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Volumn 61, Issue 4, 1997, Pages 503-532

Metabolism of sulfur amino acids in Saccharomyces cerevisiae

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; GLUCOSE 6 PHOSPHATE DEHYDROGENASE; HELIX LOOP HELIX PROTEIN; HOMOCYSTEINE; HOMOSERINE; LEUCINE ZIPPER PROTEIN; METHIONINE; METHIONINE ADENOSYLTRANSFERASE; SULFITE; SULFUR AMINO ACID; SUPEROXIDE DISMUTASE; ZINC FINGER PROTEIN;

EID: 0031457095     PISSN: 10922172     EISSN: None     Source Type: Journal    
DOI: 10.1128/.61.4.503-532.1997     Document Type: Review
Times cited : (584)

References (272)
  • 1
    • 0024331502 scopus 로고
    • Cognate DNA binding specificity retained after leucine zipper exchange between GCN4 and C/ EBP
    • Agre, P., P. F. Johnson, and S. L. McKnight. 1989. Cognate DNA binding specificity retained after leucine zipper exchange between GCN4 and C/ EBP. Science 246:922-926.
    • (1989) Science , vol.246 , pp. 922-926
    • Agre, P.1    Johnson, P.F.2    McKnight, S.L.3
  • 2
    • 0029586511 scopus 로고
    • An overview of membrane transport proteins in Saccharomyces cerevisiae
    • André, B. 1995. An overview of membrane transport proteins in Saccharomyces cerevisiae. Yeast 11:1575-1611.
    • (1995) Yeast , vol.11 , pp. 1575-1611
    • André, B.1
  • 3
    • 0000852070 scopus 로고
    • Yeast sulfate reducing system. II. Enzymatic reduction of protein disulfide
    • Asahi, T., R. S. Bandurski, and L. G. Wilson. 1961. Yeast sulfate reducing system. II. Enzymatic reduction of protein disulfide. J. Biol. Chem. 236: 1830-1835.
    • (1961) J. Biol. Chem. , vol.236 , pp. 1830-1835
    • Asahi, T.1    Bandurski, R.S.2    Wilson, L.G.3
  • 4
    • 0029813691 scopus 로고    scopus 로고
    • Multicopy FZF1 (SUL1) suppresses the sulfite sensitivity but not the glucose derepression or aberrant cell morphology of a grr1 mutant of Saccharomyces cerevisiae
    • Avram, D., and A. T. Bakalinsky. 1996. Multicopy FZF1 (SUL1) suppresses the sulfite sensitivity but not the glucose derepression or aberrant cell morphology of a grr1 mutant of Saccharomyces cerevisiae. Genetics 144: 511-521.
    • (1996) Genetics , vol.144 , pp. 511-521
    • Avram, D.1    Bakalinsky, A.T.2
  • 5
    • 0019945865 scopus 로고
    • Identification of 2-keto-4-methylthiobutyrate as an intermediate compound in methionine synthesis from 5′-methylthioadenosine
    • Backlund, P. S., Jr., C. P. Chang, and R. A. Smith. 1982. Identification of 2-keto-4-methylthiobutyrate as an intermediate compound in methionine synthesis from 5′-methylthioadenosine. J. Biol. Chem. 257:4196-4202.
    • (1982) J. Biol. Chem. , vol.257 , pp. 4196-4202
    • Backlund Jr., P.S.1    Chang, C.P.2    Smith, R.A.3
  • 6
    • 0030602813 scopus 로고    scopus 로고
    • SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box
    • Bai, C., O. Sen, K. Hofmann, L. Ma, M. Goebl, J. W. Harper, and S. J. Elledge. 1996. SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box. Cell 86:263-274.
    • (1996) Cell , vol.86 , pp. 263-274
    • Bai, C.1    Sen, O.2    Hofmann, K.3    Ma, L.4    Goebl, M.5    Harper, J.W.6    Elledge, S.J.7
  • 7
    • 0024356738 scopus 로고
    • Purification of the yeast centromere binding protein CP1 and a mutational analysis of its binding site
    • Baker, R. E., M. Fitzgerald-Hayes, and T. O'Brien. 1989. Purification of the yeast centromere binding protein CP1 and a mutational analysis of its binding site. J. Biol. Chem. 264:10843-10850.
    • (1989) J. Biol. Chem. , vol.264 , pp. 10843-10850
    • Baker, R.E.1    Fitzgerald-Hayes, M.2    O'Brien, T.3
  • 8
    • 0025370208 scopus 로고
    • Isolation of the gene encoding the Saccharomyces cerevisiae centromere binding protein CP1
    • Baker, R. E., and D. C. Masison. 1990. Isolation of the gene encoding the Saccharomyces cerevisiae centromere binding protein CP1. Mol. Cell. Biol. 10:2458-2467.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 2458-2467
    • Baker, R.E.1    Masison, D.C.2
  • 9
    • 0025178838 scopus 로고
    • Characterization of yeast Vps33p, a protein required for vacuolar protein sorting and vacuole biogenesis
    • Banta, L. M., T. A. Vida, P. K. Herman, and S. D. Emr. 1990. Characterization of yeast Vps33p, a protein required for vacuolar protein sorting and vacuole biogenesis. Mol. Cell. Biol. 10:4638-4649.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 4638-4649
    • Banta, L.M.1    Vida, T.A.2    Herman, P.K.3    Emr, S.D.4
  • 10
    • 2642709806 scopus 로고    scopus 로고
    • Barbey, R., and D. Thomas. Unpublished results
    • Barbey, R., and D. Thomas. Unpublished results.
  • 11
    • 0022891719 scopus 로고
    • Molecular cloning and regulation of the expression of the MET2 gene of Saccharomyces cerevisiae
    • Baroni, M., S. Livian, E. Martegani, and L. Alberghina. 1986. Molecular cloning and regulation of the expression of the MET2 gene of Saccharomyces cerevisiae. Gene 46:71-78.
    • (1986) Gene , vol.46 , pp. 71-78
    • Baroni, M.1    Livian, S.2    Martegani, E.3    Alberghina, L.4
  • 12
    • 0028986667 scopus 로고
    • G1 cyclin turnover and nutrient uptake are controlled by a common pathway in yeast
    • Barral, Y., S. Jentsch, and C. Mann. 1995. G1 cyclin turnover and nutrient uptake are controlled by a common pathway in yeast. Genes Dev. 9:399-409.
    • (1995) Genes Dev. , vol.9 , pp. 399-409
    • Barral, Y.1    Jentsch, S.2    Mann, C.3
  • 13
    • 0027230548 scopus 로고
    • Physical localization of yeast CYS3, a gene whose product resembles the rat gamma-cystathionase and Escherichia coli cystathionine gamma-synthase enzymes
    • Barton, A. B., D. B. Kaback, M. W. Clark, T. Keng, B. F. Ouellette, R. K. Storms, B. Zeng, W. Zhong, N. Fortin, S. Delaney, and H. Bussey. 1993. Physical localization of yeast CYS3, a gene whose product resembles the rat gamma-cystathionase and Escherichia coli cystathionine gamma-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.5    Storms, R.K.6    Zeng, B.7    Zhong, W.8    Fortin, N.9    Delaney, S.10    Bussey, H.11
  • 14
    • 85085844464 scopus 로고
    • 0) metabolisation into sulfur amino acids and glutathione, from bacteria to mammalian cells
    • Swiss Society of Microbiology
    • 0) metabolisation into sulfur amino acids and glutathione, from bacteria to mammalian cells, p. 71. In Proceedings of the 48th Annual Congress, Swiss Society of Microbiology.
    • (1989) Proceedings of the 48th Annual Congress , pp. 71
    • Beffa, T.1
  • 15
    • 0028849610 scopus 로고
    • Reaction mechanism of thioredoxin: 3′-phospho-adenylylsulfate reductase investigated by site-directed mutagenesis
    • Berendt, U., T. Haverkamp, A. Prior, and J. D. Schwenn. 1995. Reaction mechanism of thioredoxin: 3′-phospho-adenylylsulfate reductase investigated by site-directed mutagenesis. Eur. J. Biochem. 233:347-356.
    • (1995) Eur. J. Biochem. , vol.233 , pp. 347-356
    • Berendt, U.1    Haverkamp, T.2    Prior, A.3    Schwenn, J.D.4
  • 16
    • 0025763419 scopus 로고
    • Max: A helix-loop-helix zipper protein that forms a sequence-specific DNA-binding complex with Myc
    • Blackwood, E. M., and R. N. Eisenman. 1991. Max: a helix-loop-helix zipper protein that forms a sequence-specific DNA-binding complex with Myc. Science 251:1211-1217.
    • (1991) Science , vol.251 , pp. 1211-1217
    • Blackwood, E.M.1    Eisenman, R.N.2
  • 17
    • 0030979616 scopus 로고    scopus 로고
    • Met31p and Met32p, two related zinc-finger proteins, are involved in transcriptional regulation of the yeast sulfur amino acid metabolism
    • Blaiseau, P. L., A. D. Isnard, Y. Surdin-Kerjan, and D. Thomas. 1997. Met31p and Met32p, two related zinc-finger proteins, are involved in transcriptional regulation of the yeast sulfur amino acid metabolism. Mol. Cell. Biol. 17:3640-3648.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 3640-3648
    • Blaiseau, P.L.1    Isnard, A.D.2    Surdin-Kerjan, Y.3    Thomas, D.4
  • 18
    • 0029026304 scopus 로고
    • Isolation and characterisation of genes for sulphate activation and reduction in Aspergillus nidulans: Implications for evolution of an allosteric control region by gene duplication
    • Borges-Walmsley, M. I., G. Turner, A. M. Bailey, J. Brown, J. Lehmbeck, and I. G. Clausen. 1995. Isolation and characterisation of genes for sulphate activation and reduction in Aspergillus nidulans: implications for evolution of an allosteric control region by gene duplication. Mol. Gen. Genet. 247: 423-429.
    • (1995) Mol. Gen. Genet. , vol.247 , pp. 423-429
    • Borges-Walmsley, M.I.1    Turner, G.2    Bailey, A.M.3    Brown, J.4    Lehmbeck, J.5    Clausen, I.G.6
  • 19
    • 0023064359 scopus 로고
    • Isolation of a Saccharomyces cerevisiae centromere DNA-binding protein, its human homolog, and its possible role as a transcription factor
    • Bram, R. J., and R. D. Kornberg. 1987. Isolation of a Saccharomyces cerevisiae centromere DNA-binding protein, its human homolog, and its possible role as a transcription factor. Mol. Cell. Biol. 7:403-409.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 403-409
    • Bram, R.J.1    Kornberg, R.D.2
  • 20
    • 0017758198 scopus 로고
    • Sulfate uptake in Saccharomyces cerevisiae: Biochemical and genetic study
    • Breton, A., and Y. Surdin-Kerjan. 1977. Sulfate uptake in Saccharomyces cerevisiae: biochemical and genetic study. J. Bacteriol. 132:224-232.
    • (1977) J. Bacteriol. , vol.132 , pp. 224-232
    • Breton, A.1    Surdin-Kerjan, Y.2
  • 21
    • 0014486406 scopus 로고
    • The substrate specificity of 5-methyltetrahydropteroyltriglutamate-homocysteine methyltransferase
    • Burton, E., J. Selhub, and W. Sakami. 1969. The substrate specificity of 5-methyltetrahydropteroyltriglutamate-homocysteine methyltransferase. Biochem. J. 111:793-795.
    • (1969) Biochem. J. , vol.111 , pp. 793-795
    • Burton, E.1    Selhub, J.2    Sakami, W.3
  • 22
    • 0015263440 scopus 로고
    • Novel mutation causing derepression of several enzymes of sulfur metabolism in Neurospora crassa
    • Burton, E. G., and R. L. Metzenberg. 1972. Novel mutation causing derepression of several enzymes of sulfur metabolism in Neurospora crassa. J. Bacteriol. 109:140-151.
    • (1972) J. Bacteriol. , vol.109 , pp. 140-151
    • Burton, E.G.1    Metzenberg, R.L.2
  • 24
    • 0026679293 scopus 로고
    • Molecular genetics of superoxide dismutases in yeasts and related fungi
    • Butler Gralla, E., and D. J. Kosman. 1992. Molecular genetics of superoxide dismutases in yeasts and related fungi. Adv. Genet. 30:251-319.
    • (1992) Adv. Genet. , vol.30 , pp. 251-319
    • Butler Gralla, E.1    Kosman, D.J.2
  • 25
    • 0023880208 scopus 로고
    • Conversion of rat liver S-adenosyl-L-methionine synthetase from high-Mr form to low-Mr form by LiBr
    • Cabrero, C., and S. Alemany. 1988. Conversion of rat liver S-adenosyl-L-methionine synthetase from high-Mr form to low-Mr form by LiBr. Biochim. Biophys. Acta 952:277-281.
    • (1988) Biochim. Biophys. Acta , vol.952 , pp. 277-281
    • Cabrero, C.1    Alemany, S.2
  • 26
    • 0023840449 scopus 로고
    • Purification and comparison of two forms of S-adenosyl-L-methionine synthetase from rat liver
    • Cabrero, C., J. Puerta, and S. Alemany. 1987. Purification and comparison of two forms of S-adenosyl-L-methionine synthetase from rat liver. Eur. J. Biochem. 170:299-304.
    • (1987) Eur. J. Biochem. , vol.170 , pp. 299-304
    • Cabrero, C.1    Puerta, J.2    Alemany, S.3
  • 27
    • 0024676036 scopus 로고
    • Purification of a yeast centromere binding protein that is able to distinguish single-base-pair mutations in its recognition site
    • Cai, M., and R. W. Davis. 1989. Purification of a yeast centromere binding protein that is able to distinguish single-base-pair mutations in its recognition site. Mol. Cell. Biol. 9:2544-2550.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 2544-2550
    • Cai, M.1    Davis, R.W.2
  • 28
    • 0025283868 scopus 로고
    • Yeast centromere binding protein CBF1, of the helix-loop-helix protein family, is required for chromosome stability and methionine prototrophy
    • Cai, M., and R. W. Davis. 1990. Yeast centromere binding protein CBF1, of the helix-loop-helix protein family, is required for chromosome stability and methionine prototrophy. Cell 61:437-146.
    • (1990) Cell , vol.61 , pp. 437-1146
    • Cai, M.1    Davis, R.W.2
  • 29
    • 0002951002 scopus 로고
    • S-adenosylmethionine: Present status and future perspectives, p. 557-577
    • F. Salvatore, E. Borek, V. Zappia, H. G. Williams-Ashman, and F. Schlenk (ed.), Columbia University Press, New York, N.Y.
    • Cantoni, G. L. 1977. S-adenosylmethionine: present status and future perspectives, p. 557-577. In F. Salvatore, E. Borek, V. Zappia, H. G. Williams-Ashman, and F. Schlenk (ed.), The biochemistry of adenosylmethionine. Columbia University Press, New York, N.Y.
    • (1977) The Biochemistry of Adenosylmethionine
    • Cantoni, G.L.1
  • 30
    • 2642704797 scopus 로고
    • Synthesis and transfer of the labile methyl group
    • W. D. McElroy and B. Glass (ed.), Johns Hopkins University Press, Baltimore, Md.
    • Cantoni, G. L. 1952. Synthesis and transfer of the labile methyl group, p. 129-149. In W. D. McElroy and B. Glass (ed.), Phosphorus metabolism, vol. II. Johns Hopkins University Press, Baltimore, Md.
    • (1952) Phosphorus Metabolism , vol.2 , pp. 129-149
    • Cantoni, G.L.1
  • 31
    • 0027953889 scopus 로고
    • Cloning and characterization of a sulphite-resistance gene of Saccharomyces cerevisiae
    • Casalone, E., C. M. Colella, S. Daly, S. Fontana, I. Torricelli, and M. Polsinelli. 1994. Cloning and characterization of a sulphite-resistance gene of Saccharomyces cerevisiae. Yeast 10:1101-1110.
