메뉴 건너뛰기




Volumn 112, Issue 2, 1996, Pages 669-675

Sulfur availability and the SAC1 gene control adenosine triphosphate sulfurylase gene expression in Chlamydomonas reinhardtii

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA; CHLAMYDOMONAS REINHARDTII; ESCHERICHIA COLI;

EID: 0030265660     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.112.2.669     Document Type: Article
Times cited : (38)

References (46)
  • 1
    • 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 MI, Turner G, Bailey AM, Brown J, Lehmbeck J, Clausen IG (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
  • 2
    • 0001659495 scopus 로고
    • Localization of enzymes of assimilatory sulfate reduction in pea roots
    • Brunold C, Suter M (1989) Localization of enzymes of assimilatory sulfate reduction in pea roots. Planta 179: 228-234
    • (1989) Planta , vol.179 , pp. 228-234
    • Brunold, C.1    Suter, M.2
  • 3
    • 0001011753 scopus 로고
    • 4 plants. Intercellular and intracellular location of ATP sulfurylase, cysteine synthase and cystathionine β-lyase in maize leaves
    • 4 plants. Intercellular and intracellular location of ATP sulfurylase, cysteine synthase and cystathionine β-lyase in maize leaves. Plant Physiol 75: 873-875
    • (1984) Plant Physiol , vol.75 , pp. 873-875
    • Burnell, J.N.1
  • 4
    • 0011913281 scopus 로고
    • Sulfate-regulated expression of ATP sulfurylase and adenosine-5′-phosphosulfate kinase in Brassica juncea
    • abstract no. 319
    • Chen Y, Leustek T (1995) Sulfate-regulated expression of ATP sulfurylase and adenosine-5′-phosphosulfate kinase in Brassica juncea (abstract no. 319). Plant Physiol 108: S-72
    • (1995) Plant Physiol , vol.108
    • Chen, Y.1    Leustek, T.2
  • 5
    • 0023502858 scopus 로고
    • The Saccharomyces cerevisiae MET3 gene: Nucleotide sequence and relationship of the 5′-non-coding region to that of MET25
    • Cherest H, Kergan P, Surdin-Kerjan Y (1987) The Saccharomyces cerevisiae MET3 gene: nucleotide sequence and relationship of the 5′-non-coding region to that of MET25. Mol Gen Genet 210: 307-313
    • (1987) Mol Gen Genet , vol.210 , pp. 307-313
    • Cherest, H.1    Kergan, P.2    Surdin-Kerjan, Y.3
  • 6
    • 0021836161 scopus 로고
    • Transcriptional regulation of the MET3 gene of Saccharomyces cerevisiae
    • Cherest H, Thao NN, Surdin-Kerjan Y (1985) Transcriptional regulation of the MET3 gene of Saccharomyces cerevisiae. Gene 34: 269-281
    • (1985) Gene , vol.34 , pp. 269-281
    • Cherest, H.1    Thao, N.N.2    Surdin-Kerjan, Y.3
  • 8
    • 0029944852 scopus 로고    scopus 로고
    • Sac1, a putative regulator that is critical for survival of Chlamydomonas reinhardtii during sulfur deprivation
    • Davies JP, Yildiz F, Grossman AR (1996) Sac1, a putative regulator that is critical for survival of Chlamydomonas reinhardtii during sulfur deprivation. EMBO J 15: 2150-2159
    • (1996) EMBO J , vol.15 , pp. 2150-2159
    • Davies, J.P.1    Yildiz, F.2    Grossman, A.R.3
  • 9
    • 0028105642 scopus 로고
    • Mutants of Chlamydomonas with aberrant responses to sulfur deprivation
    • Davies JP, Yildiz F, Grossman AR (1994) Mutants of Chlamydomonas with aberrant responses to sulfur deprivation. Plant Cell 6: 53-63
    • (1994) Plant Cell , vol.6 , pp. 53-63
    • Davies, J.P.1    Yildiz, F.2    Grossman, A.R.3
  • 10
    • 0024712610 scopus 로고
    • Structure and expression of the gene encoding the periplasmic arylsulfatase of Chlamydomonas reinhardtii
    • de Hostos EL, Schilling J, Grossman AR (1989) Structure and expression of the gene encoding the periplasmic arylsulfatase of Chlamydomonas reinhardtii. Mol Gen Genet 218: 229-239
    • (1989) Mol Gen Genet , vol.218 , pp. 229-239
    • Hostos, E.L.1    Schilling, J.2    Grossman, A.R.3
  • 11
    • 0023877363 scopus 로고
    • Purification and biosynthesis of a derepressible periplasmic arylsulfatase from Chlamydomonas reinhardtii
    • de Hostos EL, Togasaki RK, Grossman AR (1988) Purification and biosynthesis of a derepressible periplasmic arylsulfatase from Chlamydomonas reinhardtii. J Cell Biol 106: 29-37
