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1
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0002130186
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Biosynthesis of cysteine
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B.K. Singh. New York: Marcel Dekker, Inc. One of the most recent reviews describing the mechanism and regulation of Cys biosynthesis.
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Saito K. Biosynthesis of cysteine. Singh B.K. Plant Amino Acids Biochemistry and Biotechnology. 1999;267-291 Marcel Dekker, Inc, New York. One of the most recent reviews describing the mechanism and regulation of Cys biosynthesis.
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Plant Amino Acids Biochemistry and Biotechnology
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Saito, K.1
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2
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0032841269
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Sulfate transport and assimilation in plants
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One of the most recent reviews on sulfate transport and assimilation in plants.
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Leustek T., Saito K. Sulfate transport and assimilation in plants. Plant Physiol. 120:1999;637-643. One of the most recent reviews on sulfate transport and assimilation in plants.
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Plant Physiol
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Leustek, T.1
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0030904866
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Molecular physiology of plant sulfur metabolism
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Hell R. Molecular physiology of plant sulfur metabolism. Planta. 202:1997;138-148.
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Planta
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Hell, R.1
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Molecular regulation of sulfur assimilation and cysteine synthesis
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C. Brunold, H. Rennenberg, L.J. De Kok, I. Stulen, & J-C. Davidian. Berne: Paul Haupt. in press.
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Saito K., Takahashi H., Noji M., Inoue K., Hatzfeld Y. Molecular regulation of sulfur assimilation and cysteine synthesis. Brunold C., Rennenberg H., De Kok L.J., Stulen I., Davidian J-C. Sulfur Nutrition and Assimilation in Higher Plants. 2000;Paul Haupt, Berne. in press.
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Sulfur Nutrition and Assimilation in Higher Plants
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Saito, K.1
Takahashi, H.2
Noji, M.3
Inoue, K.4
Hatzfeld, Y.5
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5
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0003033053
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Membrane and long-distance transport of sulfate
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L.J. De Kok, I. Stulen, H. Rennenberg, C. Brunold, & W.E. Rauser. The Hague: SPB Academic Publishing
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Clarkson D.T., Hawkesford M.J., Davidian J-C. Membrane and long-distance transport of sulfate. De Kok L.J., Stulen I., Rennenberg H., Brunold C., Rauser W.E. Sulfur Nutrition and Assimilation in Higher Plants - Regulatory Agricultural and Environmental Aspects. 1993;3-20 SPB Academic Publishing, The Hague.
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Sulfur Nutrition and Assimilation in Higher Plants - Regulatory Agricultural and Environmental Aspects
, pp. 3-20
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Clarkson, D.T.1
Hawkesford, M.J.2
Davidian, J.-C.3
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6
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0002648191
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Sulfate uptake and transport in plants
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C. Brunold, H. Rennenberg, L.J. De Kok, I. Stulen, & J-C. Davidian. Berne: Paul Haupt. in press
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Davidian J-C., Hatzfeld Y., Cathala N., Tagmount A., Vidmar J.J. Sulfate uptake and transport in plants. Brunold C., Rennenberg H., De Kok L.J., Stulen I., Davidian J-C. Sulfur Nutrition and Assimilation in Higher Plants. 2000;Paul Haupt, Berne. in press.
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Sulfur Nutrition and Assimilation in Higher Plants
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Davidian, J.-C.1
Hatzfeld, Y.2
Cathala, N.3
Tagmount, A.4
Vidmar, J.J.5
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8
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0030603130
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Isolation and chracterization of a cDNA encoding a sulfate transporter from Arabidopsis thaliana
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Takahashi H., Sasakura N., Noji M., Saito K. Isolation and chracterization of a cDNA encoding a sulfate transporter from Arabidopsis thaliana. FEBS Lett. 392:1996;95-99.
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Takahashi, H.1
Sasakura, N.2
Noji, M.3
Saito, K.4
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9
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0030885523
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Regulation of cysteine biosynthesis in higher plants: A sulfate transporter induced in sulfate-starved roots plays a central role in Arabidopsis thaliana
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Takahashi H., Yamazaki M., Sasakura N., Watanabe A., Leustek T., de Almeida Engler J., Engler G., Van Montagu M., Saito K. Regulation of cysteine biosynthesis in higher plants: a sulfate transporter induced in sulfate-starved roots plays a central role in Arabidopsis thaliana. Proc Natl Acad Sci USA. 94:1997;11102-11107.
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Proc Natl Acad Sci USA
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Takahashi, H.1
Yamazaki, M.2
Sasakura, N.3
Watanabe, A.4
Leustek, T.5
De Almeida Engler, J.6
Engler, G.7
Van Montagu, M.8
Saito, K.9
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10
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0001253785
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Identification of two leaf-specific sulfate transporters in Arabidopsis thaliana (Accession No. AB012048 and AB004060)
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Takahashi H., Sasakura N., Kimura A., Watanabe A., Saito K. Identification of two leaf-specific sulfate transporters in Arabidopsis thaliana (Accession No. AB012048 and AB004060). Plant Physiol. 121:1999;686.
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Plant Physiol
, vol.121
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Takahashi, H.1
Sasakura, N.2
Kimura, A.3
Watanabe, A.4
Saito, K.5
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11
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0032693542
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Cloning of an Arabidopsis cDNA encoding a chloroplast localizing sulphate transporter isoform
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This paper provides evidence of the in vivo translocation of a putative Arabidopsis sulfate transporter into chloroplasts. The investigation that is described used a fusion protein in which a sulfate transporter isoform is bound to a green fluorescent protein.
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Takahashi H., Asanuma W., Saito K. Cloning of an Arabidopsis cDNA encoding a chloroplast localizing sulphate transporter isoform. J Exp Botany. 50:1999;1713-1714. This paper provides evidence of the in vivo translocation of a putative Arabidopsis sulfate transporter into chloroplasts. The investigation that is described used a fusion protein in which a sulfate transporter isoform is bound to a green fluorescent protein.
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(1999)
J Exp Botany
, vol.50
, pp. 1713-1714
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Takahashi, H.1
Asanuma, W.2
Saito, K.3
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12
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0001035885
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Isolation and characterization of a cDNA encoding a sulfate transporter from Arabidopsis thaliana (Accession No. D89631)
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Yamaguchi Y., Nakamura T., Harada E., Koizumi N., Sano H. Isolation and characterization of a cDNA encoding a sulfate transporter from Arabidopsis thaliana (Accession No. D89631). Plant Physiol. 113:1997;1463.
