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Plastidic Δ6 fatty-acid desaturases with distinctive substrate specificity regulate the pool of c18-pufas in the ancestral picoalga ostreococcus tauri

biorxiv. 2020; 
Charlotte Degraeve-Guilbault C.,  Rodrigo E. Gomez,  Cécile. Lemoigne,  Nattiwong Pankansem,  Soizic Morin,  Karine Tuphile, Jérôme Joubès,  Juliette Jouhet, Julien Gronnier,  Iwane Suzuki,  Frédéric Domergue,  Florence Corellou
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Molecular Biology Reagents For subcellular localization, the final destination vector was pK7YWG2 (Karimi et al., 2002) N-terminal-YFP-fusion was used. Subcloning was achieved in pGEMT vector by restriction 447 enzymes (Promega, Madison, WI, US), in pUC57 for codon-optimized sequence used in 448 Synechocystis and for S. cerevisiae (GenScript Biotech, Netherlands) and/or in pDONR 221 449 for GATEWAY cloning. Get A Quote

摘要

Eukaryotic Δ6-desaturases are microsomal enzymes which balance the synthesis of ω-3 and ω-6 C18-polyunsaturated-fatty-acids (PUFA) accordingly to their specificity. In several microalgae, including O. tauri, plastidic C18-PUFA are specifically regulated by environmental cues suggesting an autonomous control of Δ6-desaturation of plastidic PUFA. Sequence retrieval from O. tauridesaturases, highlighted two putative Δ6/Δ8-desaturases sequences clustering, with other microalgal homologs, apart from other characterized Δ-6 desaturases. Their overexpression in heterologous hosts, including N. benthamiana and Synechocystis, unveiled their Δ6-desaturation activity and plastid localization. O. tauri lines... More

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