    • (1994) Yeast , vol.10 , pp. 1101-1110
    • Casalone, E.1    Colella, C.M.2    Daly, S.3    Fontana, S.4    Torricelli, I.5    Polsinelli, M.6
  • 33
    • 0024654707 scopus 로고
    • Isolation and characterization of Saccharomyces cerevisiae mutants resistant to sulphite
    • Casalone, E., C. M. Colella, F. Ricci, and M. Polsinelli. 1989. Isolation and characterization of Saccharomyces cerevisiae mutants resistant to sulphite. Yeast 5:S287-S291.
    • (1989) Yeast , vol.5
    • Casalone, E.1    Colella, C.M.2    Ricci, F.3    Polsinelli, M.4
  • 34
    • 0025195232 scopus 로고
    • 2-dependent methionine auxotrophy in Cu,Zn superoxide dismutase-deficient mutants of Saccharomyces cerevisiae
    • 2-dependent methionine auxotrophy in Cu,Zn superoxide dismutase-deficient mutants of Saccharomyces cerevisiae. J. Bacteriol. 172:1840-1845.
    • (1990) J. Bacteriol. , vol.172 , pp. 1840-1845
    • Chang, E.C.1    Kosman, D.J.2
  • 35
    • 0029118563 scopus 로고
    • Demonstration that mammalian methionine synthases are predominantly cobalamin-loaded
    • Chen, Z., S. Chakraborty, and R. Banerjee. 1995. Demonstration that mammalian methionine synthases are predominantly cobalamin-loaded. J. Biol. Chem. 270:19246-19249.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19246-19249
    • Chen, Z.1    Chakraborty, S.2    Banerjee, R.3
  • 36
    • 2642706440 scopus 로고    scopus 로고
    • Personal communication
    • Cherest, H. Personal communication.
    • Cherest, H.1
  • 37
    • 0031018636 scopus 로고    scopus 로고
    • Molecular characterization of two high affinity sulfate transporters in Saccharomyces cerevisiae
    • Cherest, H., J.-C. Davidian, D. Thomas, V. Benes, W. Ansorge, and Y. Surdin-Kerjan. 1997. Molecular characterization of two high affinity sulfate transporters in Saccharomyces cerevisiae. Genetics 145:627-635.
    • (1997) Genetics , vol.145 , pp. 627-635
    • Cherest, H.1    Davidian, J.-C.2    Thomas, D.3    Benes, V.4    Ansorge, W.5    Surdin-Kerjan, Y.6
  • 38
    • 0014440241 scopus 로고
    • Genetic and regulatory aspects of methionine biosynthesis in Saccharomyces cerevisiae
    • Cherest, H., F. Eichler, and H. de Robichon-Szulmajster. 1969. Genetic and regulatory aspects of methionine biosynthesis in Saccharomyces cerevisiae. J. Bacteriol. 97:328-336.
    • (1969) J. Bacteriol. , vol.97 , pp. 328-336
    • Cherest, H.1    Eichler, F.2    De Robichon-Szulmajster, H.3
  • 39
    • 0023502858 scopus 로고
    • The Saccharomyces cerevisiae MET3 gene: Nucleotide sequence and relationships with that of MET25
    • Cherest, H., P. Kerjan, and Y. Surdin-Kerjan. 1987. The Saccharomyces cerevisiae MET3 gene: nucleotide sequence and relationships with that of MET25. Mol. Gen. Genet. 210:307-313.
    • (1987) Mol. Gen. Genet. , vol.210 , pp. 307-313
    • Cherest, H.1    Kerjan, P.2    Surdin-Kerjan, Y.3
  • 40
    • 0021836161 scopus 로고
    • Transcriptional regulation of the MET3 gene of Saccharomyces cerevisiae
    • Cherest, H., N. T. Nguyen, and Y. Surdin-Kerjan. 1985. Transcriptional regulation of the MET3 gene of Saccharomyces cerevisiae. Gene 34:269-281.
    • (1985) Gene , vol.34 , pp. 269-281
    • Cherest, H.1    Nguyen, N.T.2    Surdin-Kerjan, Y.3
  • 41
    • 0026598896 scopus 로고
    • Genetic analysis of a new mutation conferring cysteine auxotrophy in Saccharomyces cerevisiae: Updating of the sulfur metabolism pathway
    • Cherest, H., and Y. Surdin-Kerjan. 1992. Genetic analysis of a new mutation conferring cysteine auxotrophy in Saccharomyces cerevisiae: updating of the sulfur metabolism pathway. Genetics 130:51-58.
    • (1992) Genetics , vol.130 , pp. 51-58
    • Cherest, H.1    Surdin-Kerjan, Y.2
  • 42
    • 0015632377 scopus 로고
    • S-Adenosylmethionine-mediated repression of methionine biosynthetic enzymes in Saccharomyces cerevisiae
    • Cherest, H., Y. Surdin-Kerjan, J. Antoniewski, and H. de Robichon-Szulmajster. 1973. S-Adenosylmethionine-mediated repression of methionine biosynthetic enzymes in Saccharomyces cerevisiae. J. Bacteriol. 114:928-933.
    • (1973) J. Bacteriol. , vol.114 , pp. 928-933
    • Cherest, H.1    Surdin-Kerjan, Y.2    Antoniewski, J.3    De Robichon-Szulmajster, H.4
  • 43
    • 0015799624 scopus 로고
    • Effects of regulatory mutations upon methionine biosynthesis in Saccharomyces cerevisiae: Loci eth2-eth3-eth10
    • Cherest, H., Y. Surdin-Kerjan, J. Antoniewski, and H. de Robichon-Szulmajster. 1973. Effects of regulatory mutations upon methionine biosynthesis in Saccharomyces cerevisiae: loci eth2-eth3-eth10. J. Bacteriol. 115:1084-1093.
    • (1973) J. Bacteriol. , vol.115 , pp. 1084-1093
    • Cherest, H.1    Surdin-Kerjan, Y.2    Antoniewski, J.3    De Robichon-Szulmajster, H.4
  • 44
    • 0017841141 scopus 로고
    • S-adenosyl methionine requiring mutants in Saccharomyces cerevisiae: Evidences for the existence of two methionine adenosyl transferases
    • Cherest, H., Y. Surdin-Kerjan, F. Exinger, and F. Lacroute. 1978. S-adenosyl methionine requiring mutants in Saccharomyces cerevisiae: evidences for the existence of two methionine adenosyl transferases. Mol. Gen. Genet. 163:153-167.
    • (1978) Mol. Gen. Genet. , vol.163 , pp. 153-167
    • Cherest, H.1    Surdin-Kerjan, Y.2    Exinger, F.3    Lacroute, F.4
  • 45
    • 0016758399 scopus 로고
    • Methionine- And S-adenosylmethionine-mediated repression in a methionyl-transfer ribonucleic acid synthetase mutant of Saccharomyces cerevisiae
    • Cherest, H., Y. Surdin-Kerjan, and H. de Robichon-Szulmajster. 1975. Methionine-and S-adenosylmethionine-mediated repression in a methionyl-transfer ribonucleic acid synthetase mutant of Saccharomyces cerevisiae. J. Bacteriol. 123:428-435.
    • (1975) J. Bacteriol. , vol.123 , pp. 428-435
    • Cherest, H.1    Surdin-Kerjan, Y.2    De Robichon-Szulmajster, H.3
  • 46
    • 0027320121 scopus 로고
    • Cysteine biosynthesis in Saccharomyces cerevisiae occurs through the transsulfuration pathway which has been built up by enzyme recruitment
    • Cherest, H., D. Thomas, and Y. Surdin-Kerjan. 1993. Cysteine biosynthesis in Saccharomyces cerevisiae occurs through the transsulfuration pathway which has been built up by enzyme recruitment. J. Bacteriol. 175:5366-5374.
    • (1993) J. Bacteriol. , vol.175 , pp. 5366-5374
    • Cherest, H.1    Thomas, D.2    Surdin-Kerjan, Y.3
  • 47
    • 0017401520 scopus 로고
    • Activation of methionine for transmethylation. Purification of the S-adenosylmethionine synthetase of baker's yeast and its separation into two forms
    • Chiang, P. K., and G. L. Cantoni. 1977. Activation of methionine for transmethylation. Purification of the S-adenosylmethionine synthetase of baker's yeast and its separation into two forms. J. Biol. Chem. 252:4506-4513.
    • (1977) J. Biol. Chem. , vol.252 , pp. 4506-4513
    • Chiang, P.K.1    Cantoni, G.L.2
  • 48
    • 0015505466 scopus 로고
    • The mechanism of S-adenosyl-L-methionine synthesis by purified preparations of baker's yeast
    • Chou, T. C., and P. Talalay. 1972. The mechanism of S-adenosyl-L-methionine synthesis by purified preparations of baker's yeast. Biochemistry 11:1065-1073.
    • (1972) Biochemistry , vol.11 , pp. 1065-1073
    • Chou, T.C.1    Talalay, P.2
  • 49
    • 0000080389 scopus 로고
    • Contrasting responses of sulfate and phosphate transport in barley (Hordeum vulgare L.) roots to protein modifying reagents and inhibition of protein synthesis
    • Clarkson, D. T., M. J. Hawkesfors, J.-C. Davidian, and C. Grignon. 1992. Contrasting responses of sulfate and phosphate transport in barley (Hordeum vulgare L.) roots to protein modifying reagents and inhibition of protein synthesis. Planta 187:306-614.
    • (1992) Planta , vol.187 , pp. 306-614
    • Clarkson, D.T.1    Hawkesfors, M.J.2    Davidian, J.-C.3    Grignon, C.4
  • 50
    • 0001369943 scopus 로고
    • Regulation of sulphate transport in a tropical legume Macroptilium atropurpureum, cv Siratro
    • Clarkson, D. T., F. W. Smith, and P. J. Vanden Berg. 1983. Regulation of sulphate transport in a tropical legume Macroptilium atropurpureum, cv Siratro. J. Exp. Bot. 34:1463-1483.
    • (1983) J. Exp. Bot. , vol.34 , pp. 1463-1483
    • Clarkson, D.T.1    Smith, F.W.2    Vanden Berg, P.J.3
  • 51
    • 0019908039 scopus 로고
    • Utilization by Saccharomyces cerevisiae of 5′-methylthioadenosine as a source of both purine and methionine
    • Cone, M. C., K. Marchitto, B. Zehfus, and A. J. Ferro. 1982. Utilization by Saccharomyces cerevisiae of 5′-methylthioadenosine as a source of both purine and methionine. J. Bacteriol. 151:510-515.
    • (1982) J. Bacteriol. , vol.151 , pp. 510-515
    • Cone, M.C.1    Marchitto, K.2    Zehfus, B.3    Ferro, A.J.4
  • 52
    • 0030602823 scopus 로고    scopus 로고
    • Budding yeast SKP1 encodes an evolutionarily conserved kinetochore protein required for cell cycle progression
    • Connelly, C., and P. Hieter. 1996. Budding yeast SKP1 encodes an evolutionarily conserved kinetochore protein required for cell cycle progression. Cell 86:275-285.
    • (1996) Cell , vol.86 , pp. 275-285
    • Connelly, C.1    Hieter, P.2
  • 53
    • 0029891413 scopus 로고    scopus 로고
    • Affinity purification of 5-methylthioribose/S-adenosylhomocysteine nucleosidase from Klebsiella pneumoniae
    • Cornell, K. A., R. W. Winter, P. A. Tower, and M. K. Riscoe. 1996. Affinity purification of 5-methylthioribose/S-adenosylhomocysteine nucleosidase from Klebsiella pneumoniae. Biochem. J. 317:285-290.
    • (1996) Biochem. J. , vol.317 , pp. 285-290
    • Cornell, K.A.1    Winter, R.W.2    Tower, P.A.3    Riscoe, M.K.4
  • 54
    • 0029770113 scopus 로고    scopus 로고
    • A useful colony colour phenotype associated with the yeast selectable/counter-selectable marker MET15
    • Cost, G. J., and J. D. Boeke. 1996. A useful colony colour phenotype associated with the yeast selectable/counter-selectable marker MET15. Yeast 12:939-941.
    • (1996) Yeast , vol.12 , pp. 939-941
    • Cost, G.J.1    Boeke, J.D.2
  • 55
    • 0001677162 scopus 로고
    • Characteristics of sulphate transport across plasmalemma and tonoplast of carrot root cells
    • Cram, L. J. 1983. Characteristics of sulphate transport across plasmalemma and tonoplast of carrot root cells. Plant Physiol. 72:204-211.
    • (1983) Plant Physiol. , vol.72 , pp. 204-211
    • Cram, L.J.1
  • 56
    • 0022864298 scopus 로고
    • Molecular cloning and characterization of the MET6 gene of Saccharomyces cerevisiae
    • Csaikl, U., and F. Csaikl. 1986. Molecular cloning and characterization of the MET6 gene of Saccharomyces cerevisiae. Gene 46:207-214.
    • (1986) Gene , vol.46 , pp. 207-214
    • Csaikl, U.1    Csaikl, F.2
  • 57
    • 0023433803 scopus 로고
    • Mutational analysis of meiotic and mitotic centromere function in Saccharomyces cerevisiae
    • Cumberledge, S., and J. Carbon. 1987. Mutational analysis of meiotic and mitotic centromere function in Saccharomyces cerevisiae. Genetics 117:203-212.
    • (1987) Genetics , vol.117 , pp. 203-212
    • Cumberledge, S.1    Carbon, J.2
  • 58
    • 0026546825 scopus 로고
    • Discrimination between related DNA sites hy a single amino acid residue of Myc-relatcd basic-helix-loop-helix proteins
    • Dang, C. V., C. Dolde, M. L. Gillison, and G. J. Kato. 1992. Discrimination between related DNA sites hy a single amino acid residue of Myc-relatcd basic-helix-loop-helix proteins. Proc. Natl. Acad. Sci. USA 89:599-602.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 599-602
    • Dang, C.V.1    Dolde, C.2    Gillison, M.L.3    Kato, G.J.4
  • 59
    • 0015979239 scopus 로고
    • Homocysteine biosynthesis in green plants. O-phosphorylhomoserine as the physiological substrate for cystathionine gamma-synthase
    • Datko, A. H., J. Giovanelli, and S. H. Mudd. 1974. Homocysteine biosynthesis in green plants. O-phosphorylhomoserine as the physiological substrate for cystathionine gamma-synthase. J. Biol. Chem. 249:1139-1155.
    • (1974) J. Biol. Chem. , vol.249 , pp. 1139-1155
    • Datko, A.H.1    Giovanelli, J.2    Mudd, S.H.3
  • 60
    • 0001258765 scopus 로고
    • Sulfate activation and transfer
    • D. M. Greenberg (ed.). Academic Press, Inc., New York, N.Y.
    • De Meio, R. M. 1975. Sulfate activation and transfer, p. 287-358. In D. M. Greenberg (ed.). Metabolic pathways, vol. VII. Academic Press, Inc., New York, N.Y.
    • (1975) Metabolic Pathways , vol.7 , pp. 287-358
    • De Meio, R.M.1
  • 62
    • 0026656414 scopus 로고
    • The centromere and promoter factor 1 of yeast contains a dimerisation domain located carboxyterminal to the bHLH domain
    • Dowell, S. J., J. S. H. Tsang, and J. Mellor. 1992. The centromere and promoter factor 1 of yeast contains a dimerisation domain located carboxyterminal to the bHLH domain. Nucleic Acids Res. 20:4229-4236.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 4229-4236
    • Dowell, S.J.1    Tsang, J.S.H.2    Mellor, J.3
  • 63
    • 0001379243 scopus 로고
    • A hydrolytic nucleosidase acting on S-adenosylhomocysteine and on 5′-methylthioadenosine
    • Duerre, J. A. 1962. A hydrolytic nucleosidase acting on S-adenosylhomocysteine and on 5′-methylthioadenosine. J. Biol. Chem. 237:3737-3741.
    • (1962) J. Biol. Chem. , vol.237 , pp. 3737-3741
    • Duerre, J.A.1
  • 64
    • 0014423843 scopus 로고
    • In vivo and in vitro metabolism of S-adenosyl-homoserine by Saccharomyces cerevisiae
    • Duerre, J. A. 1968. In vivo and in vitro metabolism of S-adenosyl-homoserine by Saccharomyces cerevisiae. Arch. Biochem. Biophys. 124:422-430.
