Analysis of triglyceride synthesis unveils a green algal soluble diacylglycerol acyltransferase and provides clues to potential enzymatic components of the chloroplast pathway

• DOI: 10.1186/s12864-017-3602-0
• Publication Date: 2017-03-09T01:56:30Z
• Authors: Carolina Bagnato; María B. Prados; Gisela R. Franchini; Natalia Scaglia; Silvia E. Miranda; María V. Beligni
• Keywords: 0301 basic medicine; Chloroplasts; Amino Acid Motifs; Diacylglycerol kinase; Triacylglycerol Synthesis; Biochemistry; Gene; Computational biology; HMMER PROFILING; Chlorophyta; https://purl.org/becyt/ford/1.6; PROTEIN PHYLOGENY; Triglyceride metabolism; Conserved Sequence; Phylogeny; Microalgae as a Source for Biofuels Production; Energy; Genome; CHLOROPLAST; SOLUBLE ACYLTRANSFERASE; Life Sciences; Biodiesel production; Protein phylogeny; Physical Sciences; Ferredoxins; Fatty Acid Biosynthesis; NEUTRAL LIPIDS; Metabolic Networks and Pathways; Neutral lipids; Biotechnology; Research Article; Algae; Plastid; Soluble acyltransferase; Chloroplast; Molecular Mechanisms of Photosynthesis and Photoprotection; Evolution, Molecular; 03 medical and health sciences; ALGAE; Protein kinase C; Biochemistry, Genetics and Molecular Biology; Genetics; Position-Specific Scoring Matrices; Computer Simulation; HMMER profiling; Amino Acid Sequence; Diacylglycerol O-Acyltransferase; https://purl.org/becyt/ford/1; Molecular Biology; Biology; BIODIESEL PRODUCTION; Ciencias Exactas; Triglycerides; Lipid Metabolism and Storage in Organisms; TRIGLYCERIDE METABOLISM; Renewable Energy, Sustainability and the Environment; Computational Biology; Enzyme; Ciencias Médicas; Diacylglycerol Acyltransferase

Microalgal triglyceride (TAG) synthesis has attracted considerable attention. Particular emphasis been put towards characterizing the algal homologs of canonical rate-limiting enzymes, diacylglycerol acyltransferase (DGAT) and phospholipid:diacylglycerol (PDAT). Less work done to analyze from a phylogenetic perspective. In this work, we used HMMER iterative profiling functional analyses determine number sequence characteristics DGAT PDAT, as well related sequences that constitute their corresponding superfamilies. We included most algae with available genomes, representative eukaryotic prokaryotic species.Amongst our main findings, identified novel clade DGAT1-like proteins exclusive red glaucophyta previously uncharacterized subclade DGAT2 an unusual transmembrane segments. Our analysis also revealed existence green moderate similarity plant soluble DGAT3. The DGAT3 shares recent ancestor group cyanobacteria. Subcellular targeting prediction suggests are imported chloroplast, evidencing chloroplast might have pathway for de novo TAGs. Heterologous expression C. reinhardtii produces increase in accumulation TAG, evidenced by thin layer chromatography.Our contributes advance knowledge complex superfamilies involved lipid metabolism provides clues possible enzymatic players TAG synthesis.