| DOI | Resolve DOI: https://doi.org/10.1128/AEM.03250-12 |
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| Author | Search for: Chen, Yan; Search for: Chi, Hsiang-yun; Search for: Meesapyodsuk, Dauenpen1; Search for: Qiu, Xiao1 |
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| Affiliation | - National Research Council of Canada. Aquatic and Crop Resource Development
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| Format | Text, Article |
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| Subject | Arachidonic 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 |
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| Abstract | The 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. |
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| Publication date | 2011-12-28 |
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| In | |
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| Language | English |
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| Peer reviewed | Yes |
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| NPARC number | 21270362 |
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| Export citation | Export as RIS |
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| Report a correction | Report a correction (opens in a new tab) |
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| Record identifier | f5495721-4b2e-412f-8137-2d9c702d4f50 |
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| Record created | 2014-02-05 |
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| Record modified | 2020-04-21 |
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