Diversity and evolution of plant diacylglycerol acyltransferase (DGATs) unveiled by phylogenetic, gene structure and expression analyses

Abstract

Since the first diacylglycerol acyltransferase (DGAT) gene was characterized in plants, a number of studies have focused on understanding the role of DGAT activity in plant triacylglycerol (TAG) biosynthesis. DGAT enzyme is essential in controlling TAGs synthesis and is encoded by different genes. DGAT1 and DGAT2 are the two major types of DGATs and have been well characterized in many plants. On the other hand, the DGAT3 and WS/DGAT have received less attention. In this study, we present the first general view of the presence of putative DGAT3 and WS/DGAT in several plant species and report on the diversity and evolution of these genes and its relationships with the two main DGAT genes (DGAT1 and DGAT2). According to our analyses DGAT1, DGAT2, DGAT3 and WS/DGAT are very divergent genes and may have distinct origin in plants. They also present divergent expression patterns in different organs and tissues. The maintenance of several types of genes encoding DGAT enzymes in plants demonstrates the importance of DGAT activity for TAG biosynthesis. Evolutionary history studies of DGATs coupled with their expression patterns help us to decipher their functional role in plants, helping to drive future biotechnological studies.

Genome-wide identification of Diacylglycerol Acyltransferases (DGAT) family genes influencing Milk production in Buffalo

“…Refer to the relevant studies, Frequency (%), the frequency of individuals with each haplotype among population; Haplotype combination (n), the number of individuals with each haplotype combination among population; LSM ± SE represent the least square means ± standard error; PM270, 270-day peak milk yield; MY270, 270-day total milk yield; FY270, 270-day fat yield; FP270, 270-day fat percentage; PY270, 270-day protein yield and PP270, 270-day protein percentage. For each haplotype block each trait, values with different superscripts differ significantly at Bonferroni corrected P < 0.05 and we discovered that DGAT3 and WAX-DGAT are two types of DGAT enzymes that phylogenetically divergent from DGAT1 and DGAT2 [13,23]. These two genes mostly identified in plants and yeast, but rarely found in animals [16,28].…”

“…DGAT1 and DGAT2 are essential genes related to milk traits in cattle and buffalo. The DGAT family genes encoding functional proteins have been well characterized in many plants recently [13,23]. However, investigation of DGAT gene family in animals, especially in buffalo was limited.…”

“…The diacylglycerol acyltransferases (DGAT) enzymes are essential ones that control the final rate-limiting step of triacylglycerol biosynthesis for the significant milk lipid. Presently, four distinct DGAT functional subfamilies, including DGAT1, DGAT2, DGAT3, and WAX-DGAT, have been discovered in different organisms [13][14][15]. Among them, only DGAT1 and DGAT2 enzymes have been detected in animals, which was shown to play non-redundant roles in triacylglycerides synthesis [16].…”

Genome-wide identification of diacylglycerol acyltransferases (DGAT) family genes influencing milk production traits in buffalo

“…Besides the two main clades, DGAT3 and WAX-DGAT, formed a monophyletic subgroup, which has not detected in buffalo and cattle. Refer to the relevant studies, and we discovered that DGAT3 and WAX-DGAT are two types of DGAT enzymes that phylogenetically divergent from DGAT1 and DGAT2 [13,23]. These two genes mostly identified in plants and yeast, but rarely found in animals [16,28].…”

“…The diacylglycerol acyltransferases (DGAT) enzymes are essential ones that control the final ratelimiting step of triacylglycerol biosynthesis for the significant milk lipid. Presently, four distinct DGAT functional subfamilies, including DGAT1, DGAT2, DGAT3, and WAX-DGAT, have been discovered in different organisms [13][14][15]. Among them, only DGAT1 and DGAT2 enzymes have been detected in animals, which was shown to play non-redundant roles in triacylglycerides synthesis [16].…”