Reference Report for AP20210727.1
| Title: | Identification and functional characterization of a soybean (Glycine max) thioesterase that acts on inteermediates of fatty acid biosynthesis |
| Authors: | Tran, H. T. D., Le, N. T., Khuat, V. L. U., Nguyen, T. T. H. |
| Source: | Tran et al. 2019 Plants, 8(10):397 |
| Abstract: | Background: Plants possess many acyl-acyl carrier protein (acyl-ACP) thioesterases (TEs) with unique specificity. One such TE is methylketone synthase 2 (MKS2), an enzyme with a single-hotdog-fold structure found in several tomato species that hydrolyzes 3-ketoacyl-ACPs to give free 3-ketoacids. (2) Methods: In this study, we identified and characterized a tomato MKS2 homolog gene, namely,GmMKS2, in the genome of soybean (Glycine max). (3) Results:GmMKS2underwent alternative splicing to produce three alternative transcripts, but only one encodes a protein with thioesterase activity when recombinantly expressed inEscherichia coli. Heterologous expression of the main transcript ofGmMKS2,GmMKS2-X2, inE. coligenerated various types of fatty acids, including 3-ketoacidswith 3-ketotetradecenoic acid (14:1) being the most abundantcis-5-dodecanoic acid, and 3-hydroxyacids, suggesting that GmMKS2 acts as an acyl-ACP thioesterase. In plants, theGmMKS2-X2transcript level was found to be higher in the roots compared to other examined organs.In silicoanalysis revealed that there is a substantial enrichment of putativecis-regulatory elements related to disease-resistance responses and abiotic stress responses in the promoter of this gene. (4) Conclusions: GmMKS2 showed broad substrate specificities toward a wide range of acyl-ACPs that varied in terms of chain length, oxidation state, and saturation degree. Our results suggest that GmMKS2 might have a stress-related physiological function inG. max. |
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