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Volumn 9, Issue 12, 2014, Pages

Formation of hydrogen sulfide from cysteine in Saccharomyces cerevisiae BY4742: Genome wide screen reveals a central role of the vacuole

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; HYDROGEN SULFIDE;

EID: 84919341594     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0113869     Document Type: Article
Times cited : (16)

References (62)
  • 1
    • 3142729014 scopus 로고    scopus 로고
    • Sulfur amino acid metabolism: Pathways for production and removal of homocysteine and cysteine
    • Stipanuk MH (2004) Sulfur amino acid metabolism: pathways for production and removal of homocysteine and cysteine. Ann Rev Nutr 24: 539-577.
    • (2004) Ann Rev Nutr , vol.24 , pp. 539-577
    • Stipanuk, M.H.1
  • 2
    • 33646814739 scopus 로고    scopus 로고
    • Homocysteine- and cysteine-mediated growth defect is not associated with induction of oxidative stress response genes in yeast
    • Kumar A, John L, Alam MM, Gupta A, Sharma G, et al. (2006) Homocysteine- and cysteine-mediated growth defect is not associated with induction of oxidative stress response genes in yeast. Biochem J 396: 61-69.
    • (2006) Biochem J , vol.396 , pp. 61-69
    • Kumar, A.1    John, L.2    Alam, M.M.3    Gupta, A.4    Sharma, G.5
  • 3
    • 0026088268 scopus 로고
    • Regulation of cystathionine c-lyase in Saccharomyces cerevisiae
    • Ono B-I, Naito K, Shirahige Y-I, Yamamoto M (1991) Regulation of cystathionine c-lyase in Saccharomyces cerevisiae. Yeast 7: 843-848.
    • (1991) Yeast , vol.7 , pp. 843-848
    • Ono, B.-I.1    Naito, K.2    Shirahige, Y.-I.3    Yamamoto, M.4
  • 5
    • 0025165272 scopus 로고
    • Plasma cysteine and sulphate levels in patients with motor neurone, Parkinson's and Alzheimer's disease
    • Heafield MT, Fearn S, Steventon GB, Waring RH, Williams AC, et al. (1990) Plasma cysteine and sulphate levels in patients with motor neurone, Parkinson's and Alzheimer's disease. Neurosci Lett 110: 216-220.
    • (1990) Neurosci Lett , vol.110 , pp. 216-220
    • Heafield, M.T.1    Fearn, S.2    Steventon, G.B.3    Waring, R.H.4    Williams, A.C.5
  • 6
    • 66449109703 scopus 로고    scopus 로고
    • 3-Lyase leads to the novel sulfur metabolites lanthionine and homolanthionine and is responsive to the grade of hyperhomocysteinemia
    • 3-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
  • 7
    • 77954579286 scopus 로고    scopus 로고
    • Redox biochemistry of hydrogen sulfide
    • Kabil O, 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
  • 8
    • 0036700930 scopus 로고    scopus 로고
    • Hydrogen sulfide as a neuromodulator
    • Kimura H (2002) Hydrogen sulfide as a neuromodulator. Mol Neurobiol 26: 13-19.
    • (2002) Mol Neurobiol , vol.26 , pp. 13-19
    • Kimura, H.1
  • 9
    • 0036845556 scopus 로고    scopus 로고
    • Two is company, three is a crowd: Can H2S be the third endogenous gaseous transmitter?
    • Wang RUI (2002) Two is company, three is a crowd: can H2S be the third endogenous gaseous transmitter? FASEB Journal 16: 1792-1798.
    • (2002) FASEB Journal , vol.16 , pp. 1792-1798
    • Wang, R.U.I.1
  • 10
    • 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
  • 11
    • 79961076132 scopus 로고    scopus 로고
    • The therapeutic potential of hydrogen sulfide: Separating hype from hope
    • Olson KR (2011) The therapeutic potential of hydrogen sulfide: separating hype from hope. Am J Physiol 301(2): R297-312.
    • (2011) Am J Physiol , vol.301 , Issue.2 , pp. R297-R312
    • Olson, K.R.1
  • 12
    • 0033608536 scopus 로고    scopus 로고
    • Why is the global warming proceeding much slower than expected?
    • Bengtsson L, Roeckner E, Stendel M (1999) Why is the global warming proceeding much slower than expected? J Geophys Res Atmos 104: 3865-3876.