    • (1968) Arch. Biochem. Biophys. , vol.124 , pp. 422-430
    • Duerre, J.A.1
  • 65
    • 0028978061 scopus 로고
    • 12-independent methionine synthase from a higher plant (Catharanthus roseus). Molecular characterization, regulation, heterologous expression, and enzyme properties
    • 12-independent methionine synthase from a higher plant (Catharanthus roseus). Molecular characterization, regulation, heterologous expression, and enzyme properties. Eur. J. Biochem. 230:1053-1058.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 1053-1058
    • Eichel, J.1    Gonzalez, J.C.2    Hotze, M.3    Matthews, R.G.4    Schroder, J.5
  • 66
    • 0027049805 scopus 로고
    • The GCN4 basic region leucine zipper binds DNA as a dimer of uninterrupted alpha helices: Crystal structure of the protein-DNA complex
    • Ellenberger, T. E., C. J. Brandl, K. Struhl, and S. C. Harrison. 1992. The GCN4 basic region leucine zipper binds DNA as a dimer of uninterrupted alpha helices: crystal structure of the protein-DNA complex. Cell 71:1223-1237.
    • (1992) Cell , vol.71 , pp. 1223-1237
    • Ellenberger, T.E.1    Brandl, C.J.2    Struhl, K.3    Harrison, S.C.4
  • 67
    • 0028426943 scopus 로고
    • Differential accumulation of S-adenosylmethionine synthetase transcripts in response to salt stress
    • Espartero, J., J. A. Pintor-Toro, and J. M. Pardo. 1994. Differential accumulation of S-adenosylmethionine synthetase transcripts in response to salt stress. Plant Mol. Biol. 25:217-227.
    • (1994) Plant Mol. Biol. , vol.25 , pp. 217-227
    • Espartero, J.1    Pintor-Toro, J.A.2    Pardo, J.M.3
  • 68
    • 0021098617 scopus 로고
    • Studies of compartmentation of S-adenosylmethionine in Saccharomyces cerevisiae and isolated rat hepatocytcs
    • Farooqui, J. Z., H. W. Lee, S. Kim, and W. K. Paik. 1983. Studies of compartmentation of S-adenosylmethionine in Saccharomyces cerevisiae and isolated rat hepatocytcs. Biochim. Biophys. Acta 757:342-351.
    • (1983) Biochim. Biophys. Acta , vol.757 , pp. 342-351
    • Farooqui, J.Z.1    Lee, H.W.2    Kim, S.3    Paik, W.K.4
  • 69
    • 0018166816 scopus 로고
    • 5-Methylthioribose kinase. A new enzyme involved in the formation of methionine from 5-methylthioribose
    • Ferro, A. J., A. Barrett, and S. K. Shapiro. 1978. 5-Methylthioribose kinase. A new enzyme involved in the formation of methionine from 5-methylthioribose. J. Biol. Chem. 253:6021-6025.
    • (1978) J. Biol. Chem. , vol.253 , pp. 6021-6025
    • Ferro, A.J.1    Barrett, A.2    Shapiro, S.K.3
  • 70
    • 0020064267 scopus 로고
    • Isolation and subcloning analysis of functional centromere DNA (CEN11) from Saccharomyces cerevisiae chromosome XI
    • Fitzgerald-Hayes, M., J. M. Buhler, T. G. Cooper, and J. Carbon. 1982. Isolation and subcloning analysis of functional centromere DNA (CEN11) from Saccharomyces cerevisiae chromosome XI. Mol. Cell. Biol. 2:82-87.
    • (1982) Mol. Cell. Biol. , vol.2 , pp. 82-87
    • Fitzgerald-Hayes, M.1    Buhler, J.M.2    Cooper, T.G.3    Carbon, J.4
  • 71
    • 0000356010 scopus 로고
    • Methionine biosynthesis
    • D. M. Greenberg (ed.) Academic Press, Inc., New York, N.Y.
    • Flavin, M. 1975. Methionine biosynthesis, p. 457-503. In D. M. Greenberg (ed.) Metabolic pathways, vol. VII. Academic Press, Inc., New York, N.Y.
    • (1975) Metabolic Pathways , vol.7 , pp. 457-503
    • Flavin, M.1
  • 72
    • 0028960639 scopus 로고
    • A direct sulfhydrylation pathway is used for methionine biosynthesis in Pseudomonas aeruginosa
    • Foglino, M., F. Borne, M. Bally, G. Ball, and J. C. Patte. 1995. A direct sulfhydrylation pathway is used for methionine biosynthesis in Pseudomonas aeruginosa. Microbiology 141:431-439.
    • (1995) Microbiology , vol.141 , pp. 431-439
    • Foglino, M.1    Borne, F.2    Bally, M.3    Ball, G.4    Patte, J.C.5
  • 73
    • 0027373091 scopus 로고
    • Point mutations that separate the role of Saccharomyces cerevisiae centromere binding factor 1 in chromosome segregation from its role in transcriptional activation
    • Foreman, P. K., and R. W. Davis. 1993. Point mutations that separate the role of Saccharomyces cerevisiae centromere binding factor 1 in chromosome segregation from its role in transcriptional activation. Genetics 135: 287-296.
    • (1993) Genetics , vol.135 , pp. 287-296
    • Foreman, P.K.1    Davis, R.W.2
  • 74
    • 0028050646 scopus 로고
    • Cloning and sequencing of ATP sulfurylase from Penicillium chrysogenum. Identification of a likely allosteric domain
    • Foster, B. A., S. M. Thomas, J. A. Mahr, F. Renosto, H. C. Patel, and I. H. Segel. 1994. Cloning and sequencing of ATP sulfurylase from Penicillium chrysogenum. Identification of a likely allosteric domain. J. Biol. Chem. 269:19777-19786.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19777-19786
    • Foster, B.A.1    Thomas, S.M.2    Mahr, J.A.3    Renosto, F.4    Patel, H.C.5    Segel, I.H.6
  • 75
    • 0024636085 scopus 로고
    • cys-3, the positive-acting sulfur regulatory gene of Neurospora crassa, encodes a protein with a putative leucine zipper DNA binding element
    • Fu, Y. H., J. V. Paietta, D. G. Mannix, and G. A. Marzluf. 1989. cys-3, the positive-acting sulfur regulatory gene of Neurospora crassa, encodes a protein with a putative leucine zipper DNA binding element. Mol. Cell. Biol. 9:1120-1127.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 1120-1127
    • Fu, Y.H.1    Paietta, J.V.2    Mannix, D.G.3    Marzluf, G.A.4
  • 76
    • 0026020092 scopus 로고
    • Teast thioredoxin genes
    • Gan, Z.-R. 1991. Teast thioredoxin genes. J. Biol. Chem. 266:1692-1696.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1692-1696
    • Gan, Z.-R.1
  • 77
    • 0014319916 scopus 로고
    • Appearance of double mutants in aged cultures of Salmonella typhimurium
    • Gillespie, D., M. Demerec, and H. Itikawa. 1968. Appearance of double mutants in aged cultures of Salmonella typhimurium. Genetics 59:433-442.
    • (1968) Genetics , vol.59 , pp. 433-442
    • Gillespie, D.1    Demerec, M.2    Itikawa, H.3
  • 78
    • 0000527974 scopus 로고
    • Sulfur amino acids in plants: An overview
    • Giovanelli, J. 1987. Sulfur amino acids in plants: an overview. Methods Enzymol. 143:419-426.
    • (1987) Methods Enzymol. , vol.143 , pp. 419-426
    • Giovanelli, J.1
  • 79
    • 0012082831 scopus 로고
    • Homoserine esterification in green plants
    • Giovanelli, J., S. H. Mudd, and A. H. Datko. 1974. Homoserine esterification in green plants. Plant Physiol. 54:725-736.
    • (1974) Plant Physiol. , vol.54 , pp. 725-736
    • Giovanelli, J.1    Mudd, S.H.2    Datko, A.H.3
  • 80
    • 0014191778 scopus 로고
    • Multiplicity of the amino acid permeases in Saccharomyces cerevisiae. III. Evidence for a specific methionine-transporting system
    • Gits, J. J., and M. Grenson. 1967. Multiplicity of the amino acid permeases in Saccharomyces cerevisiae. III. Evidence for a specific methionine-transporting system. Biochim. Biophys. Acta 135:507-516.
    • (1967) Biochim. Biophys. Acta , vol.135 , pp. 507-516
    • Gits, J.J.1    Grenson, M.2
  • 81
    • 0027328991 scopus 로고
    • Salt tolerance and methionine biosynthesis in Saccharomyces cerevisiae involve a putative phosphatase gene
    • Glaser, H. U., D. Thomas, R. Gaxiola, F. Montrichard, Y. Surdin-Kerjan, and R. Serrano. 1993. Salt tolerance and methionine biosynthesis in Saccharomyces cerevisiae involve a putative phosphatase gene. EMBO J. 12: 3105-3110.
    • (1993) EMBO J. , vol.12 , pp. 3105-3110
    • Glaser, H.U.1    Thomas, D.2    Gaxiola, R.3    Montrichard, F.4    Surdin-Kerjan, Y.5    Serrano, R.6
  • 82
    • 0014939566 scopus 로고
    • The involvement of the thioredoxin system in the reduction of methionine sulfoxide and sulfate
    • Gonzalez Porque, P., A. Baldesten, and P. Reichard. 1970. The involvement of the thioredoxin system in the reduction of methionine sulfoxide and sulfate. J. Biol. Chem. 245:2371-2374.
    • (1970) J. Biol. Chem. , vol.245 , pp. 2371-2374
    • Gonzalez Porque, P.1    Baldesten, A.2    Reichard, P.3
  • 84
    • 0024300760 scopus 로고
    • Molecular cloning and characterization of the met2 gene from Ascobolus immersus
    • Goyon, C., G. Faugeron, and J. L. Rossignol. 1988. Molecular cloning and characterization of the met2 gene from Ascobolus immersus. Gene 63:297-308.
    • (1988) Gene , vol.63 , pp. 297-308
    • Goyon, C.1    Faugeron, G.2    Rossignol, J.L.3
  • 85
    • 0014528301 scopus 로고
    • Kinetic studies of the mechanism of S-adenosylmethionine synthetase from yeast
    • Greene, R. C. 1969. Kinetic studies of the mechanism of S-adenosylmethionine synthetase from yeast. Biochemistry 8:2255-2265.
    • (1969) Biochemistry , vol.8 , pp. 2255-2265
    • Greene, R.C.1
  • 86
    • 0026744318 scopus 로고
    • Human and Drosophila homeodomain proteins that enhance the DNA-binding activity of serum response factor
    • Grueneberg, D. A., S. Natesan, C. Alexandre, and M. Z. Gilman. 1992. Human and Drosophila homeodomain proteins that enhance the DNA-binding activity of serum response factor. Science 257:1089-1095.
    • (1992) Science , vol.257 , pp. 1089-1095
    • Grueneberg, D.A.1    Natesan, S.2    Alexandre, C.3    Gilman, M.Z.4
  • 87
    • 0029830772 scopus 로고    scopus 로고
    • Three members of a novel small family from Arabidopsis thaliana able to complement functionally an Escherichia coli mutant defective in PAPS reductase activity encode proteins with a thioredoxin-like domain and APS reductase activity
    • Gutierrez-Marcos, J. F., M. A. Roberts, E. I. Campbell, and J. L. Wray. 1996. Three members of a novel small family from Arabidopsis thaliana able to complement functionally an Escherichia coli mutant defective in PAPS reductase activity encode proteins with a thioredoxin-like domain and APS reductase activity. Proc. Natl. Acad. Sci. USA 93:13377-13382.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13377-13382
    • Gutierrez-Marcos, J.F.1    Roberts, M.A.2    Campbell, E.I.3    Wray, J.L.4
  • 88
    • 0031035697 scopus 로고    scopus 로고
    • Siroheme biosynthesis in Saccharomyces cerevisiae requires the products of both MET1 and METS genes
    • Hansen, J., M. Muldbjerg, H. Cherest, and Y. Surdin-Kerjan. 1997. Siroheme biosynthesis in Saccharomyces cerevisiae requires the products of both MET1 and METS genes. FEBS Lett. 401:20-24.
    • (1997) FEBS Lett. , vol.401 , pp. 20-24
    • Hansen, J.1    Muldbjerg, M.2    Cherest, H.3    Surdin-Kerjan, Y.4
  • 90
    • 0015784007 scopus 로고
    • Adenosine 5′-triphosphate sulphury-lase from Saccharomyces cerevisiae
    • Hawes, C. S., and D. Nicholas. 1973. Adenosine 5′-triphosphate sulphury-lase from Saccharomyces cerevisiae. Biochem. J. 133:541-550.
    • (1973) Biochem. J. , vol.133 , pp. 541-550
    • Hawes, C.S.1    Nicholas, D.2
  • 91
    • 0000031535 scopus 로고
    • Sulphate/proton cotransport in plasma-membrane vesicles isolated from roots of Brassica napus L.: Increased transport in membranes isolated from sulphur-starved plants
    • Hawkesford, M. J., J. C. Davidian, and C. Grignon. 1993. Sulphate/proton cotransport in plasma-membrane vesicles isolated from roots of Brassica napus L.: increased transport in membranes isolated from sulphur-starved plants. Planta 190:297-304.
    • (1993) Planta , vol.190 , pp. 297-304
    • Hawkesford, M.J.1    Davidian, J.C.2    Grignon, C.3
  • 92
    • 0027634290 scopus 로고
    • The centromere of budding yeast
    • Hegemann, J. H., and U. N. Fleig. 1993. The centromere of budding yeast. Bioessays 15:451-460.
    • (1993) Bioessays , vol.15 , pp. 451-460
    • Hegemann, J.H.1    Fleig, U.N.2
  • 94
    • 0001634436 scopus 로고
    • General and pathway-specific regulatory mechanisms controlling the synthesis of amino acid biosynthetic enzymes in Saccharomyces cerevisiae
    • E. W. Jones, J. R. Pringle and J. R. Broach (ed.). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Hinnebush, A. G. 1992. General and pathway-specific regulatory mechanisms controlling the synthesis of amino acid biosynthetic enzymes in Saccharomyces cerevisiae, p 319-414. In E. W. Jones, J. R. Pringle and J. R. Broach (ed.). The molecular and cellular biology of the yeast Saccharomyces. Gene expression. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1992) The Molecular and Cellular Biology of the Yeast Saccharomyces. Gene Expression , pp. 319-414
    • Hinnebush, A.G.1
  • 95
    • 0022551258 scopus 로고
    • Functional dissection of a eukaryotic transcriptional activator protein. GCN4 of yeast
    • Hope, I. A., and K. Struhl. 1986. Functional dissection of a eukaryotic transcriptional activator protein. GCN4 of yeast. Cell 46:885-894.
    • (1986) Cell , vol.46 , pp. 885-894
    • Hope, I.A.1    Struhl, K.2
  • 96
    • 0027284136 scopus 로고
    • Immunohistochemical analysis of rat S-adenosylmethionine synthetase isozymes in developmental liver
    • Horikawa, S., H. Ozasa, K. Ota, and K. Tsukada. 1993. Immunohistochemical analysis of rat S-adenosylmethionine synthetase isozymes in developmental liver. FEBS Lett. 330:307-311.
    • (1993) FEBS Lett. , vol.330 , pp. 307-311
    • Horikawa, S.1    Ozasa, H.2    Ota, K.3    Tsukada, K.4
  • 97
    • 0026673352 scopus 로고
    • Molecular cloning and developmental expression of a human kidney S-adenosylmethionine synthetase
    • Horikawa, S., and K. Tsukada. 1992. Molecular cloning and developmental expression of a human kidney S-adenosylmethionine synthetase. FEBS Lett. 312:37-41.
    • (1992) FEBS Lett. , vol.312 , pp. 37-41
    • Horikawa, S.1    Tsukada, K.2
  • 98
    • 0026356357 scopus 로고
    • Molecular cloning and nucleotide sequence of cDNA encoding the human liver S-adenosylmethionine synthetase
    • Horikawa, S., and K. Tsukada. 1991. Molecular cloning and nucleotide sequence of cDNA encoding the human liver S-adenosylmethionine synthetase. Biochem. Int. 25:81-90.