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Plant Physiol
, vol.113
, pp. 1463
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Yamaguchi, Y.1
Nakamura, T.2
Harada, E.3
Koizumi, N.4
Sano, H.5
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13
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0033890171
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The roles of three functional sulfate transporters involved in uptake and translocation of sulfate in Arabidopsis thaliana
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in press. This study provides the first detailed characterization of three functional sulfate transporters. The different tissue localizations of these three transporters is emphasized and suggests that these transporters have distinct roles as high- and low-affinity transporters.
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Takahashi H., Watanabe-Takahashi A., Smith F.W., Blake-Kalff M., Hawkesford M.J., Saito K. The roles of three functional sulfate transporters involved in uptake and translocation of sulfate in Arabidopsis thaliana. Plant J. 2000;. in press. This study provides the first detailed characterization of three functional sulfate transporters. The different tissue localizations of these three transporters is emphasized and suggests that these transporters have distinct roles as high- and low-affinity transporters.
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(2000)
Plant J
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Takahashi, H.1
Watanabe-Takahashi, A.2
Smith, F.W.3
Blake-Kalff, M.4
Hawkesford, M.J.5
Saito, K.6
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14
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0031260181
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Regulation of exprression of a cDNA from barley roots encoding a high affinity sulphate transporter
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Smith F.K., Hawkesford M.J., Ealing P.M., Clarkson D.T., Berg P.J.V., Belcher A.R., Warrilow A.G.S. Regulation of exprression of a cDNA from barley roots encoding a high affinity sulphate transporter. Plant J. 12:1997;875-884.
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Plant J
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, pp. 875-884
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Smith, F.K.1
Hawkesford, M.J.2
Ealing, P.M.3
Clarkson, D.T.4
Berg, P.J.V.5
Belcher, A.R.6
Warrilow, A.G.S.7
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15
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0033167032
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Regulation of the hvst1 gene encoding a high-affinity sulfate transporter from Hordeum vulgare
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The authors of this paper and [14] describe the cloning of a high-affinity sulfate transporter from barley. This transporter is induced by sulfate depletion. GSH down-regulated the concentration of mRNA encoding this sulfate transporter even in sulfate-starved plants in which the transporter is usually derepressed.
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Vidmar J.J., Schjoerring J.K., Touraine B., Glass A.D.M. Regulation of the hvst1 gene encoding a high-affinity sulfate transporter from Hordeum vulgare. Plant Mol Biol. 40:1999;883-892. The authors of this paper and [14] describe the cloning of a high-affinity sulfate transporter from barley. This transporter is induced by sulfate depletion. GSH down-regulated the concentration of mRNA encoding this sulfate transporter even in sulfate-starved plants in which the transporter is usually derepressed.
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(1999)
Plant Mol Biol
, vol.40
, pp. 883-892
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Vidmar, J.J.1
Schjoerring, J.K.2
Touraine, B.3
Glass, A.D.M.4
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16
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0033083485
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Coordinate modulation of maize sulfate permease and ATP sulfurylase mRNAs in response to variations in sulfur nutritional status: Stereospecific down-regulation by L-cysteine
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Bolchi A., Petrucco S., Tenca P.L., Foroni C., Ottonello S. Coordinate modulation of maize sulfate permease and ATP sulfurylase mRNAs in response to variations in sulfur nutritional status: stereospecific down-regulation by L-cysteine. Plant Mol Biol. 39:1999;527-537.
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Plant Mol Biol
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, pp. 527-537
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Bolchi, A.1
Petrucco, S.2
Tenca, P.L.3
Foroni, C.4
Ottonello, S.5
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17
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85031646168
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Transport of sulphate and reduced sulphur compounds at the tonoplast membrane
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W.J. Cram, L.J. De Kok, I. Stulen, C. Brunold, & H. Rennenberg. Leiden: Backhuys Publishers
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Mornet C., Tommasini R., Hörtensteiner S., Martinoia E. Transport of sulphate and reduced sulphur compounds at the tonoplast membrane. Cram W.J., De Kok L.J., Stulen I., Brunold C., Rennenberg H. Sulphur Metabolism in Higher Plants Molecular, Ecophysiological and Nutritional Aspects. 1997;1-11 Backhuys Publishers, Leiden.
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Sulphur Metabolism in Higher Plants Molecular, Ecophysiological and Nutritional Aspects
, pp. 1-11
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Mornet, C.1
Tommasini, R.2
Hörtensteiner, S.3
Martinoia, E.4
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18
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0033198569
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Sulfate is both a substrate and an activator of the voltage-dependent anion channel of Arabidopsis hypocotyl cells
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Frachisse J-M., Thomine S., Colcombet J., Guern J., Barbier-Brygoo H. Sulfate is both a substrate and an activator of the voltage-dependent anion channel of Arabidopsis hypocotyl cells. Plant Physiol. 121:1999;253-261.
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(1999)
Plant Physiol
, vol.121
, pp. 253-261
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Frachisse, J.-M.1
Thomine, S.2
Colcombet, J.3
Guern, J.4
Barbier-Brygoo, H.5
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19
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0028173842
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Isolation and characterization of two cDNA clones encoding ATP-sulfurylase from potato by complementation of a yeast mutant
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Klonus D., Höfgen R., Willmitzer L., Riesmeier J.W. Isolation and characterization of two cDNA clones encoding ATP-sulfurylase from potato by complementation of a yeast mutant. Plant J. 6:1994;105-112.
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(1994)
Plant J
, vol.6
, pp. 105-112
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Klonus, D.1
Höfgen, R.2
Willmitzer, L.3
Riesmeier, J.W.4
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20
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0028466132
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Cloning of a cDNA encoding ATP sulfurylase from Arabidopsis thaliana by functional expression in Saccharomyces cerevisiae
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Leustek T., Murillo M., Cervantes M. Cloning of a cDNA encoding ATP sulfurylase from Arabidopsis thaliana by functional expression in Saccharomyces cerevisiae. Plant Physiol. 105:1994;897-902.
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Plant Physiol
, vol.105
, pp. 897-902
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Leustek, T.1
Murillo, M.2
Cervantes, M.3
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21
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15844395948
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Cloning of a cDNA encoded by a member of the Arabidopsis thaliana ATP sulfurylase multigene family
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Logan H.M., Cathala N., Grignon C., Davidian J-C. Cloning of a cDNA encoded by a member of the Arabidopsis thaliana ATP sulfurylase multigene family. J Biol Chem. 271:1996;12227-12233.
