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J. Biol. Chem., Vol. 255, Issue 4, 1623-1629, Feb, 1980

Phosphatidic acid accumulation in the membranes of Escherichia coli mutants defective in CDP-diglyceride synthetase

BR Ganong, JM Leonard and CR Raetz

CTP-phosphatidic acid cytidylyltransferase (CDP-diglyceride synthetase) is a key enzyme in the biogenesis of membrane phospholipids in Escherichia coli. Using a modification of a previously described autoradiographic screening procedure (Raetz, C. R. H. (1975) Proc. Natl. Acad. Sci. U.S.A. 72, 2274-2278), we have isolated six mutant strains in which the specific activity of the synthetase is 1 to 10% that of the wild type, as judged by in vitro assays. The synthesis of dCDP-diglyceride, as well as CDP-diglyceride, is defective in these organisms. The mutations responsible for the enzyme defects (designated cds) all map in the same location near minute 4 on the chromosome. Although none of the mutants obtained are temperature-sensitive for growth, all of them exhibit significantly elevated levels of phosphatidic acid in vivo. The highest increase is observed in the mutant GL60, in which phosphatidic acid constitutes about 5% of the membrane lipid, in contrast to 0.2% in typical wild type strains. The accumulation of phosphatidic acid occurs primarily at the expense of phosphatidylglycerol and cardiolipin, but the total lipid-to-protein ratio of GL60 is nearly normal. In vivo labeling of GL60 with 32Pi suggests that the increased phosphatidic acid pool is the result of a partial metabolic block early in the phospholipid pathway, but that most of this expanded pool is nonetheless available for de novo synthesis.
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