Abstract
Legume plants are rich in prenylated flavonoid compounds, which play an important role in plant defense and human health. In the present study, we identified a prenyltransferase (PT) gene, named LaPT2, in white lupin (Lupinus albus), which shows a high identity and close relationship with the other known PT genes involved in flavonoid prenylation in planta. The recombinant LaPT2 protein expressed in yeast cells exhibited a relatively strong activity toward several flavonols (e.g., kaempferol, quercetin, and myricetin) and a relatively weak activity toward flavanone (naringenin). In addition, the recombinant LaPT2 protein was also active toward several other types of flavonoids, including galangin, morin, 5-deoxyquercetin, 4'-O-methylkaempferol, taxifolin, and aromadendrin, with distinct enzymatic affinities. The LaPT2 gene was preferentially expressed in the roots, which is consistent with the presence of prenylated flavonoid kaempferol in the roots. Moreover, we found that the expression level of LaPT2 paralleled with those of LaF3H1 and LaFLS2 genes that were relatively higher in roots and lower in leaves, suggesting that they were essential for the accumulation of prenylated flavonoid kaempferol in roots. The deduced full-length LaPT2 protein and its signal peptide fused with a green fluorescent protein (GFP) are targeted to plastids in the Arabidopsis thaliana protoplast. Our study demonstrated that LaPT2 from white lupin is responsible for the biosynthesis of prenylated flavonoids, in particular flavonols, which could be utilized as phytoalexin for plant defense and bioactive flavonoid compounds for human health.