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J Biol Chem
, vol.271
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Logan, H.M.1
Cathala, N.2
Grignon, C.3
Davidian, J.-C.4
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22
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0034595388
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Functional characterization of a gene encoding a fourth ATP sulfurylase isoform from Arabidopsis thaliana
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in press. In this study, the gene encoding fourth chloroplastic ATP sulfurylase was isolated. The authors discuss the possibility that the cytosolic ATP sulfurylase is produced from one of the genes encoding chloroplastic isoforms by the use of a different initiation Met codon.
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Hatzfeld Y., Lee S., Lee M., Leustek T., Saito K. Functional characterization of a gene encoding a fourth ATP sulfurylase isoform from Arabidopsis thaliana. Gene. 2000;. in press. In this study, the gene encoding fourth chloroplastic ATP sulfurylase was isolated. The authors discuss the possibility that the cytosolic ATP sulfurylase is produced from one of the genes encoding chloroplastic isoforms by the use of a different initiation Met codon.
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(2000)
Gene
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Hatzfeld, Y.1
Lee, S.2
Lee, M.3
Leustek, T.4
Saito, K.5
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23
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0032036401
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Effect of ATP sulfurylase overexpression in Bright Yellow 2 tobacco cells
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This is the first report to describe the effects of overexpression of ATP sulfurylase. Although the ATP sulfurylase activity was increased 8-fold in the BY-2 cells of transgenics tobacco, no effects on cell growth and sensitivity to selenate were observed.
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Hatzfeld Y., Cathala N., Grignon C., Davidian J-C. Effect of ATP sulfurylase overexpression in Bright Yellow 2 tobacco cells. Plant Physiol. 116:1998;1307-1313. This is the first report to describe the effects of overexpression of ATP sulfurylase. Although the ATP sulfurylase activity was increased 8-fold in the BY-2 cells of transgenics tobacco, no effects on cell growth and sensitivity to selenate were observed.
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(1998)
Plant Physiol
, vol.116
, pp. 1307-1313
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Hatzfeld, Y.1
Cathala, N.2
Grignon, C.3
Davidian, J.-C.4
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24
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0032817824
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Overexpression of ATP sulfurylase in Indian mustard leads to increased selenate uptake, reduction, and tolerance
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•]. ATP sulfurylase was overexpressed in transgenic Indian mustard (Brassica juncea). The transformants showed increased selenate uptake, reduction and tolerance, suggesting that ATP sulfurylase mediates the reduction of selenate and limits the rate of selenate assimilation.
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•]. ATP sulfurylase was overexpressed in transgenic Indian mustard (Brassica juncea). The transformants showed increased selenate uptake, reduction and tolerance, suggesting that ATP sulfurylase mediates the reduction of selenate and limits the rate of selenate assimilation.
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(1999)
Plant Physiol
, vol.119
, pp. 123-132
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Pilon-Smit, E.A.H.1
Hwang, S.2
Lytle, C.M.3
Zhu, Y.4
Tai, J.C.5
Bravo, R.C.6
Chen, Y.7
Leustek, T.8
Terry, N.9
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25
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0032082922
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Plant sulfur metabolism - The reduction of sulfate to sulfite
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An up-to-date short review on the reduction of sulfate to sulfite and the enzymes involved in this reaction.
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Bick J.A., Leustek T. Plant sulfur metabolism - the reduction of sulfate to sulfite. Curr Opin Plant Biol. 1:1998;240-244. An up-to-date short review on the reduction of sulfate to sulfite and the enzymes involved in this reaction.
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Curr Opin Plant Biol
, vol.1
, pp. 240-244
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Bick, J.A.1
Leustek, T.2
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26
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0032493355
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Glutaredoxin function for the carboxyl-terminal domain of the plant-type 5¢-adenylylsulfate reductase
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The authors show that APS reductase has two domains. They present evidence showing that the carboxyl-terminal domain has a glutaredoxin-like function and that APS reductase requires GSH for its catalytic activity.
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Bick J-A., Åslund F., Chen Y., Leustek T. Glutaredoxin function for the carboxyl-terminal domain of the plant-type 5¢-adenylylsulfate reductase. Proc Natl Acad Sci USA. 95:1998;8404-8409. The authors show that APS reductase has two domains. They present evidence showing that the carboxyl-terminal domain has a glutaredoxin-like function and that APS reductase requires GSH for its catalytic activity.
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(1998)
Proc Natl Acad Sci USA
, vol.95
, pp. 8404-8409
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Bick, J.-A.1
Åslund, F.2
Chen, Y.3
Leustek, T.4
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27
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0033985137
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Adenosine 5′-phosphosulfate sulfotransferase and adenosine 5′-phosphosulfate reducatse are identical enzymes
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This is a conclusive report that shows that APS reductase and APS sulfotransferase, which are thought to be involved in the carrier-bound pathway of APS reduction, are identical enzymes. APS sulfotransferase was purified, cloned and characterized using a recombinant form of the enzyme from Lemna minor.
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Suter M., von Ballmoos P., Kopriva S., Op den Camp R., Schaller J., Kuhlemeier C., Schürmann P., Brunold C. Adenosine 5′-phosphosulfate sulfotransferase and adenosine 5′-phosphosulfate reducatse are identical enzymes. J Biol Chem. 75:2000;930-936. This is a conclusive report that shows that APS reductase and APS sulfotransferase, which are thought to be involved in the carrier-bound pathway of APS reduction, are identical enzymes. APS sulfotransferase was purified, cloned and characterized using a recombinant form of the enzyme from Lemna minor.
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(2000)
J Biol Chem
, vol.75
, pp. 930-936
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Suter, M.1
Von Ballmoos, P.2
Kopriva, S.3
Op Den Camp, R.4
Schaller, J.5
Kuhlemeier, C.6
Schürmann, P.7
Brunold, C.8
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28
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0344348998
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Cloning sulfur assimilation genes of Brassica juncea L.: Cadmium differentially affects the expression of a putative low-affinity sulfate transporter and isoforms of ATP sulfurylase and APS reductase
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Heiss S., Schäfer H.J., Haag-Kerwer A., Rausch T. Cloning sulfur assimilation genes of Brassica juncea L.: cadmium differentially affects the expression of a putative low-affinity sulfate transporter and isoforms of ATP sulfurylase and APS reductase. Plant Mol Biol. 39:1999;847-857.
