A full length cDNA clone encoding plastidic fructose-1,6-bisphosphatase (cp-FBPase), together with a transit peptide, was isolated from a potato (Solanum tuberosum L.) leaf cDNA library. Potato plants were transformed with the isolated cp-FBPase sequence behind a patatin class I promoter to ensure tuber-specific expression of the enzyme. Plant lines were selected which expressed up to 250 mU (g FW)–1 in the developing tubers, which is 10- to 20-fold the activity found in wild-type tubers. Intact amyloplasts were isolated from in vitro-grown minitubers developed in darkness. Comparison with marker enzymes showed that cp-FBPase activity in transgenic tubers, as well as the low FBPase activity in the wild-type tubers, was localised inside the amyloplasts. The intact amyloplasts isolated from both wild-type and transgenic tubers synthesised starch from [U-14C]glucose-6-phosphate. Conversely, only the transgenic tubers expressing cp-FBPase showed appreciable synthesis of starch from [U-14C]dihydroxyacetone phosphate, and this synthesis rate was correlated to the activity of cp-FBPase. Thus, the expression of cp-FBPase in tubers allows for a new route of starch biosynthesis from triose-phosphates imported from the cytosol. The transgenic tubers did not differ from wild-type tubers with respect to starch content, or the levels of neutral sugars and phosphorylated hexoses.
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Thorbjørnsen, T., Asp, T., Jørgensen, K. et al. Starch biosynthesis from triose-phosphate in transgenic potato tubers expressing plastidic fructose-1,6-bisphosphatase. Planta 214, 616–624 (2002). https://doi.org/10.1007/s004250100647
- Amyloplast Carbohydrate metabolism Plastidic fructose-1,6-bisphosphatase Solanum (starch biosynthesis) Starch biosynthesis Transgenic potato tubers