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Volumn 48, Issue 3, 2005, Pages 270-275

Interaction of sulfate assimilation with nitrate assimilation as a function of nutrient status and enzymatic co-regulation in Brassica juncea roots

Author keywords

APS reductase; ATP sulfurylase; Cysteine; Nitrite reductase; Sulfite reductase

Indexed keywords

BRASSICA; BRASSICA JUNCEA;

EID: 26844556078     PISSN: 12269239     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF03030522     Document Type: Article
Times cited : (5)

References (32)
  • 1
    • 84948882966 scopus 로고
    • Interaction of nitrate and sulfate reduction in tobacco. 1. Influence of availability of nitrate and sulfate
    • Barney PE, Bush LP (1985a) Interaction of nitrate and sulfate reduction in tobacco. 1. Influence of availability of nitrate and sulfate. J Plant Nutr 8: 505-515
    • (1985) J Plant Nutr , vol.8 , pp. 505-515
    • Barney, P.E.1    Bush, L.P.2
  • 2
    • 26844576094 scopus 로고
    • Interaction of nitrate and sulfate reduction in tobacco. 2. Influence of apical meristem removal
    • Barney PE, Bush LP (1985b) Interaction of nitrate and sulfate reduction in tobacco. 2. Influence of apical meristem removal. J Plant Nutr 8: 517-526
    • (1985) J Plant Nutr , vol.8 , pp. 517-526
    • Barney, P.E.1    Bush, L.P.2
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal Biochem 72: 248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0030592165 scopus 로고    scopus 로고
    • A cDNA clone from Arabidopsis thaliana encoding plastidic ferrodoxin:sulfite reductase
    • Bruhl A, Haverkamp T, Gisselmann G, Schwenn JD (1996) A cDNA clone from Arabidopsis thaliana encoding plastidic ferrodoxin:sulfite reductase. Biochim Biophys Acta 1295: 119-124
    • (1996) Biochim Biophys Acta , vol.1295 , pp. 119-124
    • Bruhl, A.1    Haverkamp, T.2    Gisselmann, G.3    Schwenn, J.D.4
  • 5
    • 0000009046 scopus 로고
    • Regulation of sulfate assimilation in plants. 7. Cysteine inactivation of adenosine 5′-phosphosulfate sulfotransferase in Lemna minor L.
    • Brunold C (1978) Regulation of sulfate assimilation in plants. 7. Cysteine inactivation of adenosine 5′-phosphosulfate sulfotransferase in Lemna minor L. Plant Physiol 61: 342-347
    • (1978) Plant Physiol , vol.61 , pp. 342-347
    • Brunold, C.1
  • 6
    • 0000909457 scopus 로고    scopus 로고
    • Regulation of sulfur metabolism in plants: First molecular approaches
    • Brunold C, Rennenberg H (1997) Regulation of sulfur metabolism in plants: First molecular approaches. Prog Botan 58: 164-186
    • (1997) Prog Botan , vol.58 , pp. 164-186
    • Brunold, C.1    Rennenberg, H.2
  • 7
    • 0000577076 scopus 로고
    • Regulation of sulfate assimilation by nitrogen nutrition in the duckweed Lemna minor L.
    • Brunold C, Suter M (1984) Regulation of sulfate assimilation by nitrogen nutrition in the duckweed Lemna minor L. Plant Physiol 76: 579-583
    • (1984) Plant Physiol , vol.76 , pp. 579-583
    • Brunold, C.1    Suter, M.2
  • 8
    • 85003994243 scopus 로고
    • Effect of high and low sulfate concentrations on adenosine 5′-phosphosulfate sulfotransferase activity from Lemna minor
    • Brunold C, Suter M, Lavanchy P (1987) Effect of high and low sulfate concentrations on adenosine 5′-phosphosulfate sulfotransferase activity from Lemna minor. Physiol Plant 70: 168-174
    • (1987) Physiol Plant , vol.70 , pp. 168-174
    • Brunold, C.1    Suter, M.2    Lavanchy, P.3
  • 9
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomsczynsky P, Sacchi N (1987) Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem 162: 156-159
    • (1987) Anal Biochem , vol.162 , pp. 156-159
    • Chomsczynsky, P.1    Sacchi, N.2
  • 10
    • 0001570260 scopus 로고
    • Sulfur deprivation and nitrogen metabolism in maize seedlings
    • Friedrich JW, Schrader LE (1978) Sulfur deprivation and nitrogen metabolism in maize seedlings. Plant Physiol 61: 900-903
    • (1978) Plant Physiol , vol.61 , pp. 900-903