    • (1988) J Cell Biol , vol.106 , pp. 29-37
    • Hostos, E.L.1    Togasaki, R.K.2    Grossman, A.R.3
  • 13
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan D (1983) Studies on transformation of Escherichia coli with plasmids. J Mol Biol 166: 557-580
    • (1983) J Mol Biol , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 14
    • 0024979253 scopus 로고
    • Transport and routing of proteins into chloroplasts
    • Keegstra K (1989) Transport and routing of proteins into chloroplasts. Cell 56: 247-253
    • (1989) Cell , vol.56 , pp. 247-253
    • Keegstra, K.1
  • 15
    • 0028173842 scopus 로고
    • Isolation and characterization of two cDNA clones encoding ATP-sulfurylases from potato by complementation of a yeast mutant
    • Klonus D, Höfgen R, Willmitzer L, Riesmeier J (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    Höfgen, R.2    Willmitzer, L.3    Riesmeier, J.4
  • 16
    • 0029243157 scopus 로고
    • A cDNA clone for an ATP-sulfurylase from Arabidopsis thaliana
    • Klonus D, Riesmeier JW, Willmitzer L (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
  • 17
    • 0028936193 scopus 로고
    • Functional analysis of MET4, a yeast transcriptional activator responsive to S-adenosylmethionine
    • Kuras L, Thomas D (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
  • 18
    • 0028466132 scopus 로고
    • Cloning of a cDNA encoding ATP sulfurylase from Arabidopsis thaliana by functional expression in Saccharomyces cerevisiae
    • Leustek T, Murillo M, Cervantes M (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
  • 19
    • 0014687578 scopus 로고
    • Purification and properties of the enzyme ATP sulfurylase and its relation to vitamin A
    • Levi AS, Wolf G (1969) Purification and properties of the enzyme ATP sulfurylase and its relation to vitamin A. Biochim Biophys Acta 178: 262-282
    • (1969) Biochim Biophys Acta , vol.178 , pp. 262-282
    • Levi, A.S.1    Wolf, G.2
  • 20
    • 0023874416 scopus 로고
    • The sulfate activation locus of Escherichia coli K12: Cloning, genetic and enzymatic characterization
    • Leyh TS, Taylor JC, Markham GD (1988) The sulfate activation locus of Escherichia coli K12: cloning, genetic and enzymatic characterization. J Biol Chem 263: 2409-2416
    • (1988) J Biol Chem , vol.263 , pp. 2409-2416
    • Leyh, T.S.1    Taylor, J.C.2    Markham, G.D.3
  • 21
    • 0028786032 scopus 로고
    • The isolation and characterizatrion of cDNA encoding the mouse bifunctional ATP sulfurylase-adenosine 5′-phosphosulfate kinase
    • Li H, Deyrup A, Mensch JR, Domowicz M, Konstantinidis AK, Schwartz NB (1995) The isolation and characterizatrion of cDNA encoding the mouse bifunctional ATP sulfurylase-adenosine 5′-phosphosulfate kinase. J Biol Chem 49: 29453-29459
    • (1995) J Biol Chem , vol.49 , pp. 29453-29459
    • Li, H.1    Deyrup, A.2    Mensch, J.R.3    Domowicz, M.4    Konstantinidis, A.K.5    Schwartz, N.B.6
  • 22
    • 0025877204 scopus 로고
    • Purification and properties of two forms of ATP sulfurylase from Euglena
    • Li J, Saidha T, Schiff JA (1991) Purification and properties of two forms of ATP sulfurylase from Euglena. Biochim Biophys Acta 1078: 68-76
    • (1991) Biochim Biophys Acta , vol.1078 , pp. 68-76
    • Li, J.1    Saidha, T.2    Schiff, J.A.3
  • 23
    • 0001113803 scopus 로고
    • Localization of ATP sulfurylase and O-acetylserine(thiol)lyase in spinach leaves
    • Lunn JE, Droux M, Martin J, Douce R (1990) Localization of ATP sulfurylase and O-acetylserine(thiol)lyase in spinach leaves. Plant Physiol 94: 1345-1352
    • (1990) Plant Physiol , vol.94 , pp. 1345-1352
    • Lunn, J.E.1    Droux, M.2    Martin, J.3    Douce, R.4
  • 26
    • 0014432776 scopus 로고
    • Positive control of the CYS-3 locus in regulation of sulfur metabolism in Neurospora
    • Marzluf GA (1968) Positive control of the CYS-3 locus in regulation of sulfur metabolism in Neurospora. J Mol Biol 33: 423-437
    • (1968) J Mol Biol , vol.33 , pp. 423-437
    • Marzluf, G.A.1
  • 27
    • 84961486318 scopus 로고