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(1999)
Plant Mol Biol
, vol.39
, pp. 847-857
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Heiss, S.1
Schäfer, H.J.2
Haag-Kerwer, A.3
Rausch, T.4
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29
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0033213118
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Light regulation of assimilatory sulphate reduction in Arabidopsis thaliana
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This paper describes the evidence for the existence of a diurnal rhythm in the expression of the mRNA that encodes APS reductase and for the activity of this enzyme. This evidence suggests that APS reductase is regulated by a similar mechanism to that controlling nitrate reductase. Sucrose is shown to be a positive effector of the expression of mRNA encoding APS reductase and of the activity of this enzyme.
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Kopriva S., Muheim R., Koprivova A., Trachsel N., Catalano C., Suter M., Brunold C. Light regulation of assimilatory sulphate reduction in Arabidopsis thaliana. Plant J. 20:1999;37-44. This paper describes the evidence for the existence of a diurnal rhythm in the expression of the mRNA that encodes APS reductase and for the activity of this enzyme. This evidence suggests that APS reductase is regulated by a similar mechanism to that controlling nitrate reductase. Sucrose is shown to be a positive effector of the expression of mRNA encoding APS reductase and of the activity of this enzyme.
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(1999)
Plant J
, vol.20
, pp. 37-44
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Kopriva, S.1
Muheim, R.2
Koprivova, A.3
Trachsel, N.4
Catalano, C.5
Suter, M.6
Brunold, C.7
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30
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0000101694
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Cyst(e)ine is the transport metabolite of assimilated sulfur from bundle-sheath to mesophyll cells in maize leaves
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Burgener M., Suter M., Jones S., Brunold C. Cyst(e)ine is the transport metabolite of assimilated sulfur from bundle-sheath to mesophyll cells in maize leaves. Plant Phsyiol. 116:1998;1315-1322.
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Plant Phsyiol
, vol.116
, pp. 1315-1322
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Burgener, M.1
Suter, M.2
Jones, S.3
Brunold, C.4
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31
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0345215152
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Isolation and characterization of a gene for assimilatory sulfite reductase from Arabidopsis thaliana
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Bork C., Schwenn J.D., Hell R. Isolation and characterization of a gene for assimilatory sulfite reductase from Arabidopsis thaliana. Gene. 212:1998;147-153.
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Gene
, vol.212
, pp. 147-153
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Bork, C.1
Schwenn, J.D.2
Hell, R.3
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32
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0031684320
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Molecular characterization of tobacco sulfite reductase: Enzyme purification, gene cloning, and gene expression analysis
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Yonekura-Sakakibara K., Ashikari T., Tanaka Y., Kusumi T., Hase T. Molecular characterization of tobacco sulfite reductase: enzyme purification, gene cloning, and gene expression analysis. J Biochem. 124:1998;615-621.
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, pp. 615-621
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Yonekura-Sakakibara, K.1
Ashikari, T.2
Tanaka, Y.3
Kusumi, T.4
Hase, T.5
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33
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0033777345
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Analysis of reductant supply systems for ferredoxin-dependent sulfite reductase in photosynthetic and nonphotosynthetic organs of maize
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+ reductase and sulfite reductase, using an appropriate combination of tissue-specific enzyme isoforms. This allowed the authors to investigate the efficiency of electron transfer by different enzyme isoforms in different tissues, and to examine the complementation of an E. coli sulfite reductase-deficient mutant by genes encoding the various isoforms.
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+ reductase and sulfite reductase, using an appropriate combination of tissue-specific enzyme isoforms. This allowed the authors to investigate the efficiency of electron transfer by different enzyme isoforms in different tissues, and to examine the complementation of an E. coli sulfite reductase-deficient mutant by genes encoding the various isoforms.
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(2000)
Plant Physiol
, vol.122
, pp. 887-894
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Yonekura-Sakakibara, K.1
Onda, Y.2
Ashikari, T.3
Tanaka, Y.4
Kusumi, T.5
Hase, T.6
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34
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0001113803
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Localization of ATP sulfurylase and O-acetylserine(thiol)lyase in spinach leaves
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Lunn J.E., Droux M., Martin J., Douce R. Localization of ATP sulfurylase and O-acetylserine(thiol)lyase in spinach leaves. Plant Physiol. 94:1990;1345-1352.
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Lunn, J.E.1
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Martin, J.3
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35
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0030250382
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Subcellular localization of spinach cysteine synthase isoforms and regulation of their gene expression by nitrogen and sulfur
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Takahashi H., Saito K. Subcellular localization of spinach cysteine synthase isoforms and regulation of their gene expression by nitrogen and sulfur. Plant Physiol. 112:1996;273-280.
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, vol.112
, pp. 273-280
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Takahashi, H.1
Saito, K.2
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36
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0028893483
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Subcellular distribution of serine acetyltransferase from Pisum sativum and characterization of an Arabidopsis thaliana putative cytosolic isoform
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Ruffet M-L., Lebrun M., Droux M., Douce R. Subcellular distribution of serine acetyltransferase from Pisum sativum and characterization of an Arabidopsis thaliana putative cytosolic isoform. Eur J Biochem. 227:1995;500-509.
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Droux, M.3
Douce, R.4
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37
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0032483994
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Isoform-dependent differences in feedback regulation and subcellular localization of serine acetyltransferase involved in cysteine biosynthesis from Arabidopsis thaliana
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The subcellular localization of three Ser acetyltransferases from A. thaliana was determined by transient expression of fusion proteins in which each of these three enzymes were fused with green fluorescence protein. Furthermore, it is shown that only the cytosolic isoform of Ser acetyltransferase (i.e. not the chloroplastic and mitochondrial isoforms) is regulated by feedback inhibition by Cys. This work provides evidence of the important regulatory role of cytosoic Ser acetyltransferase in Cys biosynthesis.
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Noji M., Inoue K., Kimura N., Gouda A., Saito K. Isoform-dependent differences in feedback regulation and subcellular localization of serine acetyltransferase involved in cysteine biosynthesis from Arabidopsis thaliana. J Biol Chem. 273:1998;32739-32745. The subcellular localization of three Ser acetyltransferases from A. thaliana was determined by transient expression of fusion proteins in which each of these three enzymes were fused with green fluorescence protein. Furthermore, it is shown that only the cytosolic isoform of Ser acetyltransferase (i.e. not the chloroplastic and mitochondrial isoforms) is regulated by feedback inhibition by Cys. This work provides evidence of the important regulatory role of cytosoic Ser acetyltransferase in Cys biosynthesis.