    • (1999) J Geophys Res Atmos , vol.104 , pp. 3865-3876
    • Bengtsson, L.1    Roeckner, E.2    Stendel, M.3
  • 14
    • 10644254287 scopus 로고    scopus 로고
    • 2S by Cystathionine β-Synthase via the condensation of cysteine and homocysteine
    • 2S by Cystathionine β-Synthase via the condensation of cysteine and homocysteine. J Biol Chem 279: 52082-52086.
    • (2004) J Biol Chem , vol.279 , pp. 52082-52086
    • Chen, X.1    Jhee, K.-H.2    Kruger, W.D.3
  • 15
    • 78651339218 scopus 로고    scopus 로고
    • 2-synthase deficiency: Future directions for homocysteine-to-hydrogen sulfide research
    • 2-synthase deficiency: future directions for homocysteine-to-hydrogen sulfide research. Am J Physiol Heart Circ Physiol 300: H13-H26.
    • (2011) Am J Physiol Heart Circ Physiol , vol.300 , pp. H13-H26
    • Beard, R.S.1    Bearden, S.E.2
  • 16
    • 0028198781 scopus 로고
    • A yeast system for expression of human cystathionine beta-synthase: Structural and functional conservation of the human and yeast genes
    • Kruger WD, Cox DR (1994) A yeast system for expression of human cystathionine beta-synthase: structural and functional conservation of the human and yeast genes. Proc Nat Acad Sci 91: 6614-6618.
    • (1994) Proc Nat Acad Sci , vol.91 , pp. 6614-6618
    • Kruger, W.D.1    Cox, D.R.2
  • 17
    • 0029045384 scopus 로고
    • A yeast assay for functional detection of mutations in the human cystathionine β-synthase gene
    • Kruger WD, Cox DR (1995) A yeast assay for functional detection of mutations in the human cystathionine β-synthase gene. Hum Mol Genet 4: 1155-1161.
    • (1995) Hum Mol Genet , vol.4 , pp. 1155-1161
    • Kruger, W.D.1    Cox, D.R.2
  • 18
    • 0031798556 scopus 로고    scopus 로고
    • Correction of disease-causing CBS mutations in yeast
    • Shan X, Kruger WD (1998) Correction of disease-causing CBS mutations in yeast. Nat Genet 19: 91-93.
    • (1998) Nat Genet , vol.19 , pp. 91-93
    • Shan, X.1    Kruger, W.D.2
  • 19
    • 0027230548 scopus 로고
    • Physical localization of yeast CYS3, a gene whose product resembles the rat γ-cystathionase and Escherichia coli cystathionine γ-synthase enzymes
    • Barton AB, Kaback DB, Clark MW, Keng T, Ouellette BFF, et al. (1993) Physical localization of yeast CYS3, a gene whose product resembles the rat γ-cystathionase and Escherichia coli cystathionine γ-synthase enzymes. Yeast 9: 363-369.
    • (1993) Yeast , vol.9 , pp. 363-369
    • Barton, A.B.1    Kaback, D.B.2    Clark, M.W.3    Keng, T.4    Ouellette, B.F.F.5
  • 20
    • 0032579440 scopus 로고    scopus 로고
    • Designer deletion strains derived from Saccharomyces cerevisiae S288C: A useful set of strains and plasmids for PCR-mediated gene disruption and other applications
    • Brachmann C, Davies A, Cost G, Caputo E, Li J, et al. (1998) Designer deletion strains derived from Saccharomyces cerevisiae S288C: a useful set of strains and plasmids for PCR-mediated gene disruption and other applications. Yeast 14: 115-132.
    • (1998) Yeast , vol.14 , pp. 115-132
    • Brachmann, C.1    Davies, A.2    Cost, G.3    Caputo, E.4    Li, J.5
  • 21
    • 79957763568 scopus 로고    scopus 로고
    • Contribution of cysteine and glutathione conjugates to the formation of the volatile thiols 3-mercaptohexan-1-ol (3MH) and 3-mercaptohexyl acetate (3MHA) during fermentation by Saccharomyces cerevisiae
    • Winter G, Van Der Westhuizen T, Higgins VJ, Curtin C, Ugliano M (2011) Contribution of cysteine and glutathione conjugates to the formation of the volatile thiols 3-mercaptohexan-1-ol (3MH) and 3-mercaptohexyl acetate (3MHA) during fermentation by Saccharomyces cerevisiae. Aus J Grape Wine Res 17: 285-290.
