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Identification of phospholipase B from Dictyostelium discoideum reveals a new lipase family present in mammals, flies and nematodes, but not yeast
Open accessAbstract
The social amoeba Dictyostelium discoideum exhibits high activities of phospholipase and lysophospholipase [Ferber, Munder, Fischer and Gerisch (1970) Eur. J. Biochem. 14, 253–257]. We assayed Dictyostelium lysates to demonstrate the presence of a highly active phospholipase B (PLB) enzyme that removed both fatty-acid chains from phosphatidylcholine and produced the water-soluble glycerophosphorylcholine. We purified the PLB activity from Dictyostelium cytosol using standard agarose media (size exclusion and ion exchange), and combined this with an affinity purification step using myristoylated ARF1 (ADP-ribosylation factor 1), a protein which has a single fatty acid at its N-terminus. Two proteins co-purified (48 kDa and 65 kDa), and the 48 kDa protein was digested with trypsin, peptide fragments were separated by reverse-phase chromatography, and the resultant peptides were sequenced by Edman degradation. From the peptide sequences obtained, database searches revealed a gene which encodes a protein of 65 kDa with unknown function. The 48 kDa protein therefore appears to be a fragment of the full-length 65 kDa product. Expression of the gene in Escherichia coli confirmed that it encodes a PLB. Characterization of its substrate specificity indicated that, in addition to phosphatidylcholine deacylation, the enzyme also hydrolysed phosphatidylinositol and phosphatidylethanolamine. The PLB identified in the present study is not related to existing PLBs found in bacteria, fungi or mammals. There are, however, genes similar to Dictyostelium PLB in mammals, flies, worms and Giardia, but not in yeast. We therefore have identified a novel family of intracellular PLBs.
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The substrates of these phospholipases B have been shown to be diacylglycerol-phosphocholine and -phosphoethanolamine as well as phosphatidylinositol.
“The substrates of these phospholipases B have been shown to be the diacylglycerol-phosphocholine and -phosphoethanolamine as well as phosphatidylinositol [72].”
From Genome-wide transcriptional changes induced by phagocytosis or growth on bacteria in Dictyostelium (2008) · cites this paper as [72]
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Metadata
- Authors
- MORGAN, C. P., INSALL, R., HAYNES, L., & COCKCROFT, S.
- Affiliations
- University of London (GB)
- University of Birmingham (GB)
- Corresponding author
- COCKCROFT, Shamshad
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 2004-08-24
- Volume
- 382
- Issue
- 2
- Pages
- 441-449
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- PMC
- PMC1133800
- OpenAlex
- W1980154361
- Cited by
- 35
- References
- 40
- Citations by year
- 2024: 1 · 2023: 4 · 2021: 1 · 2020: 6 · 2018: 2 · 2016: 1 · 2015: 1 · 2014: 2 · 2013: 2 · 2012: 1
- FWCI
- 0.73
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Biochemical Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- UCL Discovery (University College London) (submittedVersion)
- University of Birmingham Research Portal (University of Birmingham) (submittedVersion)
- Funders
- Wellcome Trust
- University College London
- Medical Research Council
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Lipid metabolism and biosynthesis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Sphingolipid Metabolism and Signaling
- Keywords
- phospholipase B, Dictyostelium discoideum, lysophospholipase, protein purification, substrate specificity, phosphatidylinositol, phosphatidylethanolamine, eukaryotic evolution, gene expression in Escherichia coli
- MeSH terms
- Amino Acid Sequence, Animals, Cloning, Molecular, Dictyostelium, Humans, Lysophospholipase, Mammals, Molecular Sequence Data, Nematoda, Saccharomyces cerevisiae, Substrate Specificity, Protozoan Proteins, DNA, Protozoan, Sequence Alignment, Sequence Homology, Amino Acid, DNA, Complementary, Mice
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