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J Biol Chem
, vol.273
, pp. 32739-32745
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Noji, M.1
Inoue, K.2
Kimura, N.3
Gouda, A.4
Saito, K.5
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38
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0032915394
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Molecular cloning and expression analyses of mitochondrial and plastidic isoforms of cysteine synthase (O-acetylserine (thiol)lyase) from Arabidopsis thaliana
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Hesse H., Lipke J., Altmann T., Höfgen R. Molecular cloning and expression analyses of mitochondrial and plastidic isoforms of cysteine synthase (O-acetylserine (thiol)lyase) from Arabidopsis thaliana. Amino Acids. 16:1999;113-131.
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Amino Acids
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Hesse, H.1
Lipke, J.2
Altmann, T.3
Höfgen, R.4
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39
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0031669094
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Separation, subcellular location and influence of sulphur nutrition on isoforms of cysteine synthase in spinach
-
•] deal with the relation between β-cyanoalanine synthase and OAS(thiol)-lyase [Cys synthase]. The authors of this paper present definitive evidence, which was obtained using purification techniques, to show that β-cyanoalanine synthase is predominantly located in mitochondria of spinach.
-
•] deal with the relation between β-cyanoalanine synthase and OAS(thiol)-lyase [Cys synthase]. The authors of this paper present definitive evidence, which was obtained using purification techniques, to show that β-cyanoalanine synthase is predominantly located in mitochondria of spinach.
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(1998)
J Exp Botany
, vol.49
, pp. 1625-1636
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Warrilow, A.G.S.1
Hawkesford, M.J.2
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40
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0033927405
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β-Cyanoalanine synthase is a mitochondrial cysteine synthase-like protein in spinach and Arabidopsis thaliana
-
in press. Definitive evidence is provided for the identity of β-cyanoalanine synthase with a mitochondrial OAS(thiol)-lyase [cysteine synthase], of which cDNA was previously isolated from spinach [42].
-
Hatzfeld Y., Maruyama A., Schmidt A., Noji M., Ishizawa K., Saito K. β-Cyanoalanine synthase is a mitochondrial cysteine synthase-like protein in spinach and Arabidopsis thaliana. Plant Physiol. 2000;. in press. Definitive evidence is provided for the identity of β-cyanoalanine synthase with a mitochondrial OAS(thiol)-lyase [cysteine synthase], of which cDNA was previously isolated from spinach [42].
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(2000)
Plant Physiol
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Hatzfeld, Y.1
Maruyama, A.2
Schmidt, A.3
Noji, M.4
Ishizawa, K.5
Saito, K.6
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41
-
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0031850228
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Cytosolic β cyanoalanine synthase activity attributed to cysteine synthases in Cocklebur seeds. Purification and characterization of cytosolic cysteine synthases
-
The authors used purification and a partial amino-acid sequence analysis of the purified β-cyanoalanine synthase to show that the cytosolic activity of β-cyanoalanine synthase is controlled by OAS(thiol)-lyase [Cys synthase].
-
Maruyama A., Ishizawa K., Takagi T., Esashi Y. Cytosolic β cyanoalanine synthase activity attributed to cysteine synthases in Cocklebur seeds. Purification and characterization of cytosolic cysteine synthases. Plant Cell Physiol. 39:1998;671-680. The authors used purification and a partial amino-acid sequence analysis of the purified β-cyanoalanine synthase to show that the cytosolic activity of β-cyanoalanine synthase is controlled by OAS(thiol)-lyase [Cys synthase].
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(1998)
Plant Cell Physiol
, vol.39
, pp. 671-680
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-
Maruyama, A.1
Ishizawa, K.2
Takagi, T.3
Esashi, Y.4
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42
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0028097282
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Isolation and characterization of cDNA that encodes a putative mitochondrion-localizing isoform of cysteine synthase (O-acetylserine(thiol)-lyase) from Spinacia oleracea
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Saito K., Tatsuguchi K., Takagi Y., Murakoshi I. Isolation and characterization of cDNA that encodes a putative mitochondrion-localizing isoform of cysteine synthase (O-acetylserine(thiol)-lyase) from Spinacia oleracea. J Biol Chem. 269:1994;28187-28192.
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J Biol Chem
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Saito, K.1
Tatsuguchi, K.2
Takagi, Y.3
Murakoshi, I.4
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43
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2442696023
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Determination of the sites required for the allosteric inhibition of serine acetyltransferase by L-cysteine in plants
-
This study uses a series of recombinant mutant proteins to determine the residues and domains of Ser acetyltransferase that are involved in the feedback inhibition of this enzyme by Cys.
-
Inoue K., Noji M., Saito K. Determination of the sites required for the allosteric inhibition of serine acetyltransferase by L-cysteine in plants. Eur J Biochem. 266:1999;220-227. This study uses a series of recombinant mutant proteins to determine the residues and domains of Ser acetyltransferase that are involved in the feedback inhibition of this enzyme by Cys.
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(1999)
Eur J Biochem
, vol.266
, pp. 220-227
-
-
Inoue, K.1
Noji, M.2
Saito, K.3
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44
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0029028281
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Molecular cloning and characterization of a plant serine acetyltransferase playing a regulatory role in cysteine biosynthesis from watermelon
-
Saito K., Yokoyama H., Noji M., Murakoshi I. Molecular cloning and characterization of a plant serine acetyltransferase playing a regulatory role in cysteine biosynthesis from watermelon. J Biol Chem. 270:1995;16321-16326.
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(1995)
J Biol Chem
, vol.270
, pp. 16321-16326
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Saito, K.1
Yokoyama, H.2
Noji, M.3
Murakoshi, I.4
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45
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0031079570
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Cysteine synthesis in plants: Protein-protein interactions of serine acetyltransferase from Arabidopsis thaliana
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Bogdanova N., Hell R. Cysteine synthesis in plants: protein-protein interactions of serine acetyltransferase from Arabidopsis thaliana. Plant J. 11:1997;251-262.
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(1997)
Plant J
, vol.11
, pp. 251-262
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Bogdanova, N.1
Hell, R.2
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46
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0032125745
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Interactions between serine acetyltransferase and O-acetylserine (thiol) lyase in higher plants. Structural and kinetic properties of the free and bound enzymes
-
The significance of the bienzyme complex involving OAS(thiol)-lyase and Ser acetyltransferase, and the importance of greater cellular concentrations of uncomplexed OAS(thiol)-lyase Ser acetyltransferase relative to those of the uncomplexed enzyme, is explained. An interesting regulatory mechanism is proposed that involves both free and bound forms of the two enzymes. Within the complex, the bound form of OAS(thiol)-lyase may act as a structural and/or regulatory subunit of Ser acetyltransferase. Actual OAS(thiol)-lyase activity is attributed to the free form, because the activity of bound form of OAS(thiol)-lyase is dramatically decreased.
