ArticleBMC evolutionary biology2011
Evolutionary view of acyl-CoA diacylglycerol acyltransferase (DGAT), a key enzyme in neutral lipid biosynthesis.
Article in BMC evolutionary biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.
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76 citing papers in PubMed, 205 citations in OpenAlex.
- Opposite diacylglycerol enantiomeric specificities of Arabidopsis DGAT1 and DGAT2 reveal distinct roles in TAG synthesis.Plant physiology · 2026Article
- Genomic Signatures of Artificial Selection Underlying Oil Content Differentiation in Chinese and Uruguayan Soybean Germplasm.Plants (Basel, Switzerland) · 2026Article
- Systematic analysis of the Diacylglycerol acyltransferase (DGAT) genes in oat and functional characterazation of AsDGAT2-1 involved in oil accumulation and cold stress tolerance.BMC plant biology · 2026Article
- Comparative Expression of Diacylglycerol Acyltransferases for Enhanced Accumulation of Punicic Acid-Enriched Triacylglycerols inMolecules (Basel, Switzerland) · 2026Article
- Energy's long game: thermogenic adipocytes and the metabolic diseases of modern life.Academia biology · 2026Article
- Functional diversity of sunflower DGAT1 and DGAT2 enzymes underlying seed triacylglycerol biosynthesis.Frontiers in plant science · 2026Article
- Article
- Powdery mildew induces chloroplast storage lipid formation at the expense of host thylakoids to promote spore production.The Plant cell · 2025Article
- Development of vegetative oil sorghum: From lab-to-field.Plant biotechnology journal · 2025Article
- Article
- De novo assembly ofHeliyon · 2024Article
- The role of DGAT1 and DGAT2 in regulating tumor cell growth and their potential clinical implications.Journal of translational medicine · 2024Review
- Whole-genome and genome-wide association studies improve key agricultural traits of safflower for industrial and medicinal use.Horticulture research · 2023Article
- Interference withAnimals : an open access journal from MDPI · 2023Article
- Review
- Overexpression ofAnimals : an open access journal from MDPI · 2023Article
- Applications of Diacylglycerol Acyltransferase for Triacylglycerol Production inJournal of fungi (Basel, Switzerland) · 2023Article
- Transmembrane Protein 68 Functions as an MGAT and DGAT Enzyme for Triacylglycerol Biosynthesis.International journal of molecular sciences · 2023Article
- Cell lipid biology in infections: an overview.Frontiers in cellular and infection microbiology · 2023Review
- Genome-wide association study and RNA-seq identifies GmWRI1-like transcription factor related to the seed weight in soybean.Frontiers in plant science · 2023Article
16 more citing papers are in PubMed but not listed here.
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7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundTriacylglycerides (TAGs) are a class of neutral lipids that represent the most important storage form of energy for eukaryotic cells. DGAT (acyl-CoA: diacylglycerol acyltransferase; EC 2.3.1.20) is a transmembrane enzyme that acts in the final and committed step of TAG synthesis, and it has been proposed to be the rate-limiting enzyme in plant storage lipid accumulation. In fact, two different enzymes identified in several eukaryotic species, DGAT1 and DGAT2, are the main enzymes responsible for TAG synthesis. These enzymes do not share high DNA or protein sequence similarities, and it has been suggested that they play non-redundant roles in different tissues and in some species in TAG synthesis. Despite a number of previous studies on the DGAT1 and DGAT2 genes, which have emphasized their importance as potential obesity treatment targets to increase triacylglycerol accumulation, little is known about their evolutionary timeline in eukaryotes. The goal of this study was to examine the evolutionary relationship of the DGAT1 and DGAT2 genes across eukaryotic organisms in order to infer their origin.
resultsWe have conducted a broad survey of fully sequenced genomes, including representatives of Amoebozoa, yeasts, fungi, algae, musses, plants, vertebrate and invertebrate species, for the presence of DGAT1 and DGAT2 gene homologs. We found that the DGAT1 and DGAT2 genes are nearly ubiquitous in eukaryotes and are readily identifiable in all the major eukaryotic groups and genomes examined. Phylogenetic analyses of the DGAT1 and DGAT2 amino acid sequences revealed evolutionary partitioning of the DGAT protein family into two major DGAT1 and DGAT2 clades. Protein secondary structure and hydrophobic-transmembrane analysis also showed differences between these enzymes. The analysis also revealed that the MGAT2 and AWAT genes may have arisen from DGAT2 duplication events.
conclusionsIn this study, we identified several DGAT1 and DGAT2 homologs in eukaryote taxa. Overall, the data show that DGAT1 and DGAT2 are present in most eukaryotic organisms and belong to two different gene families. The phylogenetic and evolutionary analyses revealed that DGAT1 and DGAT2 evolved separately, with functional convergence, despite their wide molecular and structural divergence.
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