    • (1991) Biochem. Int. , vol.25 , pp. 81-90
    • Horikawa, S.1    Tsukada, K.2
  • 99
    • 0029828902 scopus 로고    scopus 로고
    • The yeast copper/zinc superoxide dismutase and the pentose phosphate pathway play overlapping roles in oxidative stress protection
    • Hudak Slekar, K., D. J. Kosman, and V. Cizewski Culotta. 1996. The yeast copper/zinc superoxide dismutase and the pentose phosphate pathway play overlapping roles in oxidative stress protection. J. Biol. Chem. 271:28831-28836.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28831-28836
    • Hudak Slekar, K.1    Kosman, D.J.2    Cizewski Culotta, V.3
  • 100
    • 0030568978 scopus 로고    scopus 로고
    • The study of methionine uptake in Saccharomyces cerevisiae reveals a new family of amino acid permeases
    • Isnard, A. D., D. Thomas, and Y. Surdin-Kerjan. 1996. The study of methionine uptake in Saccharomyces cerevisiae reveals a new family of amino acid permeases. J. Mol. Biol. 262:473-484.
    • (1996) J. Mol. Biol. , vol.262 , pp. 473-484
    • Isnard, A.D.1    Thomas, D.2    Surdin-Kerjan, Y.3
  • 102
    • 0027963260 scopus 로고
    • The vacuolar compartment is required for sulfur amino acid homeoslasis in Saccharomyces cerevisiae
    • Jacquemin-Faure, I., D. Thomas, J. Laporte, C. Cibert, and Y. Surdin-Kerjan. 1994. The vacuolar compartment is required for sulfur amino acid homeoslasis in Saccharomyces cerevisiae. Mol. Gen. Genet. 244:519-529.
    • (1994) Mol. Gen. Genet. , vol.244 , pp. 519-529
    • Jacquemin-Faure, I.1    Thomas, D.2    Laporte, J.3    Cibert, C.4    Surdin-Kerjan, Y.5
  • 103
    • 0027194503 scopus 로고
    • Methionione-mediated lethality in yeast cells at elevated temperature
    • Jakubowski, H., and E. Goldman. 1993. Methionione-mediated lethality in yeast cells at elevated temperature. J. Bacteriol. 175:5469-5476.
    • (1993) J. Bacteriol. , vol.175 , pp. 5469-5476
    • Jakubowski, H.1    Goldman, E.2
  • 104
    • 0024378677 scopus 로고
    • Purification of a protein binding to the CDEI subrcgion of Saccharomyces cerevisiae centromere DNA
    • Jiang, W. D., and P. Philippsen. 1989. Purification of a protein binding to the CDEI subrcgion of Saccharomyces cerevisiae centromere DNA. Mol. Cell. Biol. 9:5585-5593.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 5585-5593
    • Jiang, W.D.1    Philippsen, P.2
  • 105
    • 0028896541 scopus 로고
    • Regulation of hydrogen sulfide liberation in wine-producing Saccharomyces cerevisiae strains by assimilable nitrogen
    • Jiranek, V., P. Langridge, and P. A. Henschke. 1995. Regulation of hydrogen sulfide liberation in wine-producing Saccharomyces cerevisiae strains by assimilable nitrogen. Appl. Environ. Microbiol. 61:461-467.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 461-467
    • Jiranek, V.1    Langridge, P.2    Henschke, P.A.3
  • 106
    • 0017600514 scopus 로고
    • Proteinase mutants of Saccharomyces cerevisiae
    • Jones, E. W. 1977. Proteinase mutants of Saccharomyces cerevisiae. Genetics 85:23-33.
    • (1977) Genetics , vol.85 , pp. 23-33
    • Jones, E.W.1
  • 107
    • 0000773895 scopus 로고
    • Regulation of amino acid and nucleotide biosynthesis in yeast
    • J. N. Strathern, E. W. Jones, and J. R. Broach (ed.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Jones, E. W., and G. R. Fink. 1982. Regulation of amino acid and nucleotide biosynthesis in yeast, p. 181-299. In J. N. Strathern, E. W. Jones, and J. R. Broach (ed.), The molecular biology of the yeast Saccharomyces: metabolism and gene expression. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1982) The Molecular Biology of the Yeast Saccharomyces: Metabolism and Gene Expression , pp. 181-299
    • Jones, E.W.1    Fink, G.R.2
  • 109
    • 0028017601 scopus 로고
    • Chromatin structure modulation in Saccharomyces cerevisiae by centromere and promoter factor 1
    • Kent, N. A., J. S. H. Tsang, D. J. Crowther, and J. Mellor. 1994. Chromatin structure modulation in Saccharomyces cerevisiae by centromere and promoter factor 1. Mol. Cell. Biol. 14:5229-5241.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 5229-5241
    • Kent, N.A.1    Tsang, J.S.H.2    Crowther, D.J.3    Mellor, J.4
  • 110
    • 0023056199 scopus 로고
    • Nucleotide sequence of the Saccharomyces cerevisiae MET25 gene
    • Kerjan, P., H. Cherest, and Y. Surdin-Kerjan. 1986. Nucleotide sequence of the Saccharomyces cerevisiae MET25 gene. Nucleic Acids Res. 14:7861-7871.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 7861-7871
    • Kerjan, P.1    Cherest, H.2    Surdin-Kerjan, Y.3
  • 111
    • 0015216970 scopus 로고
    • O-Acetylhomoserine sulfhydrylase from Neurospora. Purification and consideration of its function in homocysteine and methionine synthesis
    • Kerr, D. S. 1971. O-Acetylhomoserine sulfhydrylase from Neurospora. Purification and consideration of its function in homocysteine and methionine synthesis. J. Biol. Chem. 246:95-102.
    • (1971) J. Biol. Chem. , vol.246 , pp. 95-102
    • Kerr, D.S.1
  • 112
    • 0025805267 scopus 로고
    • Nucleotide sequence, messenger RNA stability, and DNA recognition elements of cys-14, the structural gene for sulfate permeasc II in Neurospora crassa
    • Ketter, J. S., G. Jarai, Y. H. Fu, G. A. Marzluf, J. S. Ketter, G. Jarai, Y. H. Fu, and G. A. Marzluf. 1991. Nucleotide sequence, messenger RNA stability, and DNA recognition elements of cys-14, the structural gene for sulfate permeasc II in Neurospora crassa. Biochemistry 30:1780-1787.
    • (1991) Biochemistry , vol.30 , pp. 1780-1787
    • Ketter, J.S.1    Jarai, G.2    Fu, Y.H.3    Marzluf, G.A.4    Ketter, J.S.5    Jarai, G.6    Fu, Y.H.7    Marzluf, G.A.8
  • 113
    • 0028073155 scopus 로고
    • Control of cellular morphogenesis by the Ip12/Bem2 GTPase-activating protein: Possible role of protein phosphorylation
    • Kim, Y. J., L. Francisco, G. C. Chen, E. Marcotte, and C. S. Chan. 1994. Control of cellular morphogenesis by the Ip12/Bem2 GTPase-activating protein: possible role of protein phosphorylation. J. Cell Biol. 127:1381-1394.
    • (1994) J. Cell Biol. , vol.127 , pp. 1381-1394
    • Kim, Y.J.1    Francisco, L.2    Chen, G.C.3    Marcotte, E.4    Chan, C.S.5
  • 114
    • 0024023150 scopus 로고
    • Mutants of Saccharomyces cerevisiae with defective vacuolar function
    • Kitamoto, K., K. Yoshizawa, Y. Oshumi, and Y. Anraku. 1988. Mutants of Saccharomyces cerevisiae with defective vacuolar function. Mol. Cell. Biol. 170:2687-2691.
    • (1988) Mol. Cell. Biol. , vol.170 , pp. 2687-2691
    • Kitamoto, K.1    Yoshizawa, K.2    Oshumi, Y.3    Anraku, Y.4
  • 115
    • 0025170681 scopus 로고
    • The fungal vacuole: Composition, function, and biogenesis
    • Klionskv, D. J., P. K. Herman, and S. D. Emr. 1990. The fungal vacuole: composition, function, and biogenesis. Microbiol. Rev. 54:266-292.
    • (1990) Microbiol. Rev. , vol.54 , pp. 266-292
    • Klionskv, D.J.1    Herman, P.K.2    Emr, S.D.3
  • 116
    • 0028173842 scopus 로고
    • Isolation and characterization of two cDNA clones encoding ATP-sulfurylases from potato by complementation of a yeast mutant
    • Klonus, D., R. Hofgen, L. Willmitzer, and J. W. Riesmeier. 1994. Isolation and characterization of two cDNA clones encoding ATP-sulfurylases from potato by complementation of a yeast mutant. Plant J. 6:105-112.
    • (1994) Plant J. , vol.6 , pp. 105-112
    • Klonus, D.1    Hofgen, R.2    Willmitzer, L.3    Riesmeier, J.W.4
  • 117
    • 0029243157 scopus 로고
    • A cDNA clone for an ATP-sulfurylase from Arabidopsis thaliana
    • Klonus, D., J. W. Riesmeier, and L. Willmitzer. 1995. A cDNA clone for an ATP-sulfurylase from Arabidopsis thaliana. Plant Physiol. 107:653-654.
    • (1995) Plant Physiol. , vol.107 , pp. 653-654
    • Klonus, D.1    Riesmeier, J.W.2    Willmitzer, L.3
  • 118
    • 0014518844 scopus 로고
    • Uptake and utilization of S-adenosyl-L-methionine and S-adenosyl-L-homocysteine in an adenine mutant of Saccharomyces cerevisiae
    • Knudsen, R. C., K. Moore, and I. Yall. 1969. Uptake and utilization of S-adenosyl-L-methionine and S-adenosyl-L-homocysteine in an adenine mutant of Saccharomyces cerevisiae. J. Bacteriol. 98:629-636.
    • (1969) J. Bacteriol. , vol.98 , pp. 629-636
    • Knudsen, R.C.1    Moore, K.2    Yall, I.3
  • 119
    • 0015419788 scopus 로고
    • Partial purification and characterization of S-adenosylhomocysteine hydrolase isolated from Saccharomyces cerevisiae
    • Knudsen, R. C., and I. Yall. 1972. Partial purification and characterization of S-adenosylhomocysteine hydrolase isolated from Saccharomyces cerevisiae. J. Bacteriol. 112:569-575.
    • (1972) J. Bacteriol. , vol.112 , pp. 569-575
    • Knudsen, R.C.1    Yall, I.2
  • 120
    • 0020479448 scopus 로고
    • Studies on yeast sulfite reductase. IV. Structure and steady-state kinetics
    • Kobayashi, K., and A. Yoshimoto. 1982. Studies on yeast sulfite reductase. IV. Structure and steady-state kinetics. Biochim. Biophys. Acta 705:348-356.
    • (1982) Biochim. Biophys. Acta , vol.705 , pp. 348-356
    • Kobayashi, K.1    Yoshimoto, A.2
  • 121
    • 0020476471 scopus 로고
    • Studies on yeast sulfite reductase. V. Effects of ionic strength on enzyme activities
    • Kobayashi, K., and A. Yoshimoto. 1982. Studies on yeast sulfite reductase. V. Effects of ionic strength on enzyme activities. Biochim. Biophys. Acta 709:38-45.
    • (1982) Biochim. Biophys. Acta , vol.709 , pp. 38-45
    • Kobayashi, K.1    Yoshimoto, A.2
  • 122
    • 0020476453 scopus 로고
    • Studies on yeast sulfite reductase. VI. Use of the effects of ionic strength as a probe for enzyme structure and mechanism
    • Kobayashi, K., and A. Yoshimoto. 1982. Studies on yeast sulfite reductase. VI. Use of the effects of ionic strength as a probe for enzyme structure and mechanism. Biochim. Biophys. Acta 709:46-52.
    • (1982) Biochim. Biophys. Acta , vol.709 , pp. 46-52
    • Kobayashi, K.1    Yoshimoto, A.2
  • 123
    • 0028034201 scopus 로고
    • The WD repeats of Tup1 interact with the homeo domain protein a2
    • Komachi, K., M. J. Redd, and A. D. Johnson. 1995. The WD repeats of Tup1 interact with the homeo domain protein a2. Genes Dev. 8:2857-2867.
    • (1995) Genes Dev. , vol.8 , pp. 2857-2867
    • Komachi, K.1    Redd, M.J.2    Johnson, A.D.3
  • 124
    • 2642682980 scopus 로고    scopus 로고
    • Personal communication
    • Korch, C. Personal communication.
    • Korch, C.1
  • 125
    • 0025915688 scopus 로고
    • Cloning, nucleotide sequence and regulation of MET14, the gene encoding the APS kinase of Saccharomyces cerevisiae
    • Korch, C., H. A. Mountain, and A. S. Byström. 1991. Cloning, nucleotide sequence and regulation of MET14, the gene encoding the APS kinase of Saccharomyces cerevisiae. Mol. Gen. Genet. 228:96-108.
    • (1991) Mol. Gen. Genet. , vol.228 , pp. 96-108
    • Korch, C.1    Mountain, H.A.2    Byström, A.S.3
  • 127
    • 0000527976 scopus 로고
    • Biosynthesis of cysteine
    • F. C. Niedhardt, J. L. Ingraham, K. B. Low, B. Magasanik, M. Schaechter, and H. E. Umbarger (ed.), American Society for Microbiology, Washington, D.C.
    • Kredich, N. M. 1987. Biosynthesis of cysteine, p. 419-428. In F. C. Niedhardt, J. L. Ingraham, K. B. Low, B. Magasanik, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella typhimurium: cellular and molecular biology. American Society for Microbiology, Washington, D.C.
    • (1987) Escherichia Coli and Salmonella Typhimurium: Cellular and Molecular Biology , pp. 419-428
    • Kredich, N.M.1
  • 128
    • 0026738588 scopus 로고
    • The molecular basis for positive regulation of cys promoters in Salmonella typhimurium and Escherichia coli
    • Kredich, N. M. 1992. The molecular basis for positive regulation of cys promoters in Salmonella typhimurium and Escherichia coli. Mol. Microbiol. 6:2747-2753.
    • (1992) Mol. Microbiol. , vol.6 , pp. 2747-2753
    • Kredich, N.M.1
  • 129
    • 0028906080 scopus 로고
    • Mutants of Saccharomyces cerevisiae sensitive to oxidative and osmotic stress
    • Krems, B., C. Charizanis, and K.-D. Entian. 1995. Mutants of Saccharomyces cerevisiae sensitive to oxidative and osmotic stress. Curr. Genet. 27:427-434.
    • (1995) Curr. Genet. , vol.27 , pp. 427-434
    • Krems, B.1    Charizanis, C.2    Entian, K.-D.3
  • 130
    • 2642671720 scopus 로고    scopus 로고
    • Personal communication
    • Kruger, W. D. Personal communication.
    • Kruger, W.D.1
  • 131
    • 0028198781 scopus 로고
    • A yeast system for expression of human cystathionine beta-synthase: Structural and functional conservation of the human and yeast genes
    • Kruger, W. D., and D. R. Cox. 1994. A yeast system for expression of human cystathionine beta-synthase: structural and functional conservation of the human and yeast genes. Proc. Natl. Acad. Sci. USA 91:6614-6618.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 6614-6618
    • Kruger, W.D.1    Cox, D.R.2
  • 132
    • 0029045384 scopus 로고
    • A yeast assay for functional detection of mutations in the human cystathionine beta-synthase gene
    • Kruger, W. D., and D. R. Cox. 1995. A yeast assay for functional detection of mutations in the human cystathionine beta-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
  • 133
    • 0028910319 scopus 로고
    • The sulfur controller-2 negative regulatory eene of Neurospora crassa encodes a protein with β-transducin repeats
    • Kumar, A., and J. V. Paietta. 1995. The sulfur controller-2 negative regulatory eene of Neurospora crassa encodes a protein with β-transducin repeats. Proc. Natl. Acad. Sci. USA 92:3343-3347.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3343-3347
    • Kumar, A.1    Paietta, J.V.2
  • 134
    • 0030925073 scopus 로고    scopus 로고
    • Assembly of a bZIP/bHLH transcription activation complex: Formation of the yeast Cbf1/Met4/Met28 complex is regulated through Met28 stimulation of Cbf1 DNA binding
    • Kuras, L., R. Barbey, and D. Thomas. 1997. Assembly of a bZIP/bHLH transcription activation complex: formation of the yeast Cbf1/Met4/Met28 complex is regulated through Met28 stimulation of Cbf1 DNA binding. EMBO J. 16:2441-2451.
