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Functional Characterization of Soybean Diacylglycerol Acyltransferase 3 in Yeast and Soybean

文献类型： 外文期刊

作者： Xue, Jinai 1 ; Gao, Huiling 1 ; Xue, Yinghong 1 ; Shi, Ruixiang 2 ; Liu, Mengmeng 1 ; Han, Lijun 1 ; Gao, Yu 1 ; Zhou, Yali 1 ; Zhang, Fei 1 ; Zhang, Haiping 3 ; Jia, Xiaoyun 1 ; Li, Runzhi 1 ;

作者机构： 1.Shanxi Agr Univ, Inst Mol Agr & Bioenergy, Coll Agr, Taigu, Peoples R China

2.Northeast Forestry Univ, Coll Landscape Architecture, Haerbin, Peoples R China

3.Shanxi Agr Univ, Inst Crop Germplasm Resources, Shanxi Acad Agr Sci, Ctr Agr Genet Resources Res, Taiyuan, Peoples R China

关键词： soybean (Glycine max (L; ) Merr; ); diacylglycerol acyltransferase 3 (DGAT3); yeast functional complementation assay; genetic transformation of tobacco (Nicotiana benthamiana); fatty acid and TAG biosynthesis

期刊名称：FRONTIERS IN PLANT SCIENCE （ 影响因子：6.627； 五年影响因子：7.255 ）

ISSN： 1664-462X

年卷期： 2022 年 13 卷

页码：

收录情况： SCI

摘要： Diacylglycerol acyltransferases (DGAT) function as the key rate-limiting enzymes in de novo biosynthesis of triacylglycerol (TAG) by transferring an acyl group from acyl-CoA to sn-3 of diacylglycerol (DAG) to form TAG. Here, two members of the type 3 DGAT gene family, GmDGAT3-1 and GmDGAT3-2, were identified from the soybean (Glycine max) genome. Both of them were predicted to encode soluble cytosolic proteins containing the typical thioredoxin-like ferredoxin domain. Quantitative PCR analysis revealed that GmDGAT3-2 expression was much higher than GmDGAT3-1's in various soybean tissues such as leaves, flowers, and seeds. Functional complementation assay using TAG-deficient yeast (Saccharomyces cerevisiae) mutant H1246 demonstrated that GmDGAT3-2 fully restored TAG biosynthesis in the yeast and preferentially incorporated monounsaturated fatty acids (MUFAs), especially oleic acid (C18:1) into TAGs. This substrate specificity was further verified by fatty-acid feeding assays and in vitro enzyme activity characterization. Notably, transgenic tobacco (Nicotiana benthamiana) data showed that heterogeneous expression of GmDGAT3-2 resulted in a significant increase in seed oil and C18:1 levels but little change in contents of protein and starch compared to the EV-transformed tobacco plants. Taken together, GmDGAT3-2 displayed a strong enzymatic activity to catalyze TAG assembly with high substrate specificity for MUFAs, particularly C18:1, playing an important role in the cytosolic pathway of TAG synthesis in soybean. The present findings provide a scientific reference for improving oil yield and FA composition in soybean through gene modification, further expanding our knowledge of TAG biosynthesis and its regulatory mechanism in oilseeds.

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