Molecular cloning and functional characterization of GmAAPTs from soybean (Glycine max).

Aminoalcoholphosphotransferase (AAPT) utilizes diacylglycerols and cytidine diphosphate-choline/ethanolamine as substrates for the synthesis of phosphatidylcholine (PC)/phosphatidylethanolamine (PE). Plant AAPTs involved in phospholipid metabolism mediate diverse physiological processes; however, little is known about their functions in triacylglycerol (TAG) metabolism and seed germination. In the present study, we isolated and characterized two AAPTs, GmAAPT1 and GmAAPT2, from soybean (Glycine max). GmAAPT1 and GmAAPT2 exhibited strong similarity in their amino acid contents and expression patterns, and both were found to localize to the endoplasmic reticulum and Golgi apparatus. In vitro enzymatic analyses showed that GmAAPT1 and GmAAPT2 contributed to PC and PE synthesis and exhibited choline/ethanolamine phosphotransferase-like enzymatic properties. The overexpression of GmAAPT1 and GmAAPT2 in Arabidopsis led to reduced levels of seed TAG and polyunsaturated fatty acids and decreased seed germination under freezing stress. Together, these findings suggest that GmAAPTs mediate TAG metabolism and negatively regulate seed freezing tolerance.