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A Heteromeric Plastidic Pyruvate Kinase Complex Involved in Seed Oil Biosynthesis in Arabidopsis

Carl Andre, John E. Froehlich, Matthew R. Moll and Christoph Benning
The Plant Cell
Vol. 19, No. 6 (Jun., 2007), pp. 2006-2022
Stable URL: http://www.jstor.org/stable/20077076
Page Count: 17
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
A Heteromeric Plastidic Pyruvate Kinase Complex Involved in Seed Oil Biosynthesis in Arabidopsis
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Abstract

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 α, β₁, and β₂ of plastidic pyruvate kinase. The plastid enzyme prevalent in developing seeds likely has a subunit composition of 4α4β₁, is most active at pH 8.0, and is inhibited by Glu. Disruption of the gene encoding the β₁ 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 β₁ subunit-encoding cDNA and partially by the β₂ 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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