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- W1582882798 abstract "1A temperature-sensitive mutant of Saccharomyces cerevisiae with a lesion in cholinephosphate cytidyltransferase was isolated from a choline auxotroph. This mutant grew in a medium supplemented with ethanolamine or N-methylethanolamine, but at a much slower rate in a medium supplemented with choline or N,N-dimethylethanolamine at 37 °C. At 23 °C, mutant cells grew at the same rate in any of these media.2Labelling experiments showed that the activity of phosphatidylcholine synthesis from choline in the mutant was thermolabile and rapidly lost on incubation of cells at 37 °C (half-life, 4 min).3Determination of the intermediates and the enzyme activities of the CDP-choline pathway indicated that mutant cells had a lesion in cholinephosphate cytidyltransferase.4Genetic analysis showed that the thermolabile phosphatidylcholine synthesis in the mutant arose from a single mutation in a gene coding for cholinephosphate cytidyltransferase.5The mutant strain was found to be defective in dCDP-choline synthesis. Thus, a single enzyme is responsible for the synthesis of both CDP-choline and dCDP-choline.6Ethanolaminephosphate cytidyltransferase activity in the mutant was comparable to that in the parental strain. An alteration in cholinephosphate cytidyltransferase did not affect the incorporation of labelled ethanolamine into lipids. These results indicate that ethanolaminephosphate cytidyltranferase is coded for by a distinct gene from that for cholinephosphate cytidyltransferase.7The CDP-choline pathway was not required by cells as long as phosphatidylcholine was supplied via the phosphatidylethanolamine methylation pathway. The phosphatidylethanolamine methylation pathway and the CDP-choline pathway were found to be complementary to each other in phosphatidylcholine synthesis." @default.
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- W1582882798 date "1983-03-01" @default.
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- W1582882798 title "Yeast Mutant with Thermolabile CDP-choline Synthesis. Isolation and Characterization of a Cholinephosphate Cytidyltransferase Mutant" @default.
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- W1582882798 doi "https://doi.org/10.1111/j.1432-1033.1983.tb07253.x" @default.
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