-
Droux M., Ruffet M-L., Douce R., Job D. Interactions between serine acetyltransferase and O-acetylserine (thiol) lyase in higher plants. Structural and kinetic properties of the free and bound enzymes. Eur J Biochem. 255:1998;235-245. The significance of the bienzyme complex involving OAS(thiol)-lyase and Ser acetyltransferase, and the importance of greater cellular concentrations of uncomplexed OAS(thiol)-lyase Ser acetyltransferase relative to those of the uncomplexed enzyme, is explained. An interesting regulatory mechanism is proposed that involves both free and bound forms of the two enzymes. Within the complex, the bound form of OAS(thiol)-lyase may act as a structural and/or regulatory subunit of Ser acetyltransferase. Actual OAS(thiol)-lyase activity is attributed to the free form, because the activity of bound form of OAS(thiol)-lyase is dramatically decreased.
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(1998)
Eur J Biochem
, vol.255
, pp. 235-245
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-
Droux, M.1
Ruffet, M.-L.2
Douce, R.3
Job, D.4
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47
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0033167384
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Salt-specific regulation of the cytosolic O-acetylserine (thiol)lyase gene from Arabidopsis thaliana is dependent on abscisic acid
-
Salt and heavy metal stresses induced OAS(thiol)-lyase activity suggesting a connection between these stresses and trichome-specific gene expression [48]. The induction of gene expression is presumably mediated by abscisic acid.
-
Barroso C., Romero L.C., Cejudo F.J., Vega J.M., Gotor C. Salt-specific regulation of the cytosolic O-acetylserine (thiol)lyase gene from Arabidopsis thaliana is dependent on abscisic acid. Plant Mol Biol. 40:1999;729-736. Salt and heavy metal stresses induced OAS(thiol)-lyase activity suggesting a connection between these stresses and trichome-specific gene expression [48]. The induction of gene expression is presumably mediated by abscisic acid.
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(1999)
Plant Mol Biol
, vol.40
, pp. 729-736
-
-
Barroso, C.1
Romero, L.C.2
Cejudo, F.J.3
Vega, J.M.4
Gotor, C.5
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48
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0031080605
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Tissue-specific expression of ATCYS-3A, a gene encoding the cytosolic isoform of O-acetylserine (thiol)lyase in Arabidopsis
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Gotor C., Cejudo F.J., Barroso C. Tissue-specific expression of ATCYS-3A, a gene encoding the cytosolic isoform of O-acetylserine (thiol)lyase in Arabidopsis. Plant J. 11:1997;347-352.
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Plant J
, vol.11
, pp. 347-352
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Gotor, C.1
Cejudo, F.J.2
Barroso, C.3
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49
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0028534746
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Modulation of cysteine biosynthesis in chloroplasts of transgenic tobacco overexpressing cysteine synthase [O-acetylserine(thiol)lyase]
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Saito K., Kurosawa M., Tatsuguchi K., Takagi Y., Murakoshi I. Modulation of cysteine biosynthesis in chloroplasts of transgenic tobacco overexpressing cysteine synthase [O-acetylserine(thiol)lyase]. Plant Physiol. 106:1994;887-895.
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Plant Physiol
, vol.106
, pp. 887-895
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Saito, K.1
Kurosawa, M.2
Tatsuguchi, K.3
Takagi, Y.4
Murakoshi, I.5
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50
-
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0033213374
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Increased resistance to oxidative stress in transgenic tobacco plants overexpressing bacterial serine acetyltransferase
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This paper describes the first study of overexpression of Ser acetyltransferase in plants. Although overexpression of this enzyme resulted in only two or three times higher concentrations of Cys and GSH, much greater resistance to hydrogen peroxide was generated.
-
Blaszczyk A., Brodzik R., Sirko A. Increased resistance to oxidative stress in transgenic tobacco plants overexpressing bacterial serine acetyltransferase. Plant J. 20:1999;237-243. This paper describes the first study of overexpression of Ser acetyltransferase in plants. Although overexpression of this enzyme resulted in only two or three times higher concentrations of Cys and GSH, much greater resistance to hydrogen peroxide was generated.
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(1999)
Plant J
, vol.20
, pp. 237-243
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-
Blaszczyk, A.1
Brodzik, R.2
Sirko, A.3
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51
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0002624786
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Biosynthesis of cysteine
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F.C. Neidhardt, R.C. III Curtis, J.L. Ingraham, K.B. Low, B. Magasanik, R.Z. Reznikoff, M. Riley, M. Schaechter, & H.E. Umbarger. Washington DC: American Society for Microbiology
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Kredich N.M. Biosynthesis of cysteine. Neidhardt F.C., Curtis R.C. III, Ingraham J.L., Low K.B., Magasanik B., Reznikoff R.Z., Riley M., Schaechter M., Umbarger H.E. Escherichia coli and Salmonella typhimurium: Cellular and molecular biology, vol 1, edn 2. 1996;514-527 American Society for Microbiology, Washington DC.
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(1996)
Escherichia Coli and Salmonella Typhimurium: Cellular and Molecular Biology, Vol 1, Edn 2
, pp. 514-527
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Kredich, N.M.1
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52
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0033759245
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Regulation of sulfate assimilation by nitrogen in Arabidopsis thaliana
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Koprivova A., Suter M., Op den Camp R., Brunold C., Kopriva S. Regulation of sulfate assimilation by nitrogen in Arabidopsis thaliana. Plant Physiol. 122:2000;737-746.
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(2000)
Plant Physiol
, vol.122
, pp. 737-746
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Koprivova, A.1
Suter, M.2
Op Den Camp, R.3
Brunold, C.4
Kopriva, S.5
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53
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0033199730
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Role of O-acetyl-L-serine in the coordinated regulation of the expression of a soybean seed storage-protein gene by sulfur and nitrogen nutrition
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In conditions in which sulfur is deficient (or a low ratio of sulfur to nitrogen availability exists), the β-subunit of β-conglycinin (i.e. the sulfur-poor soybean seed storage protein) is accumulated. This paper provides evidence that OAS accumulates to higher concentrations in A. thaliana and soybean cotyledons under sulfate-deficient conditions. The addition OAS results in an elevated accumulation of the mRNA encoding the β-subunit and of the protein itself. These findings suggest that OAS is a positive signal molecule for gene expression in sulfur-starved plants.