    • (2011) Aus J Grape Wine Res , vol.17 , pp. 285-290
    • Winter, G.1    Van Der Westhuizen, T.2    Higgins, V.J.3    Curtin, C.4    Ugliano, M.5
  • 24
  • 26
    • 0033529707 scopus 로고    scopus 로고
    • Functional characterization of the S. Cerevisiae genome by gene deletion and parallel analysis
    • Winzeler EA, Shoemaker DD, Astromoff A, Liang H, Anderson K, et al. (1999) Functional characterization of the S. cerevisiae genome by gene deletion and parallel analysis. Science 285: 901-906.
    • (1999) Science , vol.285 , pp. 901-906
    • Winzeler, E.A.1    Shoemaker, D.D.2    Astromoff, A.3    Liang, H.4    Anderson, K.5
  • 27
    • 60849139395 scopus 로고    scopus 로고
    • GOrilla: A tool for discovery and visualization of enriched GO terms in ranked gene lists
    • Eden E, Navon R, Steinfeld I, Lipson D, Yakhini Z (2009) GOrilla: a tool for discovery and visualization of enriched GO terms in ranked gene lists. BMC Bioinformatics 10: 48.
    • (2009) BMC Bioinformatics , vol.10 , pp. 48
    • Eden, E.1    Navon, R.2    Steinfeld, I.3    Lipson, D.4    Yakhini, Z.5
  • 28
    • 0037173615 scopus 로고    scopus 로고
    • Functional profiling of the Saccharomyces cerevisiae genome
    • Giaever G, Chu AM, Ni L, Connelly C, Riles L, et al. (2002) Functional profiling of the Saccharomyces cerevisiae genome. Nature 418: 387-391.
    • (2002) Nature , vol.418 , pp. 387-391
    • Giaever, G.1    Chu, A.M.2    Ni, L.3    Connelly, C.4    Riles, L.5
  • 29
    • 0038651222 scopus 로고    scopus 로고
    • Purine synthesis and increased Agrobacterium tumefaciens transformation of yeast and plants
    • Roberts RL, Metz M, Monks DE, Mullaney ML, Hall T, et al. (2003) Purine synthesis and increased Agrobacterium tumefaciens transformation of yeast and plants. Proc Nat Acad Sci 100: 6634-6639.
    • (2003) Proc Nat Acad Sci , vol.100 , pp. 6634-6639
    • Roberts, R.L.1    Metz, M.2    Monks, D.E.3    Mullaney, M.L.4    Hall, T.5
  • 30
    • 0031172735 scopus 로고    scopus 로고
    • Folates and one-carbon metabolism in plants and fungi
    • Cossins EA, Chen L (1997) Folates and one-carbon metabolism in plants and fungi. Phytochemistry 45: 437-452.
    • (1997) Phytochemistry , vol.45 , pp. 437-452
    • Cossins, E.A.1    Chen, L.2
  • 31
    • 33645119556 scopus 로고    scopus 로고
    • The where, when, and how of organelle acidification by the yeast vacuolar H+-ATPase
    • Kane PM (2006) The where, when, and how of organelle acidification by the yeast vacuolar H+-ATPase. Microbiol Mol Biol Rev 70: 177-191.
    • (2006) Microbiol Mol Biol Rev , vol.70 , pp. 177-191
    • Kane, P.M.1
  • 32
    • 0142089024 scopus 로고    scopus 로고
    • Assembly and regulation of the yeast vacuolar H+-ATPase
    • Kane PM, Smardon AM (2003) Assembly and regulation of the yeast vacuolar H+-ATPase. J Bioenerg Biomembr 35: 313-321.
    • (2003) J Bioenerg Biomembr , vol.35 , pp. 313-321
    • Kane, P.M.1    Smardon, A.M.2
  • 33
    • 0347994900 scopus 로고    scopus 로고
    • High-resolution yeast phenomics resolves different physiological features in the saline response
    • Warringer J, Ericson E, Fernandez L, Nerman O, Blomberg A (2003) High-resolution yeast phenomics resolves different physiological features in the saline response. Proc Nat Acad Sci 100: 15724-15729.
