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Diacylglycerol acyltransferase: A key mediator of plant triacylglycerol synthesis

  • Invited Thematic Review
  • Published:
Lipids

Abstract

Many plants deposit TAG in seeds and fruits as the major form of storage lipid. TAG production is of tremendous socioeconomic value in food, nutraceutical, and industrial applications, and thus numerous conventional and molecular genetic strategies have been explored in attempts to increase TAG content and modify the FA composition of plant seed oils. Much research has focused on the acyl-CoA-dependent reaction catalyzed by diacylglycerol acyltransferase (DGAT), which is an integral endoplasmic reticulum protein and has also been shown to be present in oil bodies and plastids. DGAT enzymes exhibit diverse biochemical properties among different plant species, many of which are summarized here. In addition to catalyzing a critical step in TAG biosynthesis, there is evidence that DGAT has roles in lipid metabolism associated with germination and leaf senescence. TAG can also be formed in plants via two different acyl-CoA-independent pathways, catalyzed by phospholipid: diacylglycerol acyltransferase and diacylglycerol transacylase. The current understanding of the terminal step in TAG formation in plants and the development of molecular genetic approaches aimed at altering TAG yield and FA composition of TAG are discussed.

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Abbreviations

ACP:

acyl carrier protein

ASP:

acylation stimulating protein

ATP:

adenosine triphosphate

CDP:

cytidine diphosphate

CPT:

cytidine diphosphate-choline: 1,2-diacylglycerol cholinephosphotransferase

DGAT:

DAG acyltransferase

DGTA:

DAG transacylase

ER:

endoplasmic reticulum

EST:

expressed sequence tag

FAD:

FA desaturation

GUS:

β-glucuronidase

MD:

microspore-derived

MEGA-8:

octanoyl-N-methylglucamide

PDAT:

phospholipid:diacylglycerol acyltransferase

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Correspondence to Randall J. Weselake.

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Lung, SC., Weselake, R.J. Diacylglycerol acyltransferase: A key mediator of plant triacylglycerol synthesis. Lipids 41, 1073–1088 (2006). https://doi.org/10.1007/s11745-006-5057-y

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