Research article summary (published 30 Aug 2004):

Expression in yeast of a novel phospholipase A1 cDNA from Arabidopsis thaliana.

Full Abstract

During a search for cDNAs encoding plant sterol acyltransferases, we isolated four full-length cDNAs from Arabidopsis thaliana that encode proteins with substantial identity with animal lecithin : cholesterol acyltransferases (LCATs). The expression of one of these cDNAs, AtLCAT3 (At3g03310), in various yeast strains resulted in the doubling of the triacylglycerol content. Furthermore, a complete lipid analysis of the transformed wild-type yeast showed that its phospholipid content was lower than that of the control (void plasmid-transformed) yeast whereas lysophospholipids and free fatty acids increased. When microsomes from the AtLCAT3-transformed yeast were incubated with di-[1-14C]oleyl phosphatidylcholine, both the lysophospholipid and free fatty acid fractions were highly and similarly labelled, whereas the same incubation with microsomes from the control yeast produced a negligible labelling of these fractions. Moreover when microsomes from AtLCAT3-transformed yeast were incubated with either sn-1- or sn-2-[1-14C]acyl phosphatidylcholine, the distribution of the labelling between the free fatty acid and the lysophosphatidylcholine fractions strongly suggested a phospholipase A1 activity for AtLCAT3. The sn-1 specificity of this phospholipase was confirmed by gas chromatography analysis of the hydrolysis of 1-myristoyl, 2-oleyl phosphatidylcholine. Phosphatidylethanolamine and phosphatidic acid were shown to be also hydrolysed by AtLCAT3, although less efficiently than phosphatidylcholine. Lysophospatidylcholine was a weak substrate whereas tripalmitoylglycerol and cholesteryl oleate were not hydrolysed at all. This novel A. thaliana phospholipase A1 shows optimal activity at pH 6-6.5 and 60-65 degrees C and appears to be unaffected by Ca2+. Its sequence is unrelated to all other known phospholipases. Further studies are in progress to elucidate its physiological role. Copyright 2004 FEBS

Author information

Author/s: Noiriel, Alexandre (A); Benveniste, Pierre (P); Banas, Antoni (A); Stymne, Sten (S); Bouvier-Navé, Pierrette (P);

Affiliation: Institut de Biologie Moléculaire des Plantes du CNRS, Département Isoprénoïdes, Institut de Botanique, Strasbourg, France.

Journal and publication information

Publication Type: Journal Article; Research Support, Non-U.S. Gov't

Journal: European journal of biochemistry / FEBS (Eur J Biochem), published in Germany. (Language: eng)

Reference: 2004-Sep; vol 271 (issue 18) : pp 3752-64

Dates: Created 2004/09/09; Completed 2004/10/18; Revised 2007/11/15;

PMID: 15355352, status: MEDLINE (last retrieval date: 2/18/2009, IMS Date: )

Sourced from the National Library of Medicine. Abstract text and other information may be subject to copyright.

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MeSH headings (categories)

This article was linked to the MESH Headings shown below.

Acyltransferases - analysis; genetics; metabolism Alleles Amino Acid Sequence Arabidopsis - enzymology Conserved Sequence DNA, Complementary - genetics Escherichia coli - genetics Expressed Sequence Tags Gene Expression Regulation, Enzymologic Lipids - analysis

Microsomes - enzymology Molecular Sequence Data Mutagenesis, Site-Directed Phospholipases A - metabolism Phospholipases A1 Phylogeny Saccharomyces cerevisiae - cytology; genetics; metabolism Sequence Homology, Amino Acid Subcellular Fractions - enzymology Substrate Specificity

Associated Chemicals: DNA, Complementary (0) ; Lipids (0) ; Acyltransferases (EC 2.3.-) ; Phospholipases A (EC 3.1.1.-) ; Phospholipases A1 (EC 3.1.1.32)

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