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Patatin-like lipolytic acyl hydrolases and galactolipid metabolism in marine diatoms of the genus Pseudo-nitzschia

Adelfi, Maria Grazia, Vitale, Rosa Maria, d'Ippolito, Giuliana, Nuzzo, Genoveffa, Gallo, Carmela, Amodeo, Pietro, Manzo, Emiliano, Pagano, Dario, Landi, Simone, Picariello, Gianluca, Ferrante, Maria Immacolata, Fontana, Angelo
Biochimica et biophysica acta 2019 v.1864 no.2 pp. 181-190
microalgae, metabolism, proteins, oxylipins, eicosapentaenoic acid, aquatic food webs, linoleate 13S-lipoxygenase, models, aldehydes, microorganisms, phospholipases, genes, enzyme activity, galactolipids, aquatic ecosystems, Bacillariophyceae
Diatoms are eukaryotic microalgae that play a pivotal role in biological and geochemical marine cycles. These microorganisms are at the basis of the trophic chain and their lipids are essential components (e.g. eicosapentaenoic acid, EPA) of aquatic food webs. Galactolipids are the primary lipid components of plastid membranes and form the largest lipid family of diatoms. As source of polyunsaturated fatty acids (PUFAs), these compounds are also involved in the synthesis of lipoxygenase (LOX) products such as non-volatile oxylipins and polyunsaturated aldehydes. Here, we report the first identification of two genes, namely PmLAH1 and PaLAH1, coding for lipolytic enzymes in two diatoms of the genus Pseudo-nitzschia. Functional and modeling studies evidence a patatin-like domain endowed with galactolipase and phospholipase activity at the C-terminus of both proteins. Homologues of Pseudo-nitzschia LAH1 genes were retrieved in other diatom species so far sequenced in agreement with conservation of the functional role of these proteins within the lineage.