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Expression of a maize sucrose phosphate synthase in tomato alters leaf carbohydrate partitioning.
Author(s) -
A. C. Worrell,
J M Bruneau,
Kristin R. Summerfelt,
Michael R. Boersig,
Toni A. Voelker
Publication year - 1991
Publication title -
the plant cell
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.324
H-Index - 341
eISSN - 1532-298X
pISSN - 1040-4651
DOI - 10.1105/tpc.3.10.1121
Subject(s) - sucrose phosphate synthase , biology , biochemistry , sucrose synthase , complementary dna , sucrose , enzyme , atp synthase , pyruvate carboxylase , rubisco , peptide sequence , phosphoenolpyruvate carboxylase , gene , invertase
We isolated a complementary DNA sequence for the enzyme sucrose phosphate synthase (SPS) from maize utilizing a limited amino acid sequence. The 3509-bp cDNA encodes a 1068-amino acid polypeptide. The identity of the cDNA was confirmed by the ability of the cloned sequence to direct sucrose phosphate synthesis in Escherichia coli. Because no plant-specific factors were necessary for enzymatic activity, we can conclude that SPS enzyme activity is conferred by a single gene product. Sequence comparisons showed that SPS is distantly related to the enzyme sucrose synthase. When expressed from a ribulose bisphosphate carboxylase small subunit promoter in transgenic tomatoes, total SPS activity was boosted up to sixfold in leaves and appeared to be physiologically uncoupled from the tomato regulation mechanism. The elevated SPS activity caused a reduction of starch and increase of sucrose in the tomato leaves. This result clearly demonstrates that SPS is involved in the regulation of carbon partitioning in the leaves.

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