 로고
    • Pattern searches for the identification of putative lipoprotein genes in Gram-positive bacterial genomes
    • Sutcliffe, I.C., and Harrington, D.J. (2002) Pattern searches for the identification of putative lipoprotein genes in Gram-positive bacterial genomes. Microbiology 148: 2065-2077.
    • (2002) Microbiology , vol.148 , pp. 2065-2077
    • Sutcliffe, I.C.1    Harrington, D.J.2
  • 51
    • 24344468705 scopus 로고    scopus 로고
    • The yliA, -B, -C, and -D genes of Escherichia coli K-12 encode a novel glutathione importer with an ATP-binding cassette
    • Suzuki, H., Koyanagi, T., Izuka, S., Onishi, A., and Kumagai, H. (2005) The yliA, -B, -C, and -D genes of Escherichia coli K-12 encode a novel glutathione importer with an ATP-binding cassette. J Bacteriol 187: 5861-5867.
    • (2005) J Bacteriol , vol.187 , pp. 5861-5867
    • Suzuki, H.1    Koyanagi, T.2    Izuka, S.3    Onishi, A.4    Kumagai, H.5
  • 52
    • 0027256676 scopus 로고
    • Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria
    • Tam, R., and Saier, M.H., Jr (1993) Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria. Microbiol Rev 57: 320-346.
    • (1993) Microbiol Rev , vol.57 , pp. 320-346
    • Tam, R.1    Saier Jr., M.H.2
  • 53
    • 0021334514 scopus 로고
    • Disulfide reduction and sulfhydryl uptake by Streptococcus mutans
    • Thomas, E.L. (1984) Disulfide reduction and sulfhydryl uptake by Streptococcus mutans. J Bacteriol 157: 240-246.
    • (1984) J Bacteriol , vol.157 , pp. 240-246
    • Thomas, E.L.1
  • 54
    • 0020657616 scopus 로고
    • Inhibition of Streptococcus mutans by the lactoperoxidase antimicrobial system
    • Thomas, E.L., Pera, K.A., Smith, K.W., and Chwang, A.K. (1983) Inhibition of Streptococcus mutans by the lactoperoxidase antimicrobial system. Infect Immun 39: 767-778.
    • (1983) Infect Immun , vol.39 , pp. 767-778
    • Thomas, E.L.1    Pera, K.A.2    Smith, K.W.3    Chwang, A.K.4
  • 55
    • 0014481378 scopus 로고
    • Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: applications to mammalian blood and other tissues
    • Tietze, F. (1969) Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: applications to mammalian blood and other tissues. Anal Biochem 27: 502-522.
    • (1969) Anal Biochem , vol.27 , pp. 502-522
    • Tietze, F.1
  • 56
    • 36549063540 scopus 로고    scopus 로고
    • Crystal structures and mutational analysis of the arginine-, lysine-, histidine-binding protein ArtJ from Geobacillus stearothermophilus. Implications for interactions of ArtJ with its cognate ATP-binding cassette transporter, Art(MP)2
    • Vahedi-Faridi, A., Eckey, V., Scheffel, F., Alings, C., Landmesser, H., Schneider, E., and Saenger, W. (2008) Crystal structures and mutational analysis of the arginine-, lysine-, histidine-binding protein ArtJ from Geobacillus stearothermophilus. Implications for interactions of ArtJ with its cognate ATP-binding cassette transporter, Art(MP)2. J Mol Biol 375: 448-459.
    • (2008) J Mol Biol , vol.375 , pp. 448-459
    • Vahedi-Faridi, A.1    Eckey, V.2    Scheffel, F.3    Alings, C.4    Landmesser, H.5    Schneider, E.6    Saenger, W.7
  • 57
    • 34250641961 scopus 로고    scopus 로고
    • Isothermal titration calorimetry to determine association constants for high-affinity ligands
    • Velazquez-Campoy, A., and Freire, E. (2006) Isothermal titration calorimetry to determine association constants for high-affinity ligands. Nature protocols 1: 186-191.
    • (2006) Nature protocols , vol.1 , pp. 186-191
    • Velazquez-Campoy, A.1    Freire, E.2
  • 58
    • 0042838106 scopus 로고    scopus 로고
    • Glutathione and catalase provide overlapping defenses for protection against respiration-generated hydrogen peroxide in Haemophilus influenzae
    • Vergauwen, B., Pauwels, F., and Van Beeumen, J.J. (2003a) Glutathione and catalase provide overlapping defenses for protection against respiration-generated hydrogen peroxide in Haemophilus influenzae. J Bacteriol 185: 5555-5562.
    • (2003) J Bacteriol , vol.185 , pp. 5555-5562
    • Vergauwen, B.1    Pauwels, F.2    Van Beeumen, J.J.3
  • 59
    • 0037369926 scopus 로고    scopus 로고
    • Exogenous glutathione completes the defense against oxidative stress in Haemophilus influenzae
    • Vergauwen, B., Pauwels, F., Vaneechoutte, M., and Van Beeumen, J.J. (2003b) Exogenous glutathione completes the defense against oxidative stress in Haemophilus influenzae. J Bacteriol 185: 1572-1581.