    • (1997) EMBO J. , vol.16 , pp. 2441-2451
    • Kuras, L.1    Barbey, R.2    Thomas, D.3
  • 135
    • 0029944825 scopus 로고    scopus 로고
    • A heteromeric complex containing the centromere binding factor 1 and two basic leucinc zipper factors, Met4 and Met28, mediates the transcription activation of yeast sulfur metabolism
    • Kuras, L., H. Cherest, Y. Surdin-Kerjan, and D. Thomas. 1996. A heteromeric complex containing the centromere binding factor 1 and two basic leucinc zipper factors, Met4 and Met28, mediates the transcription activation of yeast sulfur metabolism. EMBO J. 15:2519-2529.
    • (1996) EMBO J. , vol.15 , pp. 2519-2529
    • Kuras, L.1    Cherest, H.2    Surdin-Kerjan, Y.3    Thomas, D.4
  • 136
    • 0028936193 scopus 로고
    • Functional analysis of Met4, a yeast transcriptional activator responsive to S-adenosylmethionine
    • Kuras, L., and D. Thomas. 1995. Functional analysis of Met4, a yeast transcriptional activator responsive to S-adenosylmethionine. Mol. Cell. Biol. 15:208-216.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 208-216
    • Kuras, L.1    Thomas, D.2
  • 137
    • 0029018651 scopus 로고
    • Identification of the yeast methionine biosynthetic genes that require the centromere factor 1 for their transcriptional activation
    • Kuras, L., and D. Thomas. 1995. Identification of the yeast methionine biosynthetic genes that require the centromere factor 1 for their transcriptional activation. FEBS Lett. 367:15-18.
    • (1995) FEBS Lett. , vol.367 , pp. 15-18
    • Kuras, L.1    Thomas, D.2
  • 138
    • 2642703181 scopus 로고    scopus 로고
    • Kuras, L., and D. Thomas. Unpublished results
    • Kuras, L., and D. Thomas. Unpublished results.
  • 139
    • 0024295767 scopus 로고
    • The leucine zipper: A hypothetical structure common to a new class of DNA binding proteins
    • Landschulz, W. H., P. F. Johnson, and S. L. McKnight. 1988. The leucine zipper: a hypothetical structure common to a new class of DNA binding proteins. Science 240:1759-1764.
    • (1988) Science , vol.240 , pp. 1759-1764
    • Landschulz, W.H.1    Johnson, P.F.2    McKnight, S.L.3
  • 140
    • 0022895249 scopus 로고
    • The MET2 gene of Saccharomyces cerevisiae: Molecular cloning and nucleotide sequence
    • Langin, T., G. Faugeron, C. Goyon, A. Nicolas, and J. L. Rossignol. 1986. The MET2 gene of Saccharomyces cerevisiae: molecular cloning and nucleotide sequence. Gene 49:283-293.
    • (1986) Gene , vol.49 , pp. 283-293
    • Langin, T.1    Faugeron, G.2    Goyon, C.3    Nicolas, A.4    Rossignol, J.L.5
  • 141
    • 0003002607 scopus 로고
    • Evidence for proton-sulfate cotransport and its kinetics in Lemna gibba GI
    • Lass, B., and C. I. Ullrich-Eberius. 1984. Evidence for proton-sulfate cotransport and its kinetics in Lemna gibba GI. Planta 161:53-60.
    • (1984) Planta , vol.161 , pp. 53-60
    • Lass, B.1    Ullrich-Eberius, C.I.2
  • 142
    • 0029910712 scopus 로고    scopus 로고
    • Dual requirement for the yeast MMS19 gene in DNA repair and RNA polymerase II transcription
    • Lauder, S., M. Bankmann, S. N. Guzder, P. Sung, L. Prakash, and S. Prakash. 1996. Dual requirement for the yeast MMS19 gene in DNA repair and RNA polymerase II transcription. Mol. Cell. Biol. 16:6783-6793.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6783-6793
    • Lauder, S.1    Bankmann, M.2    Guzder, S.N.3    Sung, P.4    Prakash, L.5    Prakash, S.6
  • 143
    • 0001246177 scopus 로고
    • Selectivity and kinetics of ion uptake by barley plants following nutrient deficiency
    • Lee, R. B. 1982. Selectivity and kinetics of ion uptake by barley plants following nutrient deficiency. Ann. Bot. 50:429-449.
    • (1982) Ann. Bot. , vol.50 , pp. 429-449
    • Lee, R.B.1
  • 144
    • 0028466132 scopus 로고
    • Cloning of a cDNA encoding ATP sulfurylase from Arabidopsis thaliana by functional expression in Saccharomyces cerevisiae
    • Leustek, T., M. Murillo, and M. Cervantes. 1994. Cloning of a cDNA encoding ATP sulfurylase from Arabidopsis thaliana by functional expression in Saccharomyces cerevisiae. Plant Physiol. 105:897-902.
    • (1994) Plant Physiol. , vol.105 , pp. 897-902
    • Leustek, T.1    Murillo, M.2    Cervantes, M.3
  • 145
    • 0026728801 scopus 로고
    • Non dissociation of GAL4 and GAL80 in vivo after galactose induction
    • Leuther, K. K., and S. A. Johnston. 1992. Non dissociation of GAL4 and GAL80 in vivo after galactose induction. Science 256:1333-1335.
    • (1992) Science , vol.256 , pp. 1333-1335
    • Leuther, K.K.1    Johnston, S.A.2
  • 146
    • 0027757048 scopus 로고
    • The physical biochemistry and molecular genetics of sulfate activation
    • Leyh, T. S. 1993. The physical biochemistry and molecular genetics of sulfate activation. Crit. Rev. Biochem. Mol. Biol. 28:515-542.
    • (1993) Crit. Rev. Biochem. Mol. Biol. , vol.28 , pp. 515-542
    • Leyh, T.S.1
  • 147
    • 0026556956 scopus 로고
    • GTPase-mediated activation of ATP sulfurylase
    • Leyh, T. S., and Y. Suo. 1992. GTPase-mediated activation of ATP sulfurylase. J. Biol. Chem. 267:542-545.
    • (1992) J. Biol. Chem. , vol.267 , pp. 542-545
    • Leyh, T.S.1    Suo, Y.2
  • 148
    • 0026697593 scopus 로고
    • The DNA sequence of the sulfate activation locus from Escherichia coli K-12
    • Leyh, T. S., T. F. Vogt, and Y. Suo. 1992. The DNA sequence of the sulfate activation locus from Escherichia coli K-12. J. Biol. Chem. 267:10405-10410.
    • (1992) J. Biol. Chem. , vol.267 , pp. 10405-10410
    • Leyh, T.S.1    Vogt, T.F.2    Suo, Y.3
  • 149
    • 0028786032 scopus 로고
    • The isolation and characterization of cDNA encoding the mouse bifunctional ATP sulfurylase-adenosine 5′-phosphosulfate kinase
    • Li, H., A. Deyrup, J. R. Mensch, Jr., M. Domowicz, A. K. Konstantinidis, and N. B. Schwartz. 1995. The isolation and characterization of cDNA encoding the mouse bifunctional ATP sulfurylase-adenosine 5′-phosphosulfate kinase. J. Biol. Chem. 270:29453-29459.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29453-29459
    • Li, H.1    Deyrup, A.2    Mensch Jr., J.R.3    Domowicz, M.4    Konstantinidis, A.K.5    Schwartz, N.B.6
  • 150
    • 0029819090 scopus 로고    scopus 로고
    • Determination of the Neurospora crassa Cys3 sulfur regulatory protein consensus DNA binding site: Amino acid substitutions in the Cys3 bZIP domain that alter DNA-binding specificity
    • Li, Q., and G. A. Marzulf. 1996. Determination of the Neurospora crassa Cys3 sulfur regulatory protein consensus DNA binding site: amino acid substitutions in the Cys3 bZIP domain that alter DNA-binding specificity. Curr. Genet. 30:298-304.
    • (1996) Curr. Genet. , vol.30 , pp. 298-304
    • Li, Q.1    Marzulf, G.A.2
  • 151
    • 0029585125 scopus 로고
    • Amino-terminal protein processing in Saccharomyces cerevisiae is an essential function that requires two distinct methionine aminopeptidases
    • Li, X., and Y. H. Chang. 1995. Amino-terminal protein processing in Saccharomyces cerevisiae is an essential function that requires two distinct methionine aminopeptidases. Proc. Natl. Acad. Sci. USA 92:12357-12361.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 12357-12361
    • Li, X.1    Chang, Y.H.2
  • 152
    • 0028271645 scopus 로고
    • GTPase activation of ATP sulfurylase: The mechanism
    • Liu, C., E. Martin, and T. S. Leyh. 1994. GTPase activation of ATP sulfurylase: the mechanism. Biochemistry 33:2042-2047.
    • (1994) Biochemistry , vol.33 , pp. 2042-2047
    • Liu, C.1    Martin, E.2    Leyh, T.S.3
  • 153
    • 0028363648 scopus 로고
    • The energetic linkage of GTP hydrolysis and the synthesis of activated sulfate
    • Liu, C., Y. Suo, and T. S. Leyh. 1994. The energetic linkage of GTP hydrolysis and the synthesis of activated sulfate. Biochemistry 33:7309-7314.
    • (1994) Biochemistry , vol.33 , pp. 7309-7314
    • Liu, C.1    Suo, Y.2    Leyh, T.S.3
  • 154
    • 0020069233 scopus 로고
    • Pentose phosphate pathway mutants of yeast
    • Lobo, Z., and P. K. Maitra. 1982. Pentose phosphate pathway mutants of yeast. Mol. Gen. Genet. 185:367-368.
    • (1982) Mol. Gen. Genet. , vol.185 , pp. 367-368
    • Lobo, Z.1    Maitra, P.K.2
  • 155
    • 15844395948 scopus 로고    scopus 로고
    • Cloning of a cDNA encoded by a member of the Arabidopsis thaliana ATP sulfurylase multigene family. Expression studies in yeast and in relation to plant sulfur nutrition
    • Logan, H. M., N. Cathala, C. Grignon, and J. C. Davidian. 1996. Cloning of a cDNA encoded by a member of the Arabidopsis thaliana ATP sulfurylase multigene family. Expression studies in yeast and in relation to plant sulfur nutrition. J. Biol. Chem. 271:12227-12233.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12227-12233
    • Logan, H.M.1    Cathala, N.2    Grignon, C.3    Davidian, J.C.4
  • 157
    • 0028335104 scopus 로고
    • Intermediate channeling between ATP sulfurylase and adenosine 5′-phosphosulfate kinase from rat chondrosarcoma
    • Lyle, S., J. D. Ozeran, J. Stanczak, J. Westley, and N. B. Schwartz. 1994. Intermediate channeling between ATP sulfurylase and adenosine 5′-phosphosulfate kinase from rat chondrosarcoma. Biochemistry 33:6822-6827.
    • (1994) Biochemistry , vol.33 , pp. 6822-6827
    • Lyle, S.1    Ozeran, J.D.2    Stanczak, J.3    Westley, J.4    Schwartz, N.B.5
  • 158
    • 0028357714 scopus 로고
    • Rat chondrosarcoma ATP sulfurylase and adenosine 5′-phosphosulfate kinase reside on a single bifunctional protein
    • Lyle, S., J. Stanczak, K. Ng, and N. B. Schwartz. 1994. Rat chondrosarcoma ATP sulfurylase and adenosine 5′-phosphosulfate kinase reside on a single bifunctional protein. Biochemistry 33:5920-5925.
    • (1994) Biochemistry , vol.33 , pp. 5920-5925
    • Lyle, S.1    Stanczak, J.2    Ng, K.3    Schwartz, N.B.4
  • 159
    • 0028899388 scopus 로고
    • Sulfate-activating enzymes in normal and brachymorphic mice: Evidence for a channelling defect
    • Lyle, S., J. D. Stanczak, J. Westley, and N. B. Schwartz. 1995. Sulfate-activating enzymes in normal and brachymorphic mice: evidence for a channelling defect. Biochemistry 34:940-945.
    • (1995) Biochemistry , vol.34 , pp. 940-945
    • Lyle, S.1    Stanczak, J.D.2    Westley, J.3    Schwartz, N.B.4
  • 160
    • 0015997633 scopus 로고
    • Transport and toxicity of sulfur dioxide in Saccharomyces cerevisiae var. ellipsoidus
    • Macris, B. J., and P. Markakis. 1974. Transport and toxicity of sulfur dioxide in Saccharomyces cerevisiae var. ellipsoidus. J. Sci. Food Agric. 25:21-29.
    • (1974) J. Sci. Food Agric. , vol.25 , pp. 21-29
    • Macris, B.J.1    Markakis, P.2
  • 161
    • 0029157608 scopus 로고
    • A 43.5 kb segment of yeast chromosome XIV, which contains MFA2, MEP2, CAP.SRV2, NAM9, FKB1/FPR1/RBP1, MOM22 and CPT1, predicts an adenosine deaminase gene and 14 new open reading frames
    • Mallet, L., F. Bussereau, and M. Jacquet. 1995. A 43.5 kb segment of yeast chromosome XIV, which contains MFA2, MEP2, CAP.SRV2, NAM9, FKB1/FPR1/RBP1, MOM22 and CPT1, predicts an adenosine deaminase gene and 14 new open reading frames. Yeast 11:1195-1200.
    • (1995) Yeast , vol.11 , pp. 1195-1200
    • Mallet, L.1    Bussereau, F.2    Jacquet, M.3
  • 162
    • 0024369757 scopus 로고
    • Dimorphism in Histoplasma capsulatum: A model for the study of cell differentiation in pathogenic fungi
    • Maresca, B., and G. S. Kobayashi. 1989. Dimorphism in Histoplasma capsulatum: a model for the study of cell differentiation in pathogenic fungi. Microbiol. Rev. 53:186-209.
    • (1989) Microbiol. Rev. , vol.53 , pp. 186-209
    • Maresca, B.1    Kobayashi, G.S.2
  • 163
    • 0021718029 scopus 로고
    • The sequence of metK, the structural gene for S-adenosylmethionine synthetase in Escherichia coli
    • Markham, G. D., J. DeParasis, and J. Gatmaitan. 1984. The sequence of metK, the structural gene for S-adenosylmethionine synthetase in Escherichia coli. J. Biol. Chem. 259:14505-14507.
    • (1984) J. Biol. Chem. , vol.259 , pp. 14505-14507
    • Markham, G.D.1    Deparasis, J.2    Gatmaitan, J.3
  • 164
    • 0023303177 scopus 로고
    • Adenosine deaminase from Saccharomyces cerevisiae: Purification and characterization
    • Marmocchi, F., G. Lupidi, G. Venardi, and F. Riva. 1987. Adenosine deaminase from Saccharomyces cerevisiae: purification and characterization. Biochem. Int. 14:569-80.
    • (1987) Biochem. Int. , vol.14 , pp. 569-580
    • Marmocchi, F.1    Lupidi, G.2    Venardi, G.3    Riva, F.4
  • 165
    • 0027382484 scopus 로고
    • Regulation of sulfur and nitrogen metabolism in filamentous fungi
    • Marzluf, G. A. 1993. Regulation of sulfur and nitrogen metabolism in filamentous fungi. Annu. Rev. Microhiol. 47:31-55.
