Vacuolar Sulfate Transporters Are Essential Determinants Controlling Internal Distribution of Sulfate in Arabidopsis

Kataoka, Takahito; Watanabe-Takahashi, Akiko; Hayashi, Naomi; Ohnishi, Miwa; Mimura, Tetsuro; Büchner, Peter; Hawkesford, Malcolm J.; Yamaya, Tomoyuki; Takahashi, Hideki

doi:10.1105/tpc.104.023960

Cited by 289 publications

(258 citation statements)

References 44 publications

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“…A similar up-regulation of sulfate transporters as well as of genes involved in sulfate assimilation (Leustek et al, 1994;Gutierrez-Marcos et al, 1996;Setya et al, 1996) and Cys synthesis (Hatzfeld et al, 2000;Kawashima et al, 2005) was observed in earlier studies where plants were subjected to S deficiency (Takahashi et al, 1997(Takahashi et al, , 2000Yoshimoto et al, 2002;Maruyama-Nakashita et al, 2003, 2005Kataoka et al, 2004). Thus, selenate may be perceived by the plant as S deficiency, or even cause deficiency of certain S-containing metabolites.…”

Section: Discussionmentioning

confidence: 54%

Overexpression of AtCpNifS Enhances Selenium Tolerance and Accumulation in Arabidopsis

et al. 2005

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Selenium (Se) is an essential element for many organisms but is toxic at higher levels. CpNifS is a chloroplastic NifS-like protein in Arabidopsis (Arabidopsis thaliana) that can catalyze the conversion of cysteine into alanine and elemental sulfur (S 0 ) and of selenocysteine into alanine and elemental Se (Se 0 ). We overexpressed CpNifS to investigate the effects on Se metabolism in plants. CpNifS overexpression significantly enhanced selenate tolerance (1.9-fold) and Se accumulation (2.2-fold). CpNifS overexpressors showed significantly reduced Se incorporation into protein, which may explain their higher Se tolerance. Also, sulfur accumulation was enhanced by approximately 30% in CpNifS overexpressors, both on media with and without selenate. Root transcriptome changes in response to selenate mimicked the effects observed under sulfur starvation. There were only a few transcriptome differences between CpNifS-overexpressing plants and wild type, besides the 25-to 40-fold increase in CpNifS levels. Judged from x-ray analysis of near edge spectrum, both CpNifS overexpressors and wild type accumulated mostly selenate (Se VI ). In conclusion, overexpression of this plant NifS-like protein had a pronounced effect on plant Se metabolism. The observed enhanced Se accumulation and tolerance of CpNifS overexpressors show promise for use in phytoremediation.

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Section: Discussionmentioning

confidence: 54%

Overexpression of AtCpNifS Enhances Selenium Tolerance and Accumulation in Arabidopsis

et al. 2005

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“…Biochemical characteristics together with distinct patterns of gene expression and protein localization indicate that different sulfate transporters fulfill different roles in plants, including high-affinity uptake of soil sulfate into roots, translocation in vascular tissues, and cell-to-cell transfer of sulfate in leaves and seeds (Hawkesford, 2003). Although some plant sulfate transporters are located in the plasma membrane (Kataoka et al, 2004a), at least one has been found elsewhere, on the tonoplast (Kataoka et al, 2004b). Genetic evidence reinforces the notion that plant sulfate transporters have become specialized during evolution, although a certain level of redundancy remains.…”

Section: Discussionmentioning

confidence: 99%

The Sulfate Transporter SST1 Is Crucial for Symbiotic Nitrogen Fixation in Lotus japonicus Root Nodules

et al. 2005

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Symbiotic nitrogen fixation (SNF) by intracellular rhizobia within legume root nodules requires the exchange of nutrients between host plant cells and their resident bacteria. Little is known at the molecular level about plant transporters that mediate such exchanges. Several mutants of the model legume Lotus japonicus have been identified that develop nodules with metabolic defects that cannot fix nitrogen efficiently and exhibit retarded growth under symbiotic conditions. Mapbased cloning of defective genes in two such mutants, sst1-1 and sst1-2 (for symbiotic sulfate transporter), revealed two alleles of the same gene. The gene is expressed in a nodule-specific manner and encodes a protein homologous with eukaryotic sulfate transporters. Full-length cDNA of the gene complemented a yeast mutant defective in sulfate transport. Hence, the gene was named Sst1. The sst1-1 and sst1-2 mutants exhibited normal growth and development under nonsymbiotic growth conditions, a result consistent with the nodule-specific expression of Sst1. Data from a previous proteomic study indicate that SST1 is located on the symbiosome membrane in Lotus nodules. Together, these results suggest that SST1 transports sulfate from the plant cell cytoplasm to the intracellular rhizobia, where the nutrient is essential for protein and cofactor synthesis, including nitrogenase biosynthesis. This work shows the importance of plant sulfate transport in SNF and the specialization of a eukaryotic transporter gene for this purpose.

