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Volumn 3, Issue 3, 2000, Pages 188-195

Regulation of sulfate transport and synthesis of sulfur-containing amino acids

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EID: 0034078554     PISSN: 13695266     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1369-5266(00)00063-7     Document Type: Review
Times cited : (269)

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    • •] 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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    • 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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    • Increased resistance to oxidative stress in transgenic tobacco plants overexpressing bacterial serine acetyltransferase
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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.
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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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    • 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.
    • 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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    • The authors describe the first biochemical characterization of recombinant cystathione γ-synthase from plants.
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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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    • 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).
    • (1999) Science , vol.286 , pp. 1371-1374
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    • S-Methylmethionine plays a major role in phloem sulfur transport and is synthesized by a novel type of methyltransferase
    • 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.
    • 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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