    • (1993) Annu. Rev. Microhiol. , vol.47 , pp. 31-55
    • Marzluf, G.A.1
  • 166
    • 0027305378 scopus 로고
    • Mutational analysis of the Saccharomyces cerevisiae general regulatory factor CP1
    • Masison, D. C., K. F. O'Connell, and R. Baker. 1993. Mutational analysis of the Saccharomyces cerevisiae general regulatory factor CP1. Nucleic Acids Res. 21:4133-4141.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 4133-4141
    • Masison, D.C.1    O'Connell, K.F.2    Baker, R.3
  • 167
    • 0016823338 scopus 로고
    • Methionine biosynthesis in Saccharomyces cerevisiae. I. Genetical analysis of auxotrophic mutants
    • Masselot, M., and H. De Robichon-Szulmajster. 1975. Methionine biosynthesis in Saccharomyces cerevisiae. I. Genetical analysis of auxotrophic mutants. Mol. Gen. Genet. 139:121-132.
    • (1975) Mol. Gen. Genet. , vol.139 , pp. 121-132
    • Masselot, M.1    De Robichon-Szulmajster, H.2
  • 168
    • 0017375851 scopus 로고
    • Methionine biosynthesis in Saccharomyces cerevisiae. II. Gene-enzyme relationships in the sulfate assimilation pathway
    • Masselot, M., and Y. Surdin-Kerjan. 1977. Methionine biosynthesis in Saccharomyces cerevisiae. II. Gene-enzyme relationships in the sulfate assimilation pathway. Mol. Gen. Genet. 154:23-30.
    • (1977) Mol. Gen. Genet. , vol.154 , pp. 23-30
    • Masselot, M.1    Surdin-Kerjan, Y.2
  • 169
    • 0028795797 scopus 로고
    • Cloning of yeast HAP5: A novel subunit of a heterotrimeric complex required for CCAAT binding
    • McNabb, D. S., Y. Xing, and L. Guarente. 1995. Cloning of yeast HAP5: a novel subunit of a heterotrimeric complex required for CCAAT binding. Genes Dev. 9:47-58.
    • (1995) Genes Dev. , vol.9 , pp. 47-58
    • McNabb, D.S.1    Xing, Y.2    Guarente, L.3
  • 170
    • 0023521255 scopus 로고
    • Bicarbonate sulfate exchange in canalicular rat liver plasma membrane vesicles
    • Meier, P. J., J. Valentinas, G. Hugentobler, and I. Rahm. 1987. Bicarbonate sulfate exchange in canalicular rat liver plasma membrane vesicles. Am. J. Physiol. 253:G461-G468.
    • (1987) Am. J. Physiol. , vol.253
    • Meier, P.J.1    Valentinas, J.2    Hugentobler, G.3    Rahm, I.4
  • 172
    • 0025892340 scopus 로고
    • DNA binding of CPF1 is required for optimal centromere function but not for maintaining methionine prototrophy in yeast
    • Erratum. 19:5112
    • Mellor, J., J. Rathjen, W. Jiang, C. A. Barnes, and S. J. Dowell. 1991. DNA binding of CPF1 is required for optimal centromere function but not for maintaining methionine prototrophy in yeast. Nucleic Acids Res. 19:2961-2969. (Erratum. 19:5112.)
    • (1991) Nucleic Acids Res. , vol.19 , pp. 2961-2969
    • Mellor, J.1    Rathjen, J.2    Jiang, W.3    Barnes, C.A.4    Dowell, S.J.5
  • 173
    • 0025200973 scopus 로고
    • The specificities of yeast methionine aminopeptidase and acetylation of aminoterminal methionine in vivo. Processing of altered iso-1-cytochromes c created by oligonucleotide transformation
    • Moerschell, R. P., Y. Hosokawa, S. Tsunasawa, and F. Sherman. 1990. The specificities of yeast methionine aminopeptidase and acetylation of aminoterminal methionine in vivo. Processing of altered iso-1-cytochromes c created by oligonucleotide transformation. J. Biol. Chem. 265:19638-19643.
    • (1990) J. Biol. Chem. , vol.265 , pp. 19638-19643
    • Moerschell, R.P.1    Hosokawa, Y.2    Tsunasawa, S.3    Sherman, F.4
  • 174
    • 0026761411 scopus 로고
    • Genetic and physical maps of Saccharomyces cerevisiae, edition 11
    • Mortimer, R. K., C. R. Contopoulou, and J. S. King. 1992. Genetic and physical maps of Saccharomyces cerevisiae, edition 11. Yeast 8:817-902.
    • (1992) Yeast , vol.8 , pp. 817-902
    • Mortimer, R.K.1    Contopoulou, C.R.2    King, J.S.3
  • 175
    • 0027393364 scopus 로고
    • The general amino acid control regulates MET4, which encodes a methionine-pathway-specific transcriptional activator of Saccharomyces cerevisiae
    • Erratum, 9:221-223
    • Mountain, H. A., A. S. Bystrom, and C. Korch. 1993. The general amino acid control regulates MET4, which encodes a methionine-pathway-specific transcriptional activator of Saccharomyces cerevisiae. Mol. Microbiol. 7: 215-228. (Erratum, 9:221-223.)
    • (1993) Mol. Microbiol. , vol.7 , pp. 215-228
    • Mountain, H.A.1    Bystrom, A.S.2    Korch, C.3
  • 176
    • 0025931525 scopus 로고
    • Four major transcriptional responses in the methionine/threonine biosynthetic pathway of Saccharomyces cerevisiae
    • Mountain, H. A., A. S. Byström, J. Tang Larsen, and C. Korch. 1991. Four major transcriptional responses in the methionine/threonine biosynthetic pathway of Saccharomyces cerevisiae. Yeast 7:781-803.
    • (1991) Yeast , vol.7 , pp. 781-803
    • Mountain, H.A.1    Byström, A.S.2    Tang Larsen, J.3    Korch, C.4
  • 177
    • 0026043061 scopus 로고
    • TDH2 is linked to MET3 on chromosome X of Saccharomyces cerevisiae
    • Mountain, H. A., and C. Korch. 1991. TDH2 is linked to MET3 on chromosome X of Saccharomyces cerevisiae. Yeast 7:873-80.
    • (1991) Yeast , vol.7 , pp. 873-880
    • Mountain, H.A.1    Korch, C.2
  • 178
    • 0009829447 scopus 로고
    • Activation of methionine for transmethylation. VI. Enzyme bound tripolyphosphate as an intermediate in the reaction catalysed by the methionine activating enzyme of baker's yeast
    • Mudd, S. H. 1963. Activation of methionine for transmethylation. VI. Enzyme bound tripolyphosphate as an intermediate in the reaction catalysed by the methionine activating enzyme of baker's yeast. J. Biol. Chem. 238:2156-2163.
    • (1963) J. Biol. Chem. , vol.238 , pp. 2156-2163
    • Mudd, S.H.1
  • 179
    • 0025740886 scopus 로고
    • Thioredoxin deficiency in yeast prolongs S phase and shortens the G1 interval of the cell cycle
    • Muller, E. G. 1991. Thioredoxin deficiency in yeast prolongs S phase and shortens the G1 interval of the cell cycle. J. Biol. Chem. 266:9194-9202.
    • (1991) J. Biol. Chem. , vol.266 , pp. 9194-9202
    • Muller, E.G.1
  • 180
    • 0026513919 scopus 로고
    • Thioredoxin genes in Saccharomyces cerevisiae: Map positions of TRX1 and TRX2
    • Muller, E. G. 1992. Thioredoxin genes in Saccharomyces cerevisiae: map positions of TRX1 and TRX2. Yeast 8:117-120.
    • (1992) Yeast , vol.8 , pp. 117-120
    • Muller, E.G.1
  • 181
    • 0028912113 scopus 로고
    • A salt-sensitive 3′(2′),5′-bisphosphate nucleotidase involved in sulfate activation
    • Murguia, J. R., J. M. Belles, and R. Serrano. 1995. A salt-sensitive 3′(2′),5′-bisphosphate nucleotidase involved in sulfate activation. Science 267:232-234.
    • (1995) Science , vol.267 , pp. 232-234
    • Murguia, J.R.1    Belles, J.M.2    Serrano, R.3
  • 182
    • 0029824147 scopus 로고    scopus 로고
    • The yeast HAL2 nucleotidase is an in vivo target of salt toxicity
    • Murguia, J. R., J. M. Belles, and R. Serrano. 1996. The yeast HAL2 nucleotidase is an in vivo target of salt toxicity. J. Biol. Chem. 271:29029-29033.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29029-29033
    • Murguia, J.R.1    Belles, J.M.2    Serrano, R.3
  • 183
    • 0015293175 scopus 로고
    • Transport of S-adenosylmethionine in Saccharomyces cerevisiae
    • Murphy, J. T., and K. D. Spence. 1972. Transport of S-adenosylmethionine in Saccharomyces cerevisiae. J. Bacteriol. 109:499-504.
    • (1972) J. Bacteriol. , vol.109 , pp. 499-504
    • Murphy, J.T.1    Spence, K.D.2
  • 184
    • 0014027931 scopus 로고
    • Acetylhomoserine and methionine biosynthesis in Neurospora
    • Nagai, S., and M. Flavin. 1966. Acetylhomoserine and methionine biosynthesis in Neurospora. J. Biol. Chem. 241:3861-3863.
    • (1966) J. Biol. Chem. , vol.241 , pp. 3861-3863
    • Nagai, S.1    Flavin, M.2
  • 185
    • 0014198939 scopus 로고
    • Acetylhomoserine. An intermediate in the fungal biosynthesis of methionine
    • Nagai, S., and M. Flavin. 1967. Acetylhomoserine. An intermediate in the fungal biosynthesis of methionine. J. Biol. Chem. 242:3884-3895.
    • (1967) J. Biol. Chem. , vol.242 , pp. 3884-3895
    • Nagai, S.1    Flavin, M.2
  • 186
    • 0028076764 scopus 로고
    • The ancient regulatory-protein family of WD-repeat proteins
    • Neer, E. J., C. J. Schmidt, R. Nambudripad, and T. F. Smith. 1994. The ancient regulatory-protein family of WD-repeat proteins. Nature 371:297-300.
    • (1994) Nature , vol.371 , pp. 297-300
    • Neer, E.J.1    Schmidt, C.J.2    Nambudripad, R.3    Smith, T.F.4
  • 188
    • 0026054687 scopus 로고
    • Diverse proteins homologous to inositol monophosphatase
    • Neuwald, A. F., J. D. York, and P. W. Majerus. 1991. Diverse proteins homologous to inositol monophosphatase. FEBS Lett. 294:16-18.
    • (1991) FEBS Lett. , vol.294 , pp. 16-18
    • Neuwald, A.F.1    York, J.D.2    Majerus, P.W.3
  • 189
    • 0028961858 scopus 로고
    • Role of the Saccharomyces cerevisiae general regulatory factor CP1 in methionine biosynthetic gene transcription
    • O'Connell, K., Y. Surdin-Kerjan, and R. E. Baker. 1995. Role of the Saccharomyces cerevisiae general regulatory factor CP1 in methionine biosynthetic gene transcription. Mol. Cell. Biol. 15:1879-1888.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1879-1888
    • O'Connell, K.1    Surdin-Kerjan, Y.2    Baker, R.E.3
  • 192
    • 0029974383 scopus 로고    scopus 로고
    • Single point mutation in Met4p impair the transcriptional repression of MET genes in Saccharomyces cerevisiae
    • Omura, F., A. Fulita, and Y. Shibano. 1996. Single point mutation in Met4p impair the transcriptional repression of MET genes in Saccharomyces cerevisiae. FEBS Lett. 387:179-183.
    • (1996) FEBS Lett. , vol.387 , pp. 179-183
    • Omura, F.1    Fulita, A.2    Shibano, Y.3
  • 195
    • 0028301740 scopus 로고
    • Purification and properties of Saccharomyces cerevisiae cystathionine beta-synthase
    • Ono, B., K. Kijima, T. Inoue, S. Miyoshi, A. Matsuda, and S. Shinoda. 1994. Purification and properties of Saccharomyces cerevisiae cystathionine beta-synthase. Yeast 10:333-339.
    • (1994) Yeast , vol.10 , pp. 333-339
    • Ono, B.1    Kijima, K.2    Inoue, T.3    Miyoshi, S.4    Matsuda, A.5    Shinoda, S.6
  • 196
    • 0026066631 scopus 로고
    • The cysteine transport system of Saccharomyces cerevisiae
    • Ono, B., and K. Naito. 1991. The cysteine transport system of Saccharomyces cerevisiae. Yeast 7:849-855.
    • (1991) Yeast , vol.7 , pp. 849-855
    • Ono, B.1    Naito, K.2
  • 197
    • 0024225039 scopus 로고
    • Cysteine biosynthesis in Saccharomyces cerevisiae: Mutation that confers cystathionine beta-synthase deficiency
    • Ono, B., Y. Shirahige, A. Nanjoh, N. Andou, H. Ohue, and Y. Ishino-Arao. 1988. Cysteine biosynthesis in Saccharomyces cerevisiae: mutation that confers cystathionine beta-synthase deficiency. J. Bacteriol. 170:5883-5889.
    • (1988) J. Bacteriol. , vol.170 , pp. 5883-5889
    • Ono, B.1    Shirahige, Y.2    Nanjoh, A.3    Andou, N.4    Ohue, H.5    Ishino-Arao, Y.6
  • 200
    • 0024462430 scopus 로고
    • Characterization of the flavoprotein moieties of NADPH-sulfite reductase from Salmonella typhimurium and Escherichia coli. Physicochemical and catalytic properties, amino acid sequence deduced from DNA sequence of cysJ, and comparison with NADPH-cytochrome P-450 reductase
    • Ostrowski, J., M. J. Barber, D. C. Rueger, B. E. Miller, L. M. Siegel, and N. M. Kredich. 1989. Characterization of the flavoprotein moieties of NADPH-sulfite reductase from Salmonella typhimurium and Escherichia coli. Physicochemical and catalytic properties, amino acid sequence deduced from DNA sequence of cysJ, and comparison with NADPH-cytochrome P-450 reductase. J. Biol. Chem. 264:15796-15808.
    • (1989) J. Biol. Chem. , vol.264 , pp. 15796-15808
    • Ostrowski, J.1    Barber, M.J.2    Rueger, D.C.3    Miller, B.E.4    Siegel, L.M.5    Kredich, N.M.6
  • 202
    • 0019988692 scopus 로고
    • Methionine biosynthesis in Brevibacterium flavum: Properties and essential role of O-acetylhomoserine sulfhydrylase
    • Tokyo
    • Ozaki, H., and I. Shiio. 1982. Methionine biosynthesis in Brevibacterium flavum: properties and essential role of O-acetylhomoserine sulfhydrylase. J. Biochem. (Tokyo) 91:1163-1171.
    • (1982) J. Biochem. , vol.91 , pp. 1163-1171
    • Ozaki, H.1    Shiio, I.2
  • 203
    • 0028872732 scopus 로고
    • Three different regulatory mechanisms enable yeast hexose transporter (HXT) genes to be induced by different levels of glucose
    • Ozcan, S., and M. Johnston. 1995. Three different regulatory mechanisms enable yeast hexose transporter (HXT) genes to be induced by different levels of glucose. Mol. Cell. Biol. 15:1564-1572.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1564-1572
    • Ozcan, S.1    Johnston, M.2
  • 204
    • 0024301133 scopus 로고
    • Strong cellular preference in the expression of a housekeeping gene of Arabidopsis thaliana encoding S-adenosylmethionine synthetase
    • Peleman, J., W. Boerjan, G. Engler, J. Seurinck, J. Botterman, T. Alliotte, M. Van Montagu, and D. Inze. 1989. Strong cellular preference in the expression of a housekeeping gene of Arabidopsis thaliana encoding S-adenosylmethionine synthetase. Plant Cell. 1:81-93.
    • (1989) Plant Cell. , vol.1 , pp. 81-93
    • Peleman, J.1    Boerjan, W.2    Engler, G.3    Seurinck, J.4    Botterman, J.5    Alliotte, T.6    Van Montagu, M.7    Inze, D.8
  • 205
    • 0024852938 scopus 로고
    • Structure and expression analyses of the S-adenosylmethionine synthetase gene family in Arabidopsis thaliana
    • Peleman, J., K. Saito, B. Cottyn, G. Engler, J. Seurinck, M. Van Montagu, and D. Inze. 1989. Structure and expression analyses of the S-adenosylmethionine synthetase gene family in Arabidopsis thaliana. Gene 84:359-369.