    • Friedrich, J.W.1    Schrader, L.E.2
  • 11
    • 85009575616 scopus 로고
    • Regulation of ATP-sulfurylase and adenosine 5′-phosphosulfate sulfotransferase by the sulfur and the nitrogen source in heterotrophic cell suspension cultures of Paul's scarlet rose
    • Haller E, Suter M, Brunold C (1986) Regulation of ATP-sulfurylase and adenosine 5′-phosphosulfate sulfotransferase by the sulfur and the nitrogen source in heterotrophic cell suspension cultures of Paul's scarlet rose. J Plant Physiol 125: 275-283
    • (1986) J Plant Physiol , vol.125 , pp. 275-283
    • Haller, E.1    Suter, M.2    Brunold, C.3
  • 12
    • 34249928216 scopus 로고
    • Differential protein synthesis in response to sulphate and phosphate deprivation: Identification of possible components of plasma membrane transport systems in cultured tomato roots
    • Hawkesford MJ, Belcher AR (1991) Differential protein synthesis in response to sulphate and phosphate deprivation: Identification of possible components of plasma membrane transport systems in cultured tomato roots. Planta 185: 323-329
    • (1991) Planta , vol.185 , pp. 323-329
    • Hawkesford, M.J.1    Belcher, A.R.2
  • 13
    • 0030904866 scopus 로고    scopus 로고
    • Molecular physiology of sulfur metabolism
    • Hell R (1997) Molecular physiology of sulfur metabolism. Planta 202: 138-148
    • (1997) Planta , vol.202 , pp. 138-148
    • Hell, R.1
  • 14
    • 2942532392 scopus 로고    scopus 로고
    • Molecular analysis and control of cysteine biosynthesis: Integration of nitrogen and sulphur metabolism
    • Hesse H, Nikiforova V, Gakiere B, Hoefgen R (2004) Molecular analysis and control of cysteine biosynthesis: Integration of nitrogen and sulphur metabolism. J Exp Bot 55: 1283-1292
    • (2004) J Exp Bot , vol.55 , pp. 1283-1292
    • Hesse, H.1    Nikiforova, V.2    Gakiere, B.3    Hoefgen, R.4
  • 16
    • 4344587717 scopus 로고    scopus 로고
    • Control of sulphate assimilation and glutathione synthesis: Interaction with N and C metabolism
    • Kopriva S, Rennenberg H (2004) Control of sulphate assimilation and glutathione synthesis: Interaction with N and C metabolism. J Exp Bot 55: 1831-1842
    • (2004) J Exp Bot , vol.55 , pp. 1831-1842
    • Kopriva, S.1    Rennenberg, H.2
  • 19
    • 20744434747 scopus 로고    scopus 로고
    • Cysteine does not repress adenosine-5′-phosphosulphate reductase through its conversion to either sulfate or glutathione
    • in press
    • Lee S (2005) Cysteine does not repress adenosine-5′-phosphosulphate reductase through its conversion to either sulfate or glutathione. J Plant Biol (in press)
    • (2005) J Plant Biol
    • Lee, S.1
  • 20
    • 0017643426 scopus 로고
    • RNA molecular weight determinations by gel electrophoresis under denaturing conditions: A critical reexamination
    • Lehrach H, Diamond D, Wonzney JM, Boedtker H (1977) RNA molecular weight determinations by gel electrophoresis under denaturing conditions: A critical reexamination. Biochem 16: 4743-4751
    • (1977) Biochem , vol.16 , pp. 4743-4751
    • Lehrach, H.1    Diamond, D.2    Wonzney, J.M.3    Boedtker, H.4
  • 21
    • 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
  • 22
    • 15844395948 scopus 로고    scopus 로고
    • Cloning of a cDNA encoded by a member of the Arabidopsis thaliana ATP sulfurylase multigene family
    • Logan HM, Cathala N, Grignon C, Davidian JC (1996) Cloning of a cDNA encoded by a member of the Arabidopsis thaliana ATP sulfurylase multigene family. 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
  • 23
    • 0035094564 scopus 로고    scopus 로고
    • Rapid disruption of nitrogen metabolism and nitrate transport in spinach plants deprived of sulphate
    • Prosser M, Purves JV, Saker LR, Clarkson DT (2001) Rapid disruption of nitrogen metabolism and nitrate transport in spinach plants deprived of sulphate. J Exp Bot 52: 113-121
    • (2001) J Exp Bot , vol.52 , pp. 113-121
