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J. Biol. Chem., Vol. 269, Issue 45, 28010-28016, 11, 1994
CR McMaster and RM Bell
The Saccharomyces cerevisiae CPT1 and EPT1 genes encode distinct choline-
and choline/ethanolaminephosphotransferases, respectively. In vitro, each
gene product accounts for 50% of the measurable choline- phosphotransferase
activity. Strains containing null mutations in the CPT1 and EPT1 loci were
used to investigate the function of each gene product in vivo. The CPT1
gene product was responsible for 95% of phosphatidylcholine (PC) synthesis
via the CDP-choline pathway in vivo. The EPT1 gene product accounted for
only 5% of PC synthesis in vivo. Chimeric CPT1/EPT1 enzymes with
diacylglycerol and CDP-aminoalcohol specificities both similar and distinct
from the parental enzymes were used to determine the specific segments of
the CPT1/EPT1 gene products required to restore PC synthesis to cpt- cells
in vivo. Only chimeras expressing the CDP-aminoalcohol specificity region
of CPT1 were capable of PC synthesis via the CDP-choline pathway in vivo.
Analysis of phospholipids extracted from wild type, cpt-, and ept- cells
labeled with 32Pi indicated an intact CPT1 gene product was required for
the pleiotropic regulation of phospholipid synthesis by inositol. Chimeric
CPT1/EPT1 enzymes expressed in a cpt- background mapped the regulatory
region of the CPT1 gene product required for the inositol-dependent
regulation of phospholipid synthesis to the CDP-aminoalcohol binding domain
of CPT1. Strains harboring dysfunctional cholinephosphotransferase enzymes
also displayed decreased levels of choline uptake, suggesting that a
feedback loop exists to coordinate choline uptake with ongoing PC
biosynthesis. The data also implicate the CPT1 gene product in PC
biosynthesis from an endogenous source of choline derived from turnover of
PC via the phosphatidylserine- dependent route for PC synthesis.
Phosphatidylcholine biosynthesis in Saccharomyces cerevisiae. Regulatory insights from studies employing null and chimeric sn-1,2- diacylglycerol choline- and ethanolaminephosphotransferases
Department of Molecular Cancer Biology, Duke University Medical Center, Durham, North Carolina 27710.
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