-
Kim H., Hirai M.Y., Hayashi H., Chino M., Naito S., Fujiwara T. Role of O-acetyl-L-serine in the coordinated regulation of the expression of a soybean seed storage-protein gene by sulfur and nitrogen nutrition. Planta. 209:1999;282-289. In conditions in which sulfur is deficient (or a low ratio of sulfur to nitrogen availability exists), the β-subunit of β-conglycinin (i.e. the sulfur-poor soybean seed storage protein) is accumulated. This paper provides evidence that OAS accumulates to higher concentrations in A. thaliana and soybean cotyledons under sulfate-deficient conditions. The addition OAS results in an elevated accumulation of the mRNA encoding the β-subunit and of the protein itself. These findings suggest that OAS is a positive signal molecule for gene expression in sulfur-starved plants.
-
(1999)
Planta
, vol.209
, pp. 282-289
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Kim, H.1
Hirai, M.Y.2
Hayashi, H.3
Chino, M.4
Naito, S.5
Fujiwara, T.6
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54
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0033056545
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Uptake and assimilation of sulphate by sulphur deficient Zea mays cells: The role of O-acetyl-L-serine in the interaction between nitrogen and sulphur assimilatory pathways
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Clarkson D., Diogo E., Amâncio S. Uptake and assimilation of sulphate by sulphur deficient Zea mays cells: the role of O-acetyl-L-serine in the interaction between nitrogen and sulphur assimilatory pathways. Plant Physiol Biochem. 37:1999;283-290.
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(1999)
Plant Physiol Biochem
, vol.37
, pp. 283-290
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Clarkson, D.1
Diogo, E.2
Amâncio, S.3
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55
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0028151944
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Influence of glutathione (GSH) on net uptake of sulphate and sulphate transport to tobacco plants
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Herschbach C., Rennenberg H. Influence of glutathione (GSH) on net uptake of sulphate and sulphate transport to tobacco plants. J Exp Botany. 45:1994;1069-1076.
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J Exp Botany
, vol.45
, pp. 1069-1076
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Herschbach, C.1
Rennenberg, H.2
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57
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0033119341
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Inter organ signaling in plants: Regulation of ATP sulfurylase and sulfate transporter genes expression in roots mediated by phloem-translocated compound
-
An impressive report that suggests a role for GSH as a phloem-translocated signal molecule that represses the expression of genes encoding ATP sulfurylase and a sulfate transporter. These conclusions are based on the results of 'split root' experiments using A. thaliana and B. napus.
-
Lappartient A.G., Vidmar J.J., Leustek T., Glass A.D.M., Touraine B. Inter organ signaling in plants: regulation of ATP sulfurylase and sulfate transporter genes expression in roots mediated by phloem-translocated compound. Plant J. 18:1999;89-95. An impressive report that suggests a role for GSH as a phloem-translocated signal molecule that represses the expression of genes encoding ATP sulfurylase and a sulfate transporter. These conclusions are based on the results of 'split root' experiments using A. thaliana and B. napus.
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(1999)
Plant J
, vol.18
, pp. 89-95
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-
Lappartient, A.G.1
Vidmar, J.J.2
Leustek, T.3
Glass, A.D.M.4
Touraine, B.5
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58
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0038221650
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Regulation of recombinant soybean serine acetyltransferase by CDPK
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Yoo B-C., Harmon A.C. Regulation of recombinant soybean serine acetyltransferase by CDPK. Plant Physiol Suppl. 114:1997;267.
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Plant Physiol Suppl
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, pp. 267
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Yoo, B.-C.1
Harmon, A.C.2
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59
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0029944852
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Sac1, a putative regulator that is critical for survival of Chlamydomonas reinhardtii during sulfur deprivation
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Davies J.P., Yildiz F., Grossman A. Sac1, a putative regulator that is critical for survival of Chlamydomonas reinhardtii during sulfur deprivation. EMBO J. 15:1996;2150-2159.
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Davies, J.P.1
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Grossman, A.3
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60
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0033149802
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Sac3, an Snf1-like serine/threonine kinase that positively and negatively regulates the responses of Chlamydomonas to sulfur limitation
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This paper and [59] demonstrate the benefits of using the unicellular green algae Chlamydomonas as a model organism in which to study the effects of nutritional stress on signal transduction. Sac3 cDNA was identified by its complementation of a Chlamydomonas Sac3 mutant, which lacked the proper responses to sulfate deprivation. The Sac3 product is a Snf1-related serine/threonine kinase. The involvement of the same product in responses to sulfur deprivation in higher plants is an intriguing possibility.
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Davies J.P., Yildiz F.H., Grossman A.R. Sac3, an Snf1-like serine/threonine kinase that positively and negatively regulates the responses of Chlamydomonas to sulfur limitation. Plant Cell. 11:1999;1179-1190. This paper and [59] demonstrate the benefits of using the unicellular green algae Chlamydomonas as a model organism in which to study the effects of nutritional stress on signal transduction. Sac3 cDNA was identified by its complementation of a Chlamydomonas Sac3 mutant, which lacked the proper responses to sulfate deprivation. The Sac3 product is a Snf1-related serine/threonine kinase. The involvement of the same product in responses to sulfur deprivation in higher plants is an intriguing possibility.
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(1999)
Plant Cell
, vol.11
, pp. 1179-1190
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Davies, J.P.1
Yildiz, F.H.2
Grossman, A.R.3
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61
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0031260404
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The biosynthesis and metabolism of the aspartate derived amino acids in higher plants
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Azevedo R.A., Arruda P., Turner W.L., Lea P.J. The biosynthesis and metabolism of the aspartate derived amino acids in higher plants. Phytochemistry. 46:1997;395-419.
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Phytochemistry
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Azevedo, R.A.1
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Lea, P.J.4
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62
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0001951059
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Lysine, threonine, and methionine biosynthesis
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B.J. Singh. New York: Marcel Dekker, Inc. An excellent review describing the up-to-date information on biosynthesis of amino acids in the aspartate family.
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Matthews B.F. Lysine, threonine, and methionine biosynthesis. Singh B.J. Plant Amino Acids Biochemistry and Biotechnology. 1999;205-225 Marcel Dekker, Inc, New York. An excellent review describing the up-to-date information on biosynthesis of amino acids in the aspartate family.
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Plant Amino Acids Biochemistry and Biotechnology
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Matthews, B.F.1
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63
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Methionine biosynthesis in higher plants. I. Purification and characterization of cystathione γ-synthase from spinach chloroplasts
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Ravanel S., Droux M., Douce R. Methionine biosynthesis in higher plants. I. Purification and characterization of cystathione γ-synthase from spinach chloroplasts. Arch Biochem Biophys. 316:1995;572-584.