    • Prosser, M.1    Purves, J.V.2    Saker, L.R.3    Clarkson, D.T.4
  • 24
    • 0027138759 scopus 로고
    • ATP sulfurylase from higher plants: Kinetic and structural characterization of the chloroplast and cytosolic 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 cytosolic 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
  • 25
    • 0001353659 scopus 로고
    • Regulatory coupling of nitrate and sulfate assimilation pathways in cultured tobacco cells
    • USA
    • Reuveny Z, Dougall DK, Trinity PM (1980) Regulatory coupling of nitrate and sulfate assimilation pathways in cultured tobacco cells. Proc Natl Acad Sci USA 77: 6670-6672
    • (1980) Proc Natl Acad Sci , vol.77 , pp. 6670-6672
    • Reuveny, Z.1    Dougall, D.K.2    Trinity, P.M.3
  • 26
    • 0017350111 scopus 로고
    • Regulation of adenosine triphosphate sulfurylase in cultured tobacco cells. Effects of sulfur and nitrogen sources on the formation and decay of the enzyme
    • Reuveny Z, Filner P (1977) Regulation of adenosine triphosphate sulfurylase in cultured tobacco cells. Effects of sulfur and nitrogen sources on the formation and decay of the enzyme. J Biol Chem 252: 1858-1864
    • (1977) J Biol Chem , vol.252 , pp. 1858-1864
    • Reuveny, Z.1    Filner, P.2
  • 27
    • 0030295364 scopus 로고    scopus 로고
    • Isolation and characterization of a cDNA that encodes maize uroporphyrinogen III methyltransferase, an enzyme involved in the synthesis of siroheme, which is a prosthetic group of nitrite reductase
    • Sakakibara H, Takei K, Sugiyama T (1996) Isolation and characterization of a cDNA that encodes maize uroporphyrinogen III methyltransferase, an enzyme involved in the synthesis of siroheme, which is a prosthetic group of nitrite reductase. Plant J 10: 883-892
    • (1996) Plant J , vol.10 , pp. 883-892
    • Sakakibara, H.1    Takei, K.2    Sugiyama, T.3
  • 28
    • 0029841432 scopus 로고    scopus 로고
    • Sulfate reduction in higher plants: Molecular evidence for a novel 5′-adenylsulfate reductase
    • USA
    • Setya A, Murillo M, Leustek T (1996) Sulfate reduction in higher plants: Molecular evidence for a novel 5′-adenylsulfate reductase. Proc Natl Acad Sci USA 93: 13383-13388
    • (1996) Proc Natl Acad Sci , vol.93 , pp. 13383-13388
    • Setya, A.1    Murillo, M.2    Leustek, T.3
  • 29
    • 0000174267 scopus 로고
    • Regulation of sulfate assimilation in cultured tobacco cells. Effect of nitrogen and sulfur nutrition on sulfate permease and O-acetylserine sulfhydrylase
    • Smith IK (1980) Regulation of sulfate assimilation in cultured tobacco cells. Effect of nitrogen and sulfur nutrition on sulfate permease and O-acetylserine sulfhydrylase. Plant Physiol 66: 877-883
    • (1980) Plant Physiol , vol.66 , pp. 877-883
    • Smith, I.K.1
  • 30
    • 38249042756 scopus 로고
    • Regulation of sulfate assimilation by amino acids in Lemna minor L.
    • Suter M, Lavanchy P, Arb CV, Brunold C (1986) Regulation of sulfate assimilation by amino acids in Lemna minor L. Plant Sci 44: 125-132
    • (1986) Plant Sci , vol.44 , pp. 125-132
    • Suter, M.1    Lavanchy, P.2    Arb, C.V.3    Brunold, C.4
  • 31
    • 0030250382 scopus 로고    scopus 로고
    • Subcellular localization of spinach cysteine synthase isoforms and regulation of their gene expression by nitrogen and sulfur
    • Takahashi H, Saito K (1996) Subcellular localization of spinach cysteine synthase isoforms and regulation of their gene expression by nitrogen and sulfur. Plant Physiol 112: 273-280
    • (1996) Plant Physiol , vol.112 , pp. 273-280
    • Takahashi, H.1    Saito, K.2
  • 32
    • 0011696478 scopus 로고
    • Regulation of ATP-sulfurylase by various nitrogen and sulfur sources in cultured Ipomoea sp.
    • Zenk MW (1984) Regulation of ATP-sulfurylase by various nitrogen and sulfur sources in cultured Ipomoea sp. Can J Bot 62: 2107-2113
    • (1984) Can J Bot , vol.62 , pp. 2107-2113
    • Zenk, M.W.1


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