    • (1989) Gene , vol.84 , pp. 359-369
    • Peleman, J.1    Saito, K.2    Cottyn, B.3    Engler, G.4    Seurinck, J.5    Van Montagu, M.6    Inze, D.7
  • 206
    • 0028858093 scopus 로고
    • 2+-sensitive 3′(2′),5′-diphosphonucleoside 3′(2′)-phosphohydrolase and complements yeast met22 and Escherichia coli cysQ mutations
    • 2+-sensitive 3′(2′),5′-diphosphonucleoside 3′(2′)-phosphohydrolase and complements yeast met22 and Escherichia coli cysQ mutations. J. Biol. Chem. 270:29105-29110.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29105-29110
    • Peng, Z.1    Verma, D.P.2
  • 207
    • 0023787981 scopus 로고
    • Reactions of Saccharomyces cerevisiae and Zygosaccharomyces bailii to sulphite
    • Pilkington, B. J., and A. H. Rose. 1988. Reactions of Saccharomyces cerevisiae and Zygosaccharomyces bailii to sulphite. J. Gen. Microbiol. 134:2823-2830.
    • (1988) J. Gen. Microbiol. , vol.134 , pp. 2823-2830
    • Pilkington, B.J.1    Rose, A.H.2
  • 208
    • 0017409010 scopus 로고
    • Isolation and characterization of MMS-sensitive mutants of Saccharomvces cerevisiae
    • Prakash, L., and S. Prakash. 1977. Isolation and characterization of MMS-sensitive mutants of Saccharomvces cerevisiae. Genetics 86:33-55.
    • (1977) Genetics , vol.86 , pp. 33-55
    • Prakash, L.1    Prakash, S.2
  • 209
    • 0026649405 scopus 로고
    • Anatomy of a transcription factor important for the start of the cell cycle in Saccharomyces cerevisiae
    • Primig, M., S. Sockanathan, H. Auer, and K. Nasmyth. 1992. Anatomy of a transcription factor important for the start of the cell cycle in Saccharomyces cerevisiae. Nature 358:593-597.
    • (1992) Nature , vol.358 , pp. 593-597
    • Primig, M.1    Sockanathan, S.2    Auer, H.3    Nasmyth, K.4
  • 210
    • 0030099036 scopus 로고    scopus 로고
    • The SAL1 gene of Arabidopsis, encoding an enzyme with 3′(2′),5′-bisphosphate nucleotidase and inositol polyphosphate 1-phosphatase activities, increases salt tolerance in yeast
    • Quintero, F. J., B. Garciadeblas, and A. Rodriguez-Navarro. 1996. The SAL1 gene of Arabidopsis, encoding an enzyme with 3′(2′),5′-bisphosphate nucleotidase and inositol polyphosphate 1-phosphatase activities, increases salt tolerance in yeast. Plant Cell 8:529-537.
    • (1996) Plant Cell , vol.8 , pp. 529-537
    • Quintero, F.J.1    Garciadeblas, B.2    Rodriguez-Navarro, A.3
  • 212
    • 84989748895 scopus 로고
    • Recovery of sulfate transport into heterotrophic tobacco cells from inhibition by reduced glutathione
    • Rennenberg, H., O. Kemper, and B. Thoene. 1989. Recovery of sulfate transport into heterotrophic tobacco cells from inhibition by reduced glutathione. Physiol. Plant. 76:271-276.
    • (1989) Physiol. Plant. , vol.76 , pp. 271-276
    • Rennenberg, H.1    Kemper, O.2    Thoene, B.3
  • 213
    • 0001663552 scopus 로고
    • Enzymatic synthesis of adenosine-5′-phosphosulfate
    • Robbins, P. W., and F. Lipmann. 1958. Enzymatic synthesis of adenosine-5′-phosphosulfate. J. Biol. Chem. 233:686-690.
    • (1958) J. Biol. Chem. , vol.233 , pp. 686-690
    • Robbins, P.W.1    Lipmann, F.2
  • 214
    • 0014213126 scopus 로고
    • Regulation of homoserine O-transacetylase, first step in methionine biosyntheis in Saccharomyces cerevisiae
    • Robichon-Szulmajster, H., and H. Cherest. 1967. Regulation of homoserine O-transacetylase, first step in methionine biosyntheis in Saccharomyces cerevisiae. Biochem. Biophys. Res. Commun. 28:256-262.
    • (1967) Biochem. Biophys. Res. Commun. , vol.28 , pp. 256-262
    • Robichon-Szulmajster, H.1    Cherest, H.2
  • 216
    • 0028865615 scopus 로고
    • A multifunctional Urechis caupo protein, PAPS synthetase, has both ATP sulfurylase and APS kinase activities
    • Rosenthal, E., and T. Leustek. 1995. A multifunctional Urechis caupo protein, PAPS synthetase, has both ATP sulfurylase and APS kinase activities. Gene 165:243-248.
    • (1995) Gene , vol.165 , pp. 243-248
    • Rosenthal, E.1    Leustek, T.2
  • 217
    • 0025325932 scopus 로고
    • Thioredoxin or glutaredoxin in Escherichia coli is essential for sulfate reduction but not for deoxyribonucleotide synthesis
    • Russel, M., P. Model, and A. Holmgren. 1990. Thioredoxin or glutaredoxin in Escherichia coli is essential for sulfate reduction but not for deoxyribonucleotide synthesis. J. Bacteriol. 172:1923-1929.
    • (1990) J. Bacteriol. , vol.172 , pp. 1923-1929
    • Russel, M.1    Model, P.2    Holmgren, A.3
  • 218
    • 0021781098 scopus 로고
    • The expression of the MET25 gene of Saccharomyces cerevisiae is regulated transcriptionally
    • Sangsoda, S., H. Cherest, and Y. Surdin-Kerjan. 1985. The expression of the MET25 gene of Saccharomyces cerevisiae is regulated transcriptionally. Mol. Gen. Genet. 200:407-414.
    • (1985) Mol. Gen. Genet. , vol.200 , pp. 407-414
    • Sangsoda, S.1    Cherest, H.2    Surdin-Kerjan, Y.3
  • 219
    • 0027198978 scopus 로고
    • Isozymes of S-adenosylmethionine synthetase are encoded by tandemly duplicated genes in Escherichia coli
    • Satischandran, C., J. C. Taylor, and G. D. Markham. 1993. Isozymes of S-adenosylmethionine synthetase are encoded by tandemly duplicated genes in Escherichia coli. Mol. Microbiol. 9:835-846.
    • (1993) Mol. Microbiol. , vol.9 , pp. 835-846
    • Satischandran, C.1    Taylor, J.C.2    Markham, G.D.3
  • 220
    • 0025323933 scopus 로고
    • Novel Escherichia coli K-12 mutants impaired in S-adenosylmethionine synthesis
    • Satischandran, C., J. C. Taylor, and G. D. Markham. 1990. Novel Escherichia coli K-12 mutants impaired in S-adenosylmethionine synthesis. J. Bacteriol. 172:4489-4496.
    • (1990) J. Bacteriol. , vol.172 , pp. 4489-4496
    • Satischandran, C.1    Taylor, J.C.2    Markham, G.D.3
  • 221
    • 0024511031 scopus 로고
    • Interaction of folylpolyglutamates with enzymes in one-carbon metabolism
    • Schirch, V., and W. B. Strong. 1989. Interaction of folylpolyglutamates with enzymes in one-carbon metabolism. Arch. Biochem. Biophys. 269:371-380.
    • (1989) Arch. Biochem. Biophys. , vol.269 , pp. 371-380
    • Schirch, V.1    Strong, W.B.2
  • 222
    • 0022538259 scopus 로고
    • Properties of the purified APS-kinase from Escherichia coli and Saccharomyces cerevisiae
    • Schriek, U., and J. D. Schwenn. 1986. Properties of the purified APS-kinase from Escherichia coli and Saccharomyces cerevisiae. Arch. Microbiol. 145: 32-38.
    • (1986) Arch. Microbiol. , vol.145 , pp. 32-38
    • Schriek, U.1    Schwenn, J.D.2
  • 223
    • 0025602681 scopus 로고
    • ATP sulphurylase activity of the nodP and nodQ gene products of Rhizobium meliloti
    • Schwedock, J., and S. R. Long. 1990. ATP sulphurylase activity of the nodP and nodQ gene products of Rhizobium meliloti. Nature 348:644-647.
    • (1990) Nature , vol.348 , pp. 644-647
    • Schwedock, J.1    Long, S.R.2
  • 224
    • 0024689689 scopus 로고
    • Nucleotide sequence and protein products of two new nodulation genes of Rhizobium meliloti, nodP and nodQ
    • Schwedock, J., and S. R. Long. 1989. Nucleotide sequence and protein products of two new nodulation genes of Rhizobium meliloti, nodP and nodQ. Mol. Plant-Microbe Interact. 2:181-194.
    • (1989) Mol. Plant-Microbe Interact. , vol.2 , pp. 181-194
    • Schwedock, J.1    Long, S.R.2
  • 225
    • 0028130514 scopus 로고
    • Rhizobium meliloti NodP and NodQ form a multifunctional sulfate-activating complex requiring GTP for activity
    • Schwedock, J. S., C. Liu, T. S. Leyh, and S. R. Long. 1994. Rhizobium meliloti NodP and NodQ form a multifunctional sulfate-activating complex requiring GTP for activity. J. Bacteriol. 176:7055-7064.
    • (1994) J. Bacteriol. , vol.176 , pp. 7055-7064
    • Schwedock, J.S.1    Liu, C.2    Leyh, T.S.3    Long, S.R.4
  • 226
    • 0026440039 scopus 로고
    • Rhizobium meliloti genes involved in sulfate activation: The two copies of nodPQ and a new locus, saa
    • Schwedock, J. S., and S. R. Long. 1992. Rhizobium meliloti genes involved in sulfate activation: the two copies of nodPQ and a new locus, saa. Genetics 132:899-909.
    • (1992) Genetics , vol.132 , pp. 899-909
    • Schwedock, J.S.1    Long, S.R.2
  • 227
    • 0017067652 scopus 로고
    • The transport of S-adenosyl-L-methionine in isolated yeast vacuoles and spheroplasts
    • Schwenke, J., and H. de Robichon-Szulmajster. 1976. The transport of S-adenosyl-L-methionine in isolated yeast vacuoles and spheroplasts. Eur. J. Biochem. 65:49-60.
    • (1976) Eur. J. Biochem. , vol.65 , pp. 49-60
    • Schwenke, J.1    De Robichon-Szulmajster, H.2
  • 228
    • 0028121632 scopus 로고
    • Photosynthetic sulfate reduction
    • Schwenn, J. D. 1994. Photosynthetic sulfate reduction. Z. Naturforsch. 49c:531-539.
    • (1994) Z. Naturforsch. , vol.49 C , pp. 531-539
    • Schwenn, J.D.1
  • 229
    • 0024249959 scopus 로고
    • Yeast PAPS reductase: Properties and requirements of the purified enzyme
    • Schwenn, J. D., F. A. Krone, and K. Husmann. 1988. Yeast PAPS reductase: properties and requirements of the purified enzyme. Arch. Microbiol. 150:313-319.
    • (1988) Arch. Microbiol. , vol.150 , pp. 313-319
    • Schwenn, J.D.1    Krone, F.A.2    Husmann, K.3
  • 230
    • 0019644241 scopus 로고
    • Siroheme as an active catalyst in sulfite reduction
    • Tokyo
    • Seki, Y., N. Sogawa, and M. Ishimoto. 1981. Siroheme as an active catalyst in sulfite reduction. J. Biochem. (Tokyo) 90:1487-1492.
    • (1981) J. Biochem. , vol.90 , pp. 1487-1492
    • Seki, Y.1    Sogawa, N.2    Ishimoto, M.3
  • 231
    • 0039399893 scopus 로고
    • Biochemistry of the sulfur cycle
    • D. M. Greenberg (ed.), Academic Press, Inc., New York, N.Y.
    • Siegel, L. M. 1975. Biochemistry of the sulfur cycle, p. 217-286. In D. M. Greenberg (ed.), Metabolic pathways, vol. VII. Metabolism of sulfur compounds. Academic Press, Inc., New York, N.Y.
    • (1975) Metabolic Pathways, Vol. VII. Metabolism of Sulfur Compounds , vol.7 , pp. 217-286
    • Siegel, L.M.1
  • 232
    • 0015968302 scopus 로고
    • Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. IV. The Escherichia coli hemoflavoprotein subunit structure and dissociation into hemoprotein and flavoprotein components
    • Siegel, L. M., and P. S. Davis. 1974. Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. IV. The Escherichia coli hemoflavoprotein subunit structure and dissociation into hemoprotein and flavoprotein components. J. Biol. Chem. 249:1587-1598.
    • (1974) J. Biol. Chem. , vol.249 , pp. 1587-1598
    • Siegel, L.M.1    Davis, P.S.2
  • 233
    • 0015962153 scopus 로고
    • Association of methionine requirement with methyl mercury resistant mutants of yeast
    • Singh, A., and F. Sherman. 1974. Association of methionine requirement with methyl mercury resistant mutants of yeast. Nature 247:227-229.
    • (1974) Nature , vol.247 , pp. 227-229
    • Singh, A.1    Sherman, F.2
  • 234
    • 0016245928 scopus 로고
    • Characteristics and relationships of mercury-resistant mutants and methionine auxotrophs of yeast
    • Singh, A., and F. Sherman. 1974. Characteristics and relationships of mercury-resistant mutants and methionine auxotrophs of yeast. J. Bacteriol. 118:911-918.
    • (1974) J. Bacteriol. , vol.118 , pp. 911-918
    • Singh, A.1    Sherman, F.2
  • 235
    • 0027295625 scopus 로고
    • A new function of S-adenosylmethionine: The ribosyl moiety of AdoMet is the precursor of the cyclopentenediol moiety of the tRNA wobble base queuine
    • Slany, R. K., M. Bosl, P. F. Crain, and H. Kersten. 1993. A new function of S-adenosylmethionine: the ribosyl moiety of AdoMet is the precursor of the cyclopentenediol moiety of the tRNA wobble base queuine. Biochemistry 32:7811-7817.
    • (1993) Biochemistry , vol.32 , pp. 7811-7817
    • Slany, R.K.1    Bosl, M.2    Crain, P.F.3    Kersten, H.4
  • 236
    • 0029053572 scopus 로고
    • Isolation of a cDNA from Saccharomyces cerevisiae that encodes a high affinity sulphate transporter at the plasma membrane
    • Smith, F. W., M. J. Hawkesford, I. M. Prosser, and D. T. Clarkson. 1995. Isolation of a cDNA from Saccharomyces cerevisiae that encodes a high affinity sulphate transporter at the plasma membrane. Mol. Gen. Genet. 247:709-715.
    • (1995) Mol. Gen. Genet. , vol.247 , pp. 709-715
    • Smith, F.W.1    Hawkesford, M.J.2    Prosser, I.M.3    Clarkson, D.T.4
  • 237
    • 0001345133 scopus 로고
    • Characterization of sulfate transport in cultured tobacco roots
    • Smith, I. K. 1976. Characterization of sulfate transport in cultured tobacco roots. Plant Physiol. 58:358-362.
    • (1976) Plant Physiol. , vol.58 , pp. 358-362
    • Smith, I.K.1
  • 238
    • 0015057739 scopus 로고
    • Mutation of Saccharomyces cerevisiae preventing up-take of S-adenosylmethionine
    • Spence, K. D. 1971. Mutation of Saccharomyces cerevisiae preventing up-take of S-adenosylmethionine. J. Bacteriol. 106:325-330.
    • (1971) J. Bacteriol. , vol.106 , pp. 325-330
    • Spence, K.D.1
  • 239
    • 0016812079 scopus 로고
    • Purification and properties of 7,8-diaminopelargonic acid aminotransferase. An enzyme in the biotin biosynthetic pathway
    • Stoner, G. L., and M. A. Eisenberg. 1975. Purification and properties of 7,8-diaminopelargonic acid aminotransferase. An enzyme in the biotin biosynthetic pathway. J. Biol. Chem. 250:4029-4036.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4029-4036
    • Stoner, G.L.1    Eisenberg, M.A.2
  • 240
    • 0022629809 scopus 로고
    • Transport of sulphur dioxide by Saccharomyces cerevisiae
    • Stratford, M., and A. H. Rose. 1986. Transport of sulphur dioxide by Saccharomyces cerevisiae. J. Gen. Microbiol. 132:1-6.