    • (2003) J Bacteriol , vol.185 , pp. 1572-1581
    • Vergauwen, B.1    Pauwels, F.2    Vaneechoutte, M.3    Van Beeumen, J.J.4
  • 60
    • 33645224817 scopus 로고    scopus 로고
    • Characterization of the bifunctional gamma-glutamate-cysteine ligase/glutathione synthetase (GshF) of Pasteurella multocida
    • Vergauwen, B., De Vos, D., and Van Beeumen, J.J. (2006) Characterization of the bifunctional gamma-glutamate-cysteine ligase/glutathione synthetase (GshF) of Pasteurella multocida. J Biol Chem 281: 4380-4394.
    • (2006) J Biol Chem , vol.281 , pp. 4380-4394
    • Vergauwen, B.1    De Vos, D.2    Van Beeumen, J.J.3
  • 61
    • 77955828073 scopus 로고    scopus 로고
    • Glutathione import in Haemophilus influenzae Rd is primed by the periplasmic heme-binding protein HbpA
    • Vergauwen, B., Elegheert, J., Dansercoer, A., Devreese, B., and Savvides, S.N. (2010) Glutathione import in Haemophilus influenzae Rd is primed by the periplasmic heme-binding protein HbpA. Proc Natl Acad Sci USA 107: 13270-13275.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 13270-13275
    • Vergauwen, B.1    Elegheert, J.2    Dansercoer, A.3    Devreese, B.4    Savvides, S.N.5
  • 62
    • 81055138859 scopus 로고    scopus 로고
    • Delineation of the Pasteurellaceae-specific GbpA-family of glutathione-binding proteins
    • Vergauwen, B., Van der Meeren, R., Dansercoer, A., and Savvides, S.N. (2011) Delineation of the Pasteurellaceae-specific GbpA-family of glutathione-binding proteins. BMC Biochem 12: 59.
    • (2011) BMC Biochem , vol.12 , pp. 59
    • Vergauwen, B.1    Van der Meeren, R.2    Dansercoer, A.3    Savvides, S.N.4
  • 63
    • 37549046795 scopus 로고    scopus 로고
    • Two closely related ABC transporters in Streptococcus mutans are involved in disaccharide and/or oligosaccharide uptake
    • Webb, A.J., Homer, K.A., and Hosie, A.H. (2008) Two closely related ABC transporters in Streptococcus mutans are involved in disaccharide and/or oligosaccharide uptake. J Bacteriol 190: 168-178.
    • (2008) J Bacteriol , vol.190 , pp. 168-178
    • Webb, A.J.1    Homer, K.A.2    Hosie, A.H.3
  • 64
    • 11144292733 scopus 로고    scopus 로고
    • The membrane-associated lipoprotein-9 GmpC from Staphylococcus aureus binds the dipeptide GlyMet via side chain interactions
    • Williams, W.A., Zhang, R.G., Zhou, M., Joachimiak, G., Gornicki, P., Missiakas, D., and Joachimiak, A. (2004) The membrane-associated lipoprotein-9 GmpC from Staphylococcus aureus binds the dipeptide GlyMet via side chain interactions. Biochemistry 43: 16193-16202.
    • (2004) Biochemistry , vol.43 , pp. 16193-16202
    • Williams, W.A.1    Zhang, R.G.2    Zhou, M.3    Joachimiak, G.4    Gornicki, P.5    Missiakas, D.6    Joachimiak, A.7
  • 65
    • 0033141893 scopus 로고    scopus 로고
    • Cloning, nucleotide sequence, and disruption of Streptococcus mutans glutathione reductase gene (gor)
    • Yamamoto, Y., Kamio, Y., and Higuchi, M. (1999) Cloning, nucleotide sequence, and disruption of Streptococcus mutans glutathione reductase gene (gor). Biosci Biotechnol Biochem 63: 1056-1062.
    • (1999) Biosci Biotechnol Biochem , vol.63 , pp. 1056-1062
    • Yamamoto, Y.1    Kamio, Y.2    Higuchi, M.3
  • 66
    • 0028174670 scopus 로고
    • Refined 1.89-A structure of the histidine-binding protein complexed with histidine and its relationship with many other active transport/chemosensory proteins
    • Yao, N., Trakhanov, S., and Quiocho, F.A. (1994) Refined 1.89-A structure of the histidine-binding protein complexed with histidine and its relationship with many other active transport/chemosensory proteins. Biochemistry 33: 4769-4779.
    • (1994) Biochemistry , vol.33 , pp. 4769-4779
    • Yao, N.1    Trakhanov, S.2    Quiocho, F.A.3
  • 67
    • 0033950182 scopus 로고    scopus 로고
    • Evidence for a strong sulfur-aromatic interaction derived from crystallographic data
    • Zauhar, R.J., Colbert, C.L., Morgan, R.S., and Welsh, W.J. (2000) Evidence for a strong sulfur-aromatic interaction derived from crystallographic data. Biopolymers 53: 233-248.
    • (2000) Biopolymers , vol.53 , pp. 233-248
    • Zauhar, R.J.1    Colbert, C.L.2    Morgan, R.S.3    Welsh, W.J.4
  • 68
    • 77952252747 scopus 로고    scopus 로고
    • Proteomic analyses to reveal the protective role of glutathione in resistance of Lactococcus lactis to osmotic stress
    • Zhang, Y., Zhang, Y., Zhu, Y., Mao, S., and Li, Y. (2010) Proteomic analyses to reveal the protective role of glutathione in resistance of Lactococcus lactis to osmotic stress. Appl Environ Microbiol 76: 3177-3186.
    • (2010) Appl Environ Microbiol , vol.76 , pp. 3177-3186
    • Zhang, Y.1    Zhang, Y.2    Zhu, Y.3    Mao, S.4    Li, Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.