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Arch Biochem Biophys
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64
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0032522761
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Cystathione γ-synthase from Arabidopsis thaliana: Purification and biochemical chracterization of the recombinant enzyme overexpressed in Escherichia coli
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The authors describe the first biochemical characterization of recombinant cystathione γ-synthase from plants.
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Ravanel S., Gakiere B., Job D., Douce R. Cystathione γ-synthase from Arabidopsis thaliana: purification and biochemical chracterization of the recombinant enzyme overexpressed in Escherichia coli. Biochem J. 331:1998;639-648. The authors describe the first biochemical characterization of recombinant cystathione γ-synthase from plants.
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Ravanel, S.1
Gakiere, B.2
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65
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Cloning and analysis of the gene for cystathione γ-synthase from Arabidopsis thaliana
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Kim J., Leustek T. Cloning and analysis of the gene for cystathione γ-synthase from Arabidopsis thaliana. Plant Mol Biol. 32:1996;1117-1124.
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66
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0032801372
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Cloning and characterization of cystathione γ-synthase from Solanum tuberosum L
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The cloning of cystathione γ-synthase from potato is reported. The expression pattern of the gene encoding this enzyme exhibits a diurnal rhythm and is induced by light.
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Riedel K., Mangelsdorf C., Streber W., Willmitzer L., Höfgen R., Hesse H. Cloning and characterization of cystathione γ-synthase from Solanum tuberosum L. Plant Biol. 1:1999;638-644. The cloning of cystathione γ-synthase from potato is reported. The expression pattern of the gene encoding this enzyme exhibits a diurnal rhythm and is induced by light.
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Plant Biol
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Riedel, K.1
Mangelsdorf, C.2
Streber, W.3
Willmitzer, L.4
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67
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Methionine biosynthesis in higher plants. II. Purification and characterization of cystathione β-lyase from spinach chloroplasts
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Droux M., Ravanel S., Douce R. Methionine biosynthesis in higher plants. II. Purification and characterization of cystathione β-lyase from spinach chloroplasts. Arch Biochem Biophys. 316:1995;585-595.
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68
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An excellent article describing the current status of our knowledge of Met biosynthesis in plants.
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Ravanel S., Gakiere B., Job D., Douce R. The specific features of methionine biosynthesis and metabolism in plants. Proc Natl Acad Sci USA. 95:1998;7805-7812. An excellent article describing the current status of our knowledge of Met biosynthesis in plants.
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Proc Natl Acad Sci USA
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Ravanel, S.1
Gakiere, B.2
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Cloning of an Arabidopsis thaliana cDNA encoding cystathione β-lyase by functional complementation in Escherichia coli
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Ravanel S., Ruffet M-L., Douce R. Cloning of an Arabidopsis thaliana cDNA encoding cystathione β-lyase by functional complementation in Escherichia coli. Plant Mol Biol. 29:1995;875-882.
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71
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Vitamin-B12-independent methionine synthase from higher plant (Catharanthus roseus). Molecular characterization, regulation, heterologous expression, and enzyme properties
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Eichel J., Gonzalez J.C., Hotze M., Matthews R.G., Schröder J. Vitamin-B12-independent methionine synthase from higher plant (Catharanthus roseus). Molecular characterization, regulation, heterologous expression, and enzyme properties. Eur J Biochem. 230:1995;1053-1058.
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Petersen M., Van Der Straeten D., Bauw G. Full-length cDNA clone from Coleus blumei (GenBank Z49150) with high similarity to cobalamine-independent methionine synthase. Plant Physiol. 109:1995;338.
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73
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0032696044
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Evidence for authoregulation of cystathione γ-synthase mRNA stability in Arabidospsis
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The authors present a molecular analysis of Arabidopsis mutants that overproduce Met. They propose a unique mechanism through which stable levels of the mRNA encoding cystathione γ-synthase are maintained by the repression of this enzyme by its own translational product (i.e. cystathione γ-synthase) in the presence of Met (or its metabolites).
-
Chiba Y., Ishikawa M., Kijima F., Tyson R.H., Kim J., Yamamoto A., Nambara E., Leustek T., Wallsgrove R.M., Naito S. Evidence for authoregulation of cystathione γ-synthase mRNA stability in Arabidospsis. Science. 286:1999;1371-1374. The authors present a molecular analysis of Arabidopsis mutants that overproduce Met. They propose a unique mechanism through which stable levels of the mRNA encoding cystathione γ-synthase are maintained by the repression of this enzyme by its own translational product (i.e. cystathione γ-synthase) in the presence of Met (or its metabolites).
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Science
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Chiba, Y.1
Ishikawa, M.2
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Tyson, R.H.4
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Nambara, E.7
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74
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Repression of cystathione γ-synthase in Arabidopsis thaliana produces partial methonine auxotrophy and developmental abnormalities
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Kim J., Leustek T. Repression of cystathione γ-synthase in Arabidopsis thaliana produces partial methonine auxotrophy and developmental abnormalities. Plant Sci. 151:2000;9-18.
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Kim, J.1
Leustek, T.2
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S-Methylmethionine plays a major role in phloem sulfur transport and is synthesized by a novel type of methyltransferase
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Analysis of phloem sap moving towards wheat ears showed that S-methylmethionine is the major sulfur-containing compound in phloem sap. S-methylmethionine concentration in the phloem sap was 1.5 times that of GSH, suggesting that S-methylmethionine is the major form of sulfur transported in phloem. A unique methyltransferase that is responsible for the production of S-methylmethionine was cloned from several plant species.
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Bourgis F., Roje S., Nuccio M.L., Fisher D.B., Tarczynski M.C., Li C., Herschbach C., Rennenberg H., Pimenta M.J., Shen T-L.et al. S-Methylmethionine plays a major role in phloem sulfur transport and is synthesized by a novel type of methyltransferase. Plant Cell. 11:1999;1485-1497. Analysis of phloem sap moving towards wheat ears showed that S-methylmethionine is the major sulfur-containing compound in phloem sap. S-methylmethionine concentration in the phloem sap was 1.5 times that of GSH, suggesting that S-methylmethionine is the major form of sulfur transported in phloem. A unique methyltransferase that is responsible for the production of S-methylmethionine was cloned from several plant species.
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(1999)
Plant Cell
, vol.11
, pp. 1485-1497
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Bourgis, F.1
Roje, S.2
Nuccio, M.L.3
Fisher, D.B.4
Tarczynski, M.C.5
Li, C.6
Herschbach, C.7
Rennenberg, H.8
Pimenta, M.J.9
Shen, T.-L.10
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