    • Regulation and partial purification of the ATP-sulfurylase from the cyanobacterium Synechococcus 6301
    • Mishra D, Schmidt A (1992) Regulation and partial purification of the ATP-sulfurylase from the cyanobacterium Synechococcus 6301. Z Naturforsch 47c: 95-101
    • (1992) Z Naturforsch , vol.47 C , pp. 95-101
    • Mishra, D.1    Schmidt, A.2
  • 28
    • 0028885653 scopus 로고
    • Adenosine-5′-triphosphate-sulfurylase from Arabidopsis thaliana and Escherichia coli are functionally equivalent but structurally and kinetically divergent: Nucleotide sequence of two adenosine-5′-triphosphate-sulfurylase cDNAs from Arabidopsis thaliana and analysis of a recombinant enzyme
    • Murillo M, Leustek T (1995) Adenosine-5′-triphosphate-sulfurylase from Arabidopsis thaliana and Escherichia coli are functionally equivalent but structurally and kinetically divergent: nucleotide sequence of two adenosine-5′-triphosphate-sulfurylase cDNAs from Arabidopsis thaliana and analysis of a recombinant enzyme. Arch Biochem Biophys 323: 195-205
    • (1995) Arch Biochem Biophys , vol.323 , pp. 195-205
    • Murillo, M.1    Leustek, T.2
  • 29
    • 0345342291 scopus 로고
    • Adenosine 5′-triphosphate-sulfurylase in corn roots and its partial purification
    • Onajobi FE, Cole CV, Ross C (1973) Adenosine 5′-triphosphate-sulfurylase in corn roots and its partial purification. Plant Physiol 52: 580-584
    • (1973) Plant Physiol , vol.52 , pp. 580-584
    • Onajobi, F.E.1    Cole, C.V.2    Ross, C.3
  • 30
    • 0000894190 scopus 로고
    • ATP sulfurylase from higher plants. Purification and preliminary kinetics studies on the cabbage leaf enzyme
    • Osslund T, Chandler C, Segel IH (1982) ATP sulfurylase from higher plants. Purification and preliminary kinetics studies on the cabbage leaf enzyme. Plant Physiol 70: 39-45
    • (1982) Plant Physiol , vol.70 , pp. 39-45
    • Osslund, T.1    Chandler, C.2    Segel, I.H.3
  • 31
    • 0026603819 scopus 로고
    • Production of the CYS3 regulator, a bZIP DNA-binding protein is sufficient to induce sulfur gene expression in Neurospora crassa
    • Paietta JV (1992) Production of the CYS3 regulator, a bZIP DNA-binding protein is sufficient to induce sulfur gene expression in Neurospora crassa. Mol Cell Biol 12: 1568-1577
    • (1992) Mol Cell Biol , vol.12 , pp. 1568-1577
    • Paietta, J.V.1
  • 32
    • 0023369140 scopus 로고
    • Molecular cloning and characterization of the cys-3 regulatory gene of Neurospora crassa
    • Paietta JV, Akins RA, Lambowitz AM, Marzluf GA (1987) Molecular cloning and characterization of the cys-3 regulatory gene of Neurospora crassa. Mol Cell Biol 7: 2506-2511
    • (1987) Mol Cell Biol , vol.7 , pp. 2506-2511
    • Paietta, J.V.1    Akins, R.A.2    Lambowitz, A.M.3    Marzluf, G.A.4
  • 33
    • 0026007091 scopus 로고
    • ATP sulfurylase from trophosome tissue of Riftia pachyptila (hydrothermal vent tube worm)
    • Renosto F, Martin RL, Borrell JL, Nelson DC, Segel IH (1991) ATP sulfurylase from trophosome tissue of Riftia pachyptila (hydrothermal vent tube worm). Arch Biochem Biophys 290: 66-78
    • (1991) Arch Biochem Biophys , vol.290 , pp. 66-78
    • Renosto, F.1    Martin, R.L.2    Borrell, J.L.3    Nelson, D.C.4    Segel, I.H.5
  • 34
    • 0025296757 scopus 로고
    • Regulation of inorganic sulfate activation in filamentous fungi. Allosteric inhibition of ATP sulfurylase by 3′-phosphoadenosine-5′-phosphosulfate
    • Renosto F, Martin RL, Wailes LM, Daley LA, Segel IH (1990) Regulation of inorganic sulfate activation in filamentous fungi. Allosteric inhibition of ATP sulfurylase by 3′-phosphoadenosine-5′-phosphosulfate. J Biol Chem 265: 10300-10308
    • (1990) J Biol Chem , vol.265 , pp. 10300-10308
    • Renosto, F.1    Martin, R.L.2    Wailes, L.M.3    Daley, L.A.4    Segel, I.H.5
  • 35
    • 0027138759 scopus 로고
    • ATP sulfurylase from higher plants: Kinetic and structural characterization of the chloroplast and cytosol enzymes from spinach leaf
