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Plant Physiol, June 2000, Vol. 123, pp. 497-508
The Role of Pyruvate Dehydrogenase and Acetyl-Coenzyme
A Synthetase in Fatty Acid Synthesis in Developing
Arabidopsis Seeds1
Jinshan
Ke,2
Robert H.
Behal,2
Stephanie L.
Back,
Basil J.
Nikolau,
Eve Syrkin
Wurtele, and
David
J.
Oliver*
Department of Botany (J.K., R.H.B., S.L.B., E.S.W., D.J.O.) and
Department of Biochemistry, Biophysics, and Molecular Biology (B.J.N.),
Iowa State University, Ames, Iowa 50011
Acetyl-coenzyme A (acetyl-CoA) formed within the plastid is the
precursor for the biosynthesis of fatty acids and, through them, a
range of important biomolecules. The source of acetyl-CoA in the
plastid is not known, but two enzymes are thought to be involved:
acetyl-CoA synthetase and plastidic pyruvate dehydrogenase. To
determine the importance of these two enzymes in synthesizing acetyl-CoA during lipid accumulation in developing Arabidopsis seeds,
we isolated cDNA clones for acetyl-CoA synthetase and for the ptE1 -
and ptE1 -subunits of plastidic pyruvate dehydrogenase. To our
knowledge, this is the first reported acetyl-CoA synthetase sequence
from a plant source. The Arabidopsis acetyl-CoA synthetase preprotein
has a calculated mass of 76,678 D, an apparent plastid targeting
sequence, and the mature protein is a monomer of 70 to 72 kD. During
silique development, the spatial and temporal patterns of the ptE1
mRNA level are very similar to those of the mRNAs for the plastidic
heteromeric acetyl-CoA carboxylase subunits. The pattern of ptE1
mRNA accumulation strongly correlates with the formation of lipid
within the developing embryo. In contrast, the level of mRNA for
acetyl-CoA synthetase does not correlate in time and space with lipid
accumulation. The highest level of accumulation of the mRNA for
acetyl-CoA synthetase during silique development is within the
funiculus. These mRNA data suggest a predominant role for plastidic
pyruvate dehydrogenase in acetyl-CoA formation during lipid synthesis
in seeds.
1
This work was supported by the National Science
Foundation (grant no. IBN-9696154), Consortium for Plant
Biotechnology, U.S. Department of Agriculture-National Research
Initiative (competitive grant no. 97-01912), and the Monsanto Company,
and is a publication of the Iowa Agricultural Experiment Station.
Microscopy was conducted at the Iowa State University Bessey Microscopy Facility.
2
These authors contributed equally to the paper.
*
Corresponding author; e-mail doliver{at}iastate.edu; fax
515- 294-1337.
© 2000 American Society of Plant Physiologists
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