    • (2003) Proc Nat Acad Sci , vol.100 , pp. 15724-15729
    • Warringer, J.1    Ericson, E.2    Fernandez, L.3    Nerman, O.4    Blomberg, A.5
  • 34
    • 47149118006 scopus 로고    scopus 로고
    • Membrane transporters and protein traffic networks differentially affecting metal tolerance: A genomic phenotyping study in yeast
    • Ruotolo R, Marchini G, Ottonello S (2008) Membrane transporters and protein traffic networks differentially affecting metal tolerance: a genomic phenotyping study in yeast. Genome Biol 9: R67.
    • (2008) Genome Biol , vol.9 , pp. R67
    • Ruotolo, R.1    Marchini, G.2    Ottonello, S.3
  • 35
    • 2342487990 scopus 로고    scopus 로고
    • Cells have distinct mechanisms to maintain protection against different reactive oxygen species: Oxidative-stress-response genes
    • Thorpe GW, Fong CS, Alic N, Higgins VJ, Dawes IW (2004) Cells have distinct mechanisms to maintain protection against different reactive oxygen species: Oxidative-stress-response genes. PNAS 101: 6564-6569.
    • (2004) PNAS , vol.101 , pp. 6564-6569
    • Thorpe, G.W.1    Fong, C.S.2    Alic, N.3    Higgins, V.J.4    Dawes, I.W.5
  • 36
    • 11144331477 scopus 로고    scopus 로고
    • Genetic and environmental factors influencing glutathione homeostasis in Saccharomyces cerevisiae
    • Perrone GG, Grant CM, Dawes IW (2005) Genetic and environmental factors influencing glutathione homeostasis in Saccharomyces cerevisiae. Mol Biol Cell 16: 218-230.
    • (2005) Mol Biol Cell , vol.16 , pp. 218-230
    • Perrone, G.G.1    Grant, C.M.2    Dawes, I.W.3
  • 37
  • 38
    • 77049133293 scopus 로고
    • Reduction of inorganic substances by yeast. I. Extracellular reduction of sulfite by species of Candida
    • Nickerson WJ (1953) Reduction of inorganic substances by yeast. I. Extracellular reduction of sulfite by species of Candida. J Infectious Dis 93: 43-48.
    • (1953) J Infectious Dis , vol.93 , pp. 43-48
    • Nickerson, W.J.1
  • 39
    • 56649114285 scopus 로고    scopus 로고
    • Development of amethod to measure hydrogen sulfide in wine fermentation
    • Park SK (2008) Development of amethod to measure hydrogen sulfide in wine fermentation. J Microbiol Biotechnol 18: 1550-1554.
    • (2008) J Microbiol Biotechnol , vol.18 , pp. 1550-1554
    • Park, S.K.1
  • 40
    • 0020483746 scopus 로고
    • Characterization of the enzymic capacity for cysteine desulphhydration in liver and kidney of the rat
    • Stipanuk MH, Beck PW (1982) Characterization of the enzymic capacity for cysteine desulphhydration in liver and kidney of the rat. Biochem J 206: 267-277.
    • (1982) Biochem J , vol.206 , pp. 267-277
    • Stipanuk, M.H.1    Beck, P.W.2
  • 41
    • 0033794872 scopus 로고    scopus 로고
    • Cysteine is essential for transcriptional regulation of the sulfur assimilation genes in Saccharomyces cerevisiae
    • Hansen J, Francke Johannesen P (2000) Cysteine is essential for transcriptional regulation of the sulfur assimilation genes in Saccharomyces cerevisiae. Mol Gen Genet 263: 535-542.
    • (2000) Mol Gen Genet , vol.263 , pp. 535-542
    • Hansen, J.1    Francke Johannesen, P.2
  • 42
    • 67651160667 scopus 로고    scopus 로고
    • Dissecting the pleiotropic consequences of a quantitative trait nucleotide
    • Kim HS, Huh J, Fay JC (2009) Dissecting the pleiotropic consequences of a quantitative trait nucleotide. FEMS Yeast Res 9: 713-722.
    • (2009) FEMS Yeast Res , vol.9 , pp. 713-722
    • Kim, H.S.1    Huh, J.2    Fay, J.C.3
  • 44
    • 4344595102 scopus 로고    scopus 로고
    • Functional characterization of the eukaryotic cysteine desulfurase Nfs1p from Saccharomyces cerevisiae
    • Mühlenhoff U, Balk J, Richhardt N, Kaiser JT, Sipos K, et al. (2004) Functional characterization of the eukaryotic cysteine desulfurase Nfs1p from Saccharomyces cerevisiae. J Biol Chem 279: 36906-36915.
