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Diversity of Types of Plant Diacylglycerol Acyltransferases, Peculiarities of Their Functioning, and How Many DGATs are Required for Plants

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Abstract—

Emergence of sn-1,2-diacylglycerol-3-acyltransferases (DGATs)—the key enzymes of triacylglycerol (TAG) biosynthesis—may be regarded as an important aromorphosis in the evolution of the organic world in general and that of plants in particular. In fact, the newly originated ability to store carbon, energy, water, and “building blocks” in a form of hydrophobic compounds enabled increasing the “capacity” of storage compounds in the cells and to simultaneously reduce volumes of storage organs. DGATs are present in almost any organisms from myxomycetes, mosses, fungi, and algae to mammals, including humans. Although these enzymes are so widespread in a world of live matter, it is difficult to follow principles of their organization, evolution, and functioning because an organism may possess several DGATs belonging to different types, differently localized in the cell, and employing different substrates or competing for one substrate. They are relatives owing to only one common function—the transfer of a fatty acid residue from acyl-CoA to sn-1,2-diacyl-glycerol yielding a TAG molecule. In some cases, DGATs can acylate sterols, higher fatty alcohols, and other substrates bringing about the same product. Intense investigations of these enzymes have been continuing for the last 50 years and they present more questions than answers so far. However, clear comprehension of the traits of organization and function of DGATs opens up fantastic prospects in biotechnology and genetic engineering of functional lipids for food and pharmaceutical industries, and agriculture. This review attempts to summarize the recent data on structural and functional peculiarities of DGATs, effects of endogenous and exogenous factors on the expression levels of their genes, and the adaptive roles of these genes in the evolution of living organisms.

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Funding

The work was partially supported through State Task no. 0106-2019-0002 and the Russian Science Foundation (project no. 17-74-10127 “Peculiarities of functions of sn-1,2-diacyl-3-acyltransferases with different substrate specificity”).

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  1. Timiryazev Institute of Plant Physiology, Russian Academy of Sciences, 127276, Moscow, Russia

    O. S. Pavlenko, Y. V. Akashkina, A. V. Suhorukova, R. A. Sidorov & V. D. Tsydendambaev

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  1. O. S. Pavlenko
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  2. Y. V. Akashkina
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  3. A. V. Suhorukova
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  4. R. A. Sidorov
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  5. V. D. Tsydendambaev
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Correspondence to O. S. Pavlenko.

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Translated by A. Aver’yanov

Abbreviations: a.a.—amino acid residue; ACAT—acyl-CoA : cholesterol acyltransferase; AcDAG—3-acetyl-1,2-diacyl-sn-glycerol; DAcT—sn-1,2-diacylglycerol-3-acetyltransferase; DAG—1,2-diacyl-sn-glycerol; DGAT—diacylglycerol acyltransferase; IDR—intrinsically disordered region; MBOAT—membrane-bound O-acyltransferase; PLAG—sn-1-palmitoyl-2-linoleoyl-3-acetyl-rac-glycerol; PUFA—polyunsaturated fatty acid; sTAG—structured TAG; TAG—triacylglycerol

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Pavlenko, O.S., Akashkina, Y.V., Suhorukova, A.V. et al. Diversity of Types of Plant Diacylglycerol Acyltransferases, Peculiarities of Their Functioning, and How Many DGATs are Required for Plants. Russ J Plant Physiol 69, 2 (2022). https://doi.org/10.1134/S1021443722010162

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