PMID: 11925045Apr 2, 2002Paper

Starch biosynthesis from triose-phosphate in transgenic potato tubers expressing plastidic fructose-1,6-bisphosphatase

Planta
Tine ThorbjørnsenTom H. Nielsen

Abstract

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 tran...Continue Reading

Citations

Mar 28, 2009·Journal of Experimental Botany·Antonio Jesús SerratoMariam Sahrawy
Mar 12, 2008·The FEBS Journal·Allan StensballeKaren G Welinder
Mar 18, 2015·Bioscience, Biotechnology, and Biochemistry·Masahiro Tamoi, Shigeru Shigeoka

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