Phytophthora infestans cholinephosphotransferase with substrate specificity for very-long-chain polyunsaturated fatty acids

  1. Get@NRC: Phytophthora infestans cholinephosphotransferase with substrate specificity for very-long-chain polyunsaturated fatty acids (Opens in a new window)
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Journal titleApplied and Environmental Microbiology
Pages15731579; # of pages: 7
SubjectArachidonic acids; Diacylglycerol; Docosahexaenoic acid; Eicosapentaenoic acid; In-vitro assays; Neutral lipid; Oomycetes; Phosphatidylcholine; Phosphotransferases; Phytophthora infestans; Real-time PCR; Substrate specificity; Very-long-chain polyunsaturated fatty acids; Glycerol; Phospholipids; Polymerase chain reaction; Yeast; Substrates; cholinephosphotransferase; complementary DNA; enzyme specificity; enzymology; Saccharomyces cerevisiae; Amino Acid Sequence; Diacylglycerol Cholinephosphotransferase; DNA, Complementary; Fatty Acids, Unsaturated; Gene Expression Profiling; Molecular Sequence Data; Real-Time Polymerase Chain Reaction; Saccharomyces cerevisiae; Sequence Alignment; Sequence Analysis, DNA; Sequence Homology, Amino Acid; Substrate Specificity
AbstractThe effective flux between phospholipids and neutral lipids is critical for a high level of biosynthesis and accumulation of verylong-chain polyunsaturated fatty acids (VLCPUFAs), such as arachidonic acid (ARA; 20:4n-6), eicosapentaenoic acid (EPA; 20: 5n-3), and docosahexaenoic acid (DHA; 22:6n-3). Here we describe a cDNA (PiCPT1) from Phytophthora infestans, a VLCPUFAproducing oomycete, that may have a role in acyl trafficking between diacylglycerol (DAG) and phosphatidylcholine (PC) during the biosynthesis of VLCPUFAs. The cDNA encodes a polypeptide of 393 amino acids with a conserved CDP-alcohol phosphotransferase motif and approximately 27% amino acid identity to the Saccharomyces cerevisiae cholinephosphotransferase (ScCPT1). In vitro assays indicate that PiCPT1 has high cholinephosphotransferase (CPT) activity but no ethanolaminephosphotransferase (EPT) activity. Substrate specificity assays show that it prefers VLCPUFA-containing DAGs, such as ARA DAG and DHA DAG, as substrates. Real-time PCR analysis reveals that expression of PiCPT1 was upregulated in P. infestans organisms fed with exogenous VLCPUFAs. These results lead us to conclude that PiCPT1 is a VLCPUFA-specific CPT which may play an important role in shuffling VLCPUFAs from DAG to PC in the biosynthesis of VLCPUFAs in P. infestans.
Publication date
AffiliationAquatic and Crop Resource Development; National Research Council Canada
Peer reviewedYes
NPARC number21270362
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Record identifierf5495721-4b2e-412f-8137-2d9c702d4f50
Record created2014-02-05
Record modified2016-05-09
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