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“…Examples are the outward potassium channel SKOR (Gaymard et al, 1998), the effluxtype boron transporter BOR1 (Takano et al, 2002), the tonoplast sulfate transporters SULTR4;1 and SULTR4;2 (Kataoka et al, 2004b), the plasma membrane sulfate transporters, SULTR2;1 (A) Low-affinity nitrate uptake activity. Oocytes were incubated for 3 h with 10 mM nitrate, pH 5.5, and nitrate retained in the oocyte was measured by HPLC.…”

Section: The Pericycle Cells Close To the Protoxylem Play A Special Rmentioning

confidence: 99%

Mutation of the Arabidopsis NRT1.5 Nitrate Transporter Causes Defective Root-to-Shoot Nitrate Transport

et al. 2008

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Little is known about the molecular and regulatory mechanisms of long-distance nitrate transport in higher plants. NRT1.5 is one of the 53 Arabidopsis thaliana nitrate transporter NRT1 (Peptide Transporter PTR) genes, of which two members, NRT1.1 (CHL1 for Chlorate resistant 1) and NRT1.2, have been shown to be involved in nitrate uptake. Functional analysis of cRNA-injected Xenopus laevis oocytes showed that NRT1.5 is a low-affinity, pH-dependent bidirectional nitrate transporter. Subcellular localization in plant protoplasts and in planta promoter-b-glucuronidase analysis, as well as in situ hybridization, showed that NRT1.5 is located in the plasma membrane and is expressed in root pericycle cells close to the xylem. Knockdown or knockout mutations of NRT1.5 reduced the amount of nitrate transported from the root to the shoot, suggesting that NRT1.5 participates in root xylem loading of nitrate. However, root-to-shoot nitrate transport was not completely eliminated in the NRT1.5 knockout mutant, and reduction of NRT1.5 in the nrt1.1 background did not affect rootto-shoot nitrate transport. These data suggest that, in addition to that involving NRT1.5, another mechanism is responsible for xylem loading of nitrate. Further analyses of the nrt1.5 mutants revealed a regulatory loop between nitrate and potassium at the xylem transport step. INTRODUCTIONNitrate and ammonium ions are the two major nitrogen sources for higher plants. Due to its toxicity, ammonium is preferentially assimilated in the root and then transported in an organic form to the aerial parts. By contrast, nitrate can be assimilated into ammonium and then amino acids in the root or shoot. Partitioning of nitrate assimilation between the root and shoot depends on the plant species, external nitrate concentration, temperature, and light intensity (reviewed in Smirnoff and Stewart, 1985). If there is sufficient light, nitrate assimilation in the leaf has a lower energy cost than in the root. However, some disadvantages of leaf nitrate assimilation include (1) if light is limited, nitrate assimilation and carbon dioxide fixation will compete directly for the reductants and ATP generated by photosynthetic electron transport (Canvin and Atkins, 1974), and (2) hydroxyl ions generated in the leaf need to be neutralized by the synthesis of organic acids (in the root, the pH balance may possibly be maintained by reducing proton excretion or increasing bicarbonate excretion). Due to these factors, the partition of nitrate assimilation between the root and shoot shows both seasonal and diurnal fluctuations, allowing the plant to sustain maximal growth. In turn, the partition of nitrate assimilation depends on the partition of nitrate between the root and shoot.To transport nitrate to the aerial parts of the plant, nitrate has to be loaded into the xylem vessels of the root vascular stele. In Arabidopsis thaliana roots, four layers of cells are found surrounding the xylem, these being the epidermis, cortex, endodermis, and pericycle (in the order external to ...

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Vacuolar Sulfate Transporters Are Essential Determinants Controlling Internal Distribution of Sulfate in Arabidopsis

Cited by 289 publications

References 44 publications

Overexpression of AtCpNifS Enhances Selenium Tolerance and Accumulation in Arabidopsis

Overexpression of AtCpNifS Enhances Selenium Tolerance and Accumulation in Arabidopsis

The Sulfate Transporter SST1 Is Crucial for Symbiotic Nitrogen Fixation in Lotus japonicus Root Nodules

Mutation of the Arabidopsis NRT1.5 Nitrate Transporter Causes Defective Root-to-Shoot Nitrate Transport

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