    • (2004) J Biol Chem , vol.279 , pp. 36906-36915
    • Mühlenhoff, U.1    Balk, J.2    Richhardt, N.3    Kaiser, J.T.4    Sipos, K.5
  • 45
    • 2242453224 scopus 로고    scopus 로고
    • Characterization of iron-sulfur protein assembly in isolated mitochondria
    • Mühlenhoff U, Richhardt N, Gerber J, Lill R (2002) Characterization of iron-sulfur protein assembly in isolated mitochondria. J Biol Chem 277: 29810-29816.
    • (2002) J Biol Chem , vol.277 , pp. 29810-29816
    • Mühlenhoff, U.1    Richhardt, N.2    Gerber, J.3    Lill, R.4
  • 46
    • 4544321137 scopus 로고    scopus 로고
    • The cell's cookbook for iron-sulfur clusters: Recipes for fool's gold?
    • Balk J, Lill R (2004) The cell's cookbook for iron-sulfur clusters: recipes for fool's gold? Chembiochem 5: 1044-1049.
    • (2004) Chembiochem , vol.5 , pp. 1044-1049
    • Balk, J.1    Lill, R.2
  • 47
    • 0034255836 scopus 로고    scopus 로고
    • Maturation of cellular Fe-S proteins: An essential function of mitochondria
    • Lill R, Kispal G (2000) Maturation of cellular Fe-S proteins: an essential function of mitochondria. Trends Biochem Sci 25: 352-356.
    • (2000) Trends Biochem Sci , vol.25 , pp. 352-356
    • Lill, R.1    Kispal, G.2
  • 48
    • 17144378216 scopus 로고    scopus 로고
    • Iron-sulphur cluster biogenesis and mitochondrial iron homeostasis
    • Rouault TA, Tong W-H (2005) Iron-sulphur cluster biogenesis and mitochondrial iron homeostasis. Nat Rev Mol Cell Biol 6: 345-351.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 345-351
    • Rouault, T.A.1    Tong, W.-H.2
  • 49
    • 0033565665 scopus 로고    scopus 로고
    • The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins
    • Kispal G, Csere P, Prohl C, Lill R (1999) The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins. EMBO J 18: 3981-3989.
    • (1999) EMBO J , vol.18 , pp. 3981-3989
    • Kispal, G.1    Csere, P.2    Prohl, C.3    Lill, R.4
  • 50
    • 0032722872 scopus 로고    scopus 로고
    • Yeast mitochondrial protein, Nfs1p, coordinately regulates iron-sulfur cluster proteins, cellular iron uptake, and iron distribution
    • Li J, Kogan M, Knight SAB, Pain D, Dancis A (1999) Yeast mitochondrial protein, Nfs1p, coordinately regulates iron-sulfur cluster proteins, cellular iron uptake, and iron distribution. J Biol Chem 274: 33025-33034.
    • (1999) J Biol Chem , vol.274 , pp. 33025-33034
    • Li, J.1    Kogan, M.2    Knight, S.A.B.3    Pain, D.4    Dancis, A.5
  • 51
    • 0029786777 scopus 로고    scopus 로고
    • Regulation of sulphate assimilation in Saccharomyces cerevisiae
    • Ono B-I, Kijima K, Ishii N, Kawato T, Matsuda A, et al. (1996) Regulation of sulphate assimilation in Saccharomyces cerevisiae. Yeast 12: 1153-1162.
    • (1996) Yeast , vol.12 , pp. 1153-1162
    • Ono, B.-I.1    Kijima, K.2    Ishii, N.3    Kawato, T.4    Matsuda, A.5
  • 52
    • 0025170681 scopus 로고
    • The fungal vacuole: Composition, function, and biogenesis
    • Klionsky DJ, Herman PK, Emr SD (1990) The fungal vacuole: composition, function, and biogenesis. Microbiol Mol Biol Rev 54: 266-292.
    • (1990) Microbiol Mol Biol Rev , vol.54 , pp. 266-292
    • Klionsky, D.J.1    Herman, P.K.2    Emr, S.D.3
  • 53
    • 62949218373 scopus 로고    scopus 로고
    • The yeast lysosome-like vacuole: Endpoint and crossroads
    • Li SC, Kane PM (2009) The yeast lysosome-like vacuole: Endpoint and crossroads. Biochim Biophys Acta 1793: 650-663.