    • (1986) J. Gen. Microbiol. , vol.132 , pp. 1-6
    • Stratford, M.1    Rose, A.H.2
  • 241
    • 0029876208 scopus 로고    scopus 로고
    • Structure and function of S-adenosylmethionine synthetase: Crystal structures of S-adenosylmethionine synthetase with ADP, BrADP, and PPi at 28 angstroms resolution
    • Takusagawa, F., S. Kamitori, and G. D. Markham. 1996. Structure and function of S-adenosylmethionine synthetase: crystal structures of S-adenosylmethionine synthetase with ADP, BrADP, and PPi at 28 angstroms resolution. Biochemistry 35:2586-2596.
    • (1996) Biochemistry , vol.35 , pp. 2586-2596
    • Takusagawa, F.1    Kamitori, S.2    Markham, G.D.3
  • 243
    • 0026627761 scopus 로고
    • One rotten apple spoils the whole bushel: The role of ethylene in fruit ripening
    • Theologis, A. 1992. One rotten apple spoils the whole bushel: the role of ethylene in fruit ripening. Cell 70:181-184.
    • (1992) Cell , vol.70 , pp. 181-184
    • Theologis, A.1
  • 244
    • 0026640677 scopus 로고
    • Physiological analysis of mutants of Saccharomyces cerevisiae impaired in sulphate assimilation
    • Thomas, D., R. Barbey, D. Henry, and Y. Surdin-Kerjan. 1992. Physiological analysis of mutants of Saccharomyces cerevisiae impaired in sulphate assimilation. J. Gen. Microbiol. 138:2021-2028.
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 2021-2028
    • Thomas, D.1    Barbey, R.2    Henry, D.3    Surdin-Kerjan, Y.4
  • 245
    • 0025078941 scopus 로고
    • Gene-enzyme relationship in the sulfate assimilation pathway of Saccharomyces cerevisiae. Study of the 3′-phosphoadenylylsulfate reductase structural gene
    • Thomas, D., R. Barbey, and Y. Surdin-Kerjan. 1990. Gene-enzyme relationship in the sulfate assimilation pathway of Saccharomyces cerevisiae. Study of the 3′-phosphoadenylylsulfate reductase structural gene. J. Biol. Chem. 265:15518-15524.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15518-15524
    • Thomas, D.1    Barbey, R.2    Surdin-Kerjan, Y.3
  • 246
    • 0024356429 scopus 로고
    • Elements involved in S-adenosylmethionine mediated regulation of the Saccharomyces cerevisiae MET25 gene
    • Thomas, D., H. Cherest, and Y. Surdin-Kerjan. 1989. Elements involved in S-adenosylmethionine mediated regulation of the Saccharomyces cerevisiae MET25 gene. Mol. Cell. Biol. 9:3292-3298.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 3292-3298
    • Thomas, D.1    Cherest, H.2    Surdin-Kerjan, Y.3
  • 247
    • 0026096914 scopus 로고
    • Identification of the structural gene for glucose-6-phosphate dehydrogenase in yeast. Inactivation leads to a nutritional requirement for organic sulfur
    • Thomas, D., H. Cherest, and Y. Surdin-Kerjan. 1991. Identification of the structural gene for glucose-6-phosphate dehydrogenase in yeast. Inactivation leads to a nutritional requirement for organic sulfur. EMBO J. 10:547-553.
    • (1991) EMBO J. , vol.10 , pp. 547-553
    • Thomas, D.1    Cherest, H.2    Surdin-Kerjan, Y.3
  • 248
    • 0026546494 scopus 로고
    • MET4, a leucine zipper protein, and centromere binding factor I, are both required for transcriptional activation of sulfur metabolism in Saccharomyces cerevisiae
    • Thomas, D., I. Jacquemin, and Y. Surdin-Kerjan. 1992. MET4, a leucine zipper protein, and centromere binding factor I, are both required for transcriptional activation of sulfur metabolism in Saccharomyces cerevisiae. Mol. Cell. Biol. 12:1719-1727.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 1719-1727
    • Thomas, D.1    Jacquemin, I.2    Surdin-Kerjan, Y.3
  • 249
    • 0028806055 scopus 로고
    • Met30, a yeast transcriptional inhibitor that responds to S-adenosylmethionine, is an essential protein with WD40 repeats
    • Thomas, D., L. Kuras, R. Barbey, H. Cherest, P. L. Blaiseau, and Y. Surdin-Kerjan. 1995. Met30, a yeast transcriptional inhibitor that responds to S-adenosylmethionine, is an essential protein with WD40 repeats. Mol. Cell. Biol. 15:6526-6534.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6526-6534
    • Thomas, D.1    Kuras, L.2    Barbey, R.3    Cherest, H.4    Blaiseau, P.L.5    Surdin-Kerjan, Y.6
  • 250
    • 0024267104 scopus 로고
    • SAM2 encodes the second methionine S-adenosyl transferase in Saccharomyces cerevisiae: Physiology and regulation of both enzymes
    • Thomas, D., R. Rothstein, N. Rosenberg, and Y. Surdin-Kerjan. 1988. SAM2 encodes the second methionine S-adenosyl transferase in Saccharomyces cerevisiae: physiology and regulation of both enzymes. Mol. Cell. Biol. 8:5132-5139.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 5132-5139
    • Thomas, D.1    Rothstein, R.2    Rosenberg, N.3    Surdin-Kerjan, Y.4
  • 251
    • 0023646110 scopus 로고
    • SAM1, the structural gene for one of the S-adenosylmethionine synthetases in Saccharomyces cerevisiae. Sequence and expression
    • Thomas, D., and Y. Surdin-Kerjan. 1987. SAM1, the structural gene for one of the S-adenosylmethionine synthetases in Saccharomyces cerevisiae. Sequence and expression. J. Biol. Chem. 262:16704-16709.
    • (1987) J. Biol. Chem. , vol.262 , pp. 16704-16709
    • Thomas, D.1    Surdin-Kerjan, Y.2
  • 252
    • 0025775073 scopus 로고
    • The synthesis of the two S-adenosyl-methionine synthetases is differently regulated in Saccharomyces cerevisiae
    • Thomas, D., and Y. Surdin-Kerjan. 1991. The synthesis of the two S-adenosyl-methionine synthetases is differently regulated in Saccharomyces cerevisiae. Mol. Gen. Genet. 226:224-232.
    • (1991) Mol. Gen. Genet. , vol.226 , pp. 224-232
    • Thomas, D.1    Surdin-Kerjan, Y.2
  • 253
    • 2642651660 scopus 로고    scopus 로고
    • Thomas, D., and Y. Surdin-Kerjan. Unpublished results
    • Thomas, D., and Y. Surdin-Kerjan. Unpublished results.
  • 254
    • 0017154294 scopus 로고
    • Properties of enzyme fraction A from Chlorella and co-purification of 3′(2′),5′bisphosphonucleoside 3′(2′)-phosphohydrolase, adenosine 5′-phosphosulfate sulfohydrolase and adenosine-5′-phosphocyclase activities
    • Tsang, M. L. S., and J. A. Schiff. 1976. Properties of enzyme fraction A from Chlorella and co-purification of 3′(2′),5′bisphosphonucleoside 3′(2′)-phosphohydrolase, adenosine 5′-phosphosulfate sulfohydrolase and adenosine-5′-phosphocyclase activities. Eur. J. Biochem. 65:113-121.
    • (1976) Eur. J. Biochem. , vol.65 , pp. 113-121
    • Tsang, M.L.S.1    Schiff, J.A.2
  • 255
    • 0015239426 scopus 로고
    • Adenosine trphosphate sulfurylase from Penicillium chrysogenum. II. Physical, kinetic and regulatory properties
    • Tweedie, J. W., and I. H. Segel. 1971. Adenosine trphosphate sulfurylase from Penicillium chrysogenum. II. Physical, kinetic and regulatory properties. J. Biol. Chem. 246:2438-2446.
    • (1971) J. Biol. Chem. , vol.246 , pp. 2438-2446
    • Tweedie, J.W.1    Segel, I.H.2
  • 256
    • 2642682175 scopus 로고    scopus 로고
    • Personal communication
    • 255a. Tyers, M. Personal communication.
    • Tyers, M.1
  • 258
    • 0025269991 scopus 로고
    • The SLP1 gene of Saccharomyces cerevisiae is essential for vacuolar morphogenesis and function
    • Wada, Y., K. Kitamoto, T. Kanbe, K. Tanaka, and Y. Anraku. 1990. The SLP1 gene of Saccharomyces cerevisiae is essential for vacuolar morphogenesis and function. Mol. Cell. Biol. 10:2214-2223.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 2214-2223
    • Wada, Y.1    Kitamoto, K.2    Kanbe, T.3    Tanaka, K.4    Anraku, Y.5
  • 259
    • 0026629819 scopus 로고
    • Genes for directing vacuolar morphogenesis in Saccharomyces cerevisiae. Isolation and characterization of two classes of vam mutants
    • Wada, Y., Y. Ohsumi, and Y. Anraku. 1992. Genes for directing vacuolar morphogenesis in Saccharomyces cerevisiae. Isolation and characterization of two classes of vam mutants. J. Biol. Chem. 267:18665-18670.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18665-18670
    • Wada, Y.1    Ohsumi, Y.2    Anraku, Y.3
  • 260
    • 0027422749 scopus 로고
    • HTLV-I Tax protein stimulation of DNA binding of hZIP proteins by enhancing dimerization
    • Wagner, S., and M. R. Green. 1993. HTLV-I Tax protein stimulation of DNA binding of hZIP proteins by enhancing dimerization. Science 262: 395-399.
    • (1993) Science , vol.262 , pp. 395-399
    • Wagner, S.1    Green, M.R.2
  • 261
    • 0028095384 scopus 로고
    • Gene dissection demonstrates that the Escherichia coli cysG gene encodes a multifunctional protein
    • Warren, M. J., E. L. Bolt, C. A. Roessner, A. I. Scott, J. B. Spencer, and S. C. Woodcock. 1494. Gene dissection demonstrates that the Escherichia coli cysG gene encodes a multifunctional protein. Biochem. J. 302:837-844.
    • (1494) Biochem. J. , vol.302 , pp. 837-844
    • Warren, M.J.1    Bolt, E.L.2    Roessner, C.A.3    Scott, A.I.4    Spencer, J.B.5    Woodcock, S.C.6
  • 262
    • 0022323786 scopus 로고
    • Nitrogen catabolite repression in yeasts and filamentous fungi
    • Wiame, J. M., M. Grenson, and H. N. Arst. 1185. Nitrogen catabolite repression in yeasts and filamentous fungi. Adv. Microb. Phvsiol. 26:1-88.
    • (1185) Adv. Microb. Phvsiol. , vol.26 , pp. 1-88
    • Wiame, J.M.1    Grenson, M.2    Arst, H.N.3
  • 263
    • 0000852069 scopus 로고
    • Yeast sulfate reducing system. I. Reduction of sulfate to sulfite
    • Wilson, L. G., T. Asahi, and R. S. Bandurski. 1961. Yeast sulfate reducing system. I. Reduction of sulfate to sulfite. J. Biol. Chem. 236:1822-1829.
    • (1961) J. Biol. Chem. , vol.236 , pp. 1822-1829
    • Wilson, L.G.1    Asahi, T.2    Bandurski, R.S.3
  • 264
    • 0016593935 scopus 로고
    • Metabolism of toluene and xylene by Pseudomonas putida (arvilla) mt-2: Evidence for a new function of the TOL plasmid
    • Worsey, M. J., and P. A. Williams. 1975. Metabolism of toluene and xylene by Pseudomonas putida (arvilla) mt-2: evidence for a new function of the TOL plasmid. J. Bacteriol. 124:7-13.
    • (1975) J. Bacteriol. , vol.124 , pp. 7-13
    • Worsey, M.J.1    Williams, P.A.2
  • 265
    • 0028212746 scopus 로고
    • Isolation and characterization of sulfite mutants of Saccharomyces cerevisiae
    • Xu, X., J. D. Wightman, B. L. Geller, D. Avram, and A. T. Bakalinsky. 1994. Isolation and characterization of sulfite mutants of Saccharomyces cerevisiae. Curr. Genet. 25:488-496.
    • (1994) Curr. Genet. , vol.25 , pp. 488-496
    • Xu, X.1    Wightman, J.D.2    Geller, B.L.3    Avram, D.4    Bakalinsky, A.T.5
  • 266
    • 0017124720 scopus 로고
    • O-Acetylserine and O-acetylhomoserine sulfhydrylase of yeast. Subunit structure
    • Tokyo
    • Yamagata, S. 1976. O-Acetylserine and O-acetylhomoserine sulfhydrylase of yeast. Subunit structure. J. Biochem. (Tokyo) 80:787-797.
    • (1976) J. Biochem. , vol.80 , pp. 787-797
    • Yamagata, S.1
  • 267
    • 0023391972 scopus 로고
    • Partial purification and some properties of homoserine O-acetyltransferase of a methionine auxotroph of Saccharomyces cerevisiae
    • Yamagata, S. 1987. Partial purification and some properties of homoserine O-acetyltransferase of a methionine auxotroph of Saccharomyces cerevisiae. J. Bacteriol. 169:3458-3463.
    • (1987) J. Bacteriol. , vol.169 , pp. 3458-3463
    • Yamagata, S.1
  • 268
    • 0027214077 scopus 로고
    • Cloning and bacterial expression of the CYS3 gene encoding cystathionine gamma-lyase of Saccharomyces cerevisiae and the physicochemical and enzymatic properties of the protein
    • Yamagata, S., R. J. D'Andrea, S. Fujisaki, M. Isaji, and K. Nakamura. 1993. Cloning and bacterial expression of the CYS3 gene encoding cystathionine gamma-lyase of Saccharomyces cerevisiae and the physicochemical and enzymatic properties of the protein. J. Bacteriol. 175:4800-4808.
    • (1993) J. Bacteriol. , vol.175 , pp. 4800-4808
    • Yamagata, S.1    D'Andrea, R.J.2    Fujisaki, S.3    Isaji, M.4    Nakamura, K.5
  • 269
    • 0017175790 scopus 로고
    • O-Acetylserine and O-acetylhomoserine sulfhydrylase of yeast. Further purification and characterization as a pyridoxal enzyme
    • Tokyo
    • Yamagata, S., and K. Takeshima. 1976. O-Acetylserine and O-acetylhomoserine sulfhydrylase of yeast. Further purification and characterization as a pyridoxal enzyme. J. Biochem. (Tokyo) 80:777-785.
    • (1976) J. Biochem. , vol.80 , pp. 777-785
    • Yamagata, S.1    Takeshima, K.2
  • 270
    • 0014400791 scopus 로고
    • Studies on yeast sulfite reductase. I. Purification and characterization
    • Yoshimoto, A., and R. Sato. 1968. Studies on yeast sulfite reductase. I. Purification and characterization. Biochim. Biophys. Acta 153:555-575.
    • (1968) Biochim. Biophys. Acta , vol.153 , pp. 555-575
    • Yoshimoto, A.1    Sato, R.2
  • 271
    • 0023727338 scopus 로고
    • Superoxidized states of Escherichia coli sulfite reductase heme protein subunit
    • Young, L. J., and L. M. Siegel. 1988. Superoxidized states of Escherichia coli sulfite reductase heme protein subunit. Biochemistry 27:5984-5990.
    • (1988) Biochemistry , vol.27 , pp. 5984-5990
    • Young, L.J.1    Siegel, L.M.2
  • 272
    • 0025897384 scopus 로고
    • Transsulfuration in archaebacteria
    • Zhou, D., and R. H. White. 1991. Transsulfuration in archaebacteria. J. Bacteriol. 173:3250-3251.
    • (1991) J. Bacteriol. , vol.173 , pp. 3250-3251
    • Zhou, D.1    White, R.H.2


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