Plant Physiology 100:923-930 (1992)
© 1992 American Society of Plant Biologists
Metabolism and Enzymology
Regulation of Plant Fatty Acid Biosynthesis 1
Analysis of Acyl-Coenzyme A and Acyl-Acyl Carrier Protein Substrate Pools in Spinach and Pea Chloroplasts
Dusty Post-Beittenmiller2,
Grattan Roughan3 and
John B. Ohlrogge
Department of Botany and Plant Pathology, Michigan State University, East Lansing, Michigan 48824-1312,
Division of Horticulture and Processing, Department of Scientific and Industrial Research, Mt. Albert Research Centre, Private Bag, Auckland, New Zealand
In previous work (D. Post-Beittenmiller, J.G. Jaworski, J.B. Ohlrogge [1991] J Biol Chem 266: 1858-1865), the in vivo acyl-acyl carrier protein (ACP) pools were measured in spinach (Spinacia oleracea) leaves and changes in their levels were compared to changes in the rates of fatty acid biosynthesis. To further examine the pools of substrates and cofactors for fatty acid biosynthesis and to evaluate metabolic regulation of this pathway, we have now examined the coenzyme A (CoA) and short chain acyl-CoA pools, including acetyl- and malonyl-CoA, in isolated spinach and pea (Pisum sativum) chloroplasts. In addition, the relationships of the acetyl- and malonyl-CoA pools to the acetyl- and malonyl-ACP pools have been evaluated. These studies have led to the following conclusions: (a) Essentially all of the CoA (31-54 µM) in chloroplasts freshly isolated from light-grown spinach leaves or pea seedling was in the form of acetyl-CoA. (b) Chloroplasts contain at least 77% of the total leaf acetyl-CoA, based on comparison of acetyl-CoA levels in chloroplasts and total leaf. (c) CoA-SH was not detected either in freshly isolated chloroplasts or in incubated chloroplasts and is, therefore, less than 2 µM in the stroma. (d) The malonyl-CoA:ACP transacylase reaction is near equilibrium in both light- and dark-incubated chloroplasts, whereas the acetyl-CoA:ACP transacylase reaction is far from equilibrium in light-incubated chloroplasts. However, the acetyl-CoA:ACP transacylase reaction comes nearer to equilibrium when chloroplasts are incubated in the dark. (e) Malonyl-CoA and -ACP could be detected in isolated chloroplasts only during light incubations, and increased with increased rates of fatty acid biosynthesis. In contrast, both acetyl-CoA and acetyl-ACP were detectable in the absence of fatty acid biosynthesis, and acetyl-ACP decreased with increased rates of fatty acid biosynthesis. Together these data have provided direct in situ evidence that acetyl-CoA carboxylase plays a regulatory role in chloroplast fatty acid biosynthesis.
2 Present address: Plant Genetics Section, The Samuel Roberts Noble Foundation, Inc., P.O. Box 2180, Ardmore, OK 73402.
3 G.R. was the recipient of a Fulbright travel award.
1 This research was supported by National Science Foundation grant DCB 9005290. Acknowledgment is also made to the Michigan Agricultural Experiment Station for its support of this research.
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