Chromosome-Level Genome Assembly and Multi-Omics Dataset Provide Insights into Isoflavone and Puerarin Biosynthesis in Pueraria lobata (Wild.) Ohwi

Abstract

Pueraria lobata (wild.) Ohwi is a leguminous plant and one of the traditional Chinese herbal medicines. Its puerarin extract is widely used in the pharmaceutical industry. This study reported a chromosome-level genome assembly for P. lobata and its characteristics. The genome size was ~939.2 Mb, with a contig N50 of 29.51 Mbp. Approximately 97.82% of the assembled sequences were represented by 11 pseudochromosomes. We identified that the repetitive sequences accounted for 63.50% of the P. lobata genome. A total of 33,171 coding genes were predicted, of which 97.34% could predict the function. Compared with other species, P. lobata had 757 species-specific gene families, including 1874 genes. The genome evolution analysis revealed that P. lobata was most closely related to Glycine max and underwent two whole-genome duplication (WGD) events. One was in a gamma event shared by the core dicotyledons at around 65 million years ago, and another was in the common ancestor shared by legume species at around 25 million years ago. The collinearity analysis showed that 61.45% of the genes (54,579 gene pairs) in G. max and P. lobata had collinearity. In this study, six unique PlUGT43 homologous genes were retrieved from the genome of P. lobata, and no 2-hydroxyisoflavanone 8-C-glucoside was found in the metabolites. This also revealed that the puerarin synthesis was mainly from the glycation of daidzein. The combined transcriptome and metabolome analysis suggested that two bHLHs, six MYBs and four WRKYs were involved in the expression regulation of puerarin synthesis structural genes. The genetic information obtained in this study provided novel insights into the biological evolution of P. lobata and leguminous species, and it laid the foundation for further exploring the regulatory mechanism of puerarin synthesis.

Puerarin—A Promising Flavonoid: Biosynthesis, Extraction Methods, Analytical Techniques, and Biological Effects

“…Providing the compound 4-coumaroyl-CoA will be achieved by using 4-coumarate-CoAligase (C4CoAL) [17,31,32]. Afterwards, 4-coumaroyl-CoA is converted to isoliquiritigenin by chalcone synthase and chalcone reductase [33][34][35][36][37][38]. Chalcone isomerase (CHI) then catalyzes the formation of liquiritigenin from isoliquiritigenin, which is further catalyzed by 2-hydroxyisoflavanone (IFS) to produce 2,7,4 ′ -trihydroxyisoflavonone [36,37,39].…”

“…Two different pathways allow for the production of puerarin through the catalysis of the chalcone isoflavone, by (i) 2-hydroxyisoflavanone dehydratase (HID) to form daidzein, and by (ii) 8-C-glucosyltransferase (8-C-GT) to form trihydroxyisoflavonone-8-C-glucoside (Figure 3) [35,36]. The transformation of it into puerarin is accomplished by PlUGT43 through 8-C-glucosylation.…”