    • (2009) Biochim Biophys Acta , vol.1793 , pp. 650-663
    • Li, S.C.1    Kane, P.M.2
  • 55
    • 0024510036 scopus 로고
    • Interaction of anions and ATP with the coated vesicle proton pump
    • Arai H, Pink S, Forgac M (1989) Interaction of anions and ATP with the coated vesicle proton pump. Biochemistry 28: 3075-3082.
    • (1989) Biochemistry , vol.28 , pp. 3075-3082
    • Arai, H.1    Pink, S.2    Forgac, M.3
  • 56
    • 0019411588 scopus 로고
    • Active transport of basic amino acids driven by a proton motive force in vacuolar membrane vesicles of Saccharomyces cerevisiae
    • Ohsumi Y, Anraku Y (1981) Active transport of basic amino acids driven by a proton motive force in vacuolar membrane vesicles of Saccharomyces cerevisiae. J Biol Chem 256: 2079-2082.
    • (1981) J Biol Chem , vol.256 , pp. 2079-2082
    • Ohsumi, Y.1    Anraku, Y.2
  • 57
    • 0036052119 scopus 로고    scopus 로고
    • An overview on glutathione in Saccharomyces versus non-conventional yeasts
    • Penninckx MJ (2002) An overview on glutathione in Saccharomyces versus non-conventional yeasts. FEMS Yeast Res 2: 295-305.
    • (2002) FEMS Yeast Res , vol.2 , pp. 295-305
    • Penninckx, M.J.1
  • 58
    • 34948873616 scopus 로고    scopus 로고
    • Role of the V-ATPase in regulation of the vacuolar fission - Fusion equilibrium
    • Baars TL, Petri S, Peters C, Mayer A (2007) Role of the V-ATPase in regulation of the vacuolar fission - fusion equilibrium. Mol Biol Cell 18: 3873-3882.
    • (2007) Mol Biol Cell , vol.18 , pp. 3873-3882
    • Baars, T.L.1    Petri, S.2    Peters, C.3    Mayer, A.4
  • 59
    • 0030834977 scopus 로고    scopus 로고
    • Mutations in the CYS4 gene provide evidence for regulation of the yeast vacuolar H+-ATPase by oxidation and reduction in vivo
    • Oluwatosin YE, Kane PM (1997) Mutations in the CYS4 gene provide evidence for regulation of the yeast vacuolar H+-ATPase by oxidation and reduction in vivo. J Biol Chem 272: 28149-28157.
    • (1997) J Biol Chem , vol.272 , pp. 28149-28157
    • Oluwatosin, Y.E.1    Kane, P.M.2
  • 60
    • 0022979948 scopus 로고
    • Thiol/disulfide exchange between rabbit muscle phosphofructokinase and glutathione. Kinetics and thermodynamics of enzyme oxidation
    • Walters DW, Gilbert HF (1986) Thiol/disulfide exchange between rabbit muscle phosphofructokinase and glutathione. Kinetics and thermodynamics of enzyme oxidation. J Biol Chem 261: 15372-15377.
    • (1986) J Biol Chem , vol.261 , pp. 15372-15377
    • Walters, D.W.1    Gilbert, H.F.2
  • 61
    • 79960702245 scopus 로고    scopus 로고
    • Identification and characterization of genes involved in glutathione production in yeast
    • Suzuki T, Yokoyama A, Tsuji T, Ikeshima E, Nakashima K, et al. (2011) Identification and characterization of genes involved in glutathione production in yeast. J Biosci Bioeng 112: 107-113.
    • (2011) J Biosci Bioeng , vol.112 , pp. 107-113
    • Suzuki, T.1    Yokoyama, A.2    Tsuji, T.3    Ikeshima, E.4    Nakashima, K.5
  • 62
    • 71549134001 scopus 로고    scopus 로고
    • A genome-wide deletion mutant screen identifies pathways affected by nickel sulfate in Saccharomyces cerevisiae
    • Arita A, Zhou X, Ellen T, Liu X, Bai J, et al. (2009) A genome-wide deletion mutant screen identifies pathways affected by nickel sulfate in Saccharomyces cerevisiae. BMC Genomics 10: 524.
    • (2009) BMC Genomics , vol.10 , pp. 524
    • Arita, A.1    Zhou, X.2    Ellen, T.3    Liu, X.4    Bai, J.5


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