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A Heteromeric Plastidic Pyruvate Kinase Complex Involved in Seed Oil Biosynthesis in Arabidopsis^[W]

^a Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, Michigan 48824
^b U.S. Department of Energy–Plant Research Laboratory, Michigan State University, East Lansing, Michigan 48824
^c Department of Plant Biology, Michigan State University, East Lansing, Michigan 48824

¹ To whom correspondence should be addressed. E-mail benning{at}msu.edu; fax 517-353-9334.

Glycolysis is a ubiquitous pathway thought to be essential for the production of oil in developing seeds of Arabidopsis thaliana and oil crops. Compartmentation of primary metabolism in developing embryos poses a significant challenge for testing this hypothesis and for the engineering of seed biomass production. It also raises the question whether there is a preferred route of carbon from imported photosynthate to seed oil in the embryo. Plastidic pyruvate kinase catalyzes a highly regulated, ATP-producing reaction of glycolysis. The Arabidopsis genome encodes 14 putative isoforms of pyruvate kinases. Three genes encode subunits , ß₁, and ß₂ of plastidic pyruvate kinase. The plastid enzyme prevalent in developing seeds likely has a subunit composition of 44ß₁, is most active at pH 8.0, and is inhibited by Glu. Disruption of the gene encoding the ß₁ subunit causes a reduction in plastidic pyruvate kinase activity and 60% reduction in seed oil content. The seed oil phenotype is fully restored by expression of the ß₁ subunit–encoding cDNA and partially by the ß₂ subunit–encoding cDNA. Therefore, the identified pyruvate kinase catalyzes a crucial step in the conversion of photosynthate into oil, suggesting a preferred plastid route from its substrate phosphoenolpyruvate to fatty acids.

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