    • Renosto F, Patel HC, Martin RL, Thomassian C, Zimmerman G, Segel IH (1993) ATP sulfurylase from higher plants: kinetic and structural characterization of the chloroplast and cytosol enzymes from spinach leaf. Arch Biochem Biophys 307: 272-285
    • (1993) Arch Biochem Biophys , vol.307 , pp. 272-285
    • Renosto, F.1    Patel, H.C.2    Martin, R.L.3    Thomassian, C.4    Zimmerman, G.5    Segel, I.H.6
  • 36
    • 0028865615 scopus 로고
    • A multifunctional Urechis caupo protein, PAPS synthetase, has both ATP sulfurylase and APS kinase activities
    • Rosenthal E, Leustek T (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
  • 37
    • 3142576367 scopus 로고
    • Sulphur metabolism. ATP-sulphurylase
    • PM Dey JB Harborne, eds, Academic Press, London
    • Schmutz D (1990) Sulphur metabolism. ATP-sulphurylase. In PM Dey JB Harborne, eds, Methods in Plant Biochemistry, Vol 3. Academic Press, London, pp 335-337
    • (1990) Methods in Plant Biochemistry , vol.3 , pp. 335-337
    • Schmutz, D.1
  • 38
    • 0025602681 scopus 로고
    • ATP sulphurylase activity of the nodP and nodQ gene products of Rhizobium meliloti
    • Schwedock J, Long SR (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
  • 39
    • 0026440039 scopus 로고
    • Rhizobium meliloti genes involved in sulfate activation: The two copies of nodPQ and a new locus, saa
    • Schwedock JS, Long SR (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
  • 40
    • 0015311856 scopus 로고
    • Purification properties and substrate specificity of adenosine triphosphate sulfurylase from spinach leaf tissue
    • Shaw WH, Anderson JW (1972) Purification properties and substrate specificity of adenosine triphosphate sulfurylase from spinach leaf tissue. Biochem J 127: 237-247
    • (1972) Biochem J , vol.127 , pp. 237-247
    • Shaw, W.H.1    Anderson, J.W.2
  • 41
    • 0015516470 scopus 로고
    • Purification and properties of ATP sulfurylase from furth mouse mastocytoma
    • Shoyab M, Su LY, Marz W (1972) Purification and properties of ATP sulfurylase from furth mouse mastocytoma. Biochim Biophys Acta 258: 113-124
    • (1972) Biochim Biophys Acta , vol.258 , pp. 113-124
    • Shoyab, M.1    Su, L.Y.2    Marz, W.3
  • 42
    • 0024356429 scopus 로고
    • Elements involved in S-adenosylmethionine-mediated regulation of the Saccharomyces cerevisiae MET 25 gene
    • Thomas D, Cherest H, Surdin-Kerjan Y (1989) Elements involved in S-adenosylmethionine-mediated regulation of the Saccharomyces cerevisiae MET 25 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
  • 43
    • 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, Jacquemin I, Surdin-Kerjan Y (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
  • 44
    • 0024542834 scopus 로고
    • Domain structure of mitochondrial and chloroplast targeting peptides
    • von Heijne G, Steppuhn J, Herrmann RG (1989) Domain structure of mitochondrial and chloroplast targeting peptides. Eur J Biochem 180: 535-545
    • (1989) Eur J Biochem , vol.180 , pp. 535-545
    • Heijne, G.1    Steppuhn, J.2    Herrmann, R.G.3
  • 45
    • 0027966651 scopus 로고
    • Characterization of sulfate transport in Chlamydomonas reinhardtii during sulfur-limited and sulfur-sufficient growth
    • Yildiz FH, Davies JP, Grossman AR (1994) Characterization of sulfate transport in Chlamydomonas reinhardtii during sulfur-limited and sulfur-sufficient growth. Plant Physiol 104: 981-987
    • (1994) Plant Physiol , vol.104 , pp. 981-987
    • Yildiz, F.H.1    Davies, J.P.2    Grossman, A.R.3
  • 46
    • 0024561266 scopus 로고
    • Rat liver ATP-sulfurylase: Purification, kinetic characterization, and interaction with arsenate, selenate, phosphate, and other inorganic oxyanions
    • Yu M, Martin RL, Jain S, Chen LJ, Segel IH (1989) Rat liver ATP-sulfurylase: purification, kinetic characterization, and interaction with arsenate, selenate, phosphate, and other inorganic oxyanions. Arch Biochem Biophys 269: 156-174
    • (1989) Arch Biochem Biophys , vol.269 , pp. 156-174
    • Yu, M.1    Martin, R.L.2    Jain, S.3    Chen, L.J.4    Segel, I.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.