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SULTR2;1 is a low-affinity sulfate transporter expressed in the vascular tissues of roots and leaves for interorgan transport of sulfate in Arabidopsis thaliana. Transgenic Arabidopsis carrying a fusion gene construct of SULTR2;1 5′-promoter region and β-glucuronidase coding sequence (GUS) demonstrated that within the reproductive tissues, SULTR2;1 is specifically expressed in the bases and veins of siliques and in the funiculus, which connects the seeds and the silique. The antisense suppression of SULTR2;1 mRNA caused decrease of sulfate contents in seeds and of thiol contents both in seeds and leaves, as compared with the wildtype (WT). The effect of antisense suppression of SULTR2;1 on seed sulfur status was determined by introducing a sulfur-indicator construct, p35S::βSRx3:GUS, which drives the expression of GUS reporter under a chimeric cauliflower mosaic virus 35S promoter containing a triplicate repeat of sulfur-responsive promoter region of soybean β-conglycinin β subunit (βSRx3). The mature seeds of F1 plants carrying both the SULTR2;1 antisense and p35S::βSRx3:GUS constructs exhibited significant accumulation of GUS activities on sulfur deficiency, as compared with those carrying only the p35S::βSRx3:GUS construct in the WT background. These results suggested that SULTR2;1 is involved in controlling translocation of sulfate into developing siliques and may modulate the sulfur status of seeds in A. thaliana. [ABSTRACT FROM AUTHOR]

The accumulation of labelled ions was measured in seedlings of Arabidopsis thaliana (L.) Heynh. grown in submerged cultures. Genotypes used were wild type and the nitrate-uptake mutant B1, which is altered in the uptake of nitrate and chlorate from concentrations above 1 mM when grown under normal conditions. At low and high concentrations of chlorate, chloride, and K+, significantly less radioactivity was accumulated in seedlings of B1 than in seedlings of wild type. The influx of sulphate did not decrease in B1. The results indicate that the effect of the mutation in B1 is restricted to the uptake of monovalent ions. [ABSTRACT FROM AUTHOR]