Platycodon grandiflorus is a medicinal
plant whose main component is platycodins, which have a variety of
pharmacological effects and nutritional values. The farnesyl pyrophosphate
synthase (FPS) is a key enzyme in the isoprenoid biosynthesis pathway,
which catalyzes the synthesis of farnesyl diphosphate (FPP). In this
study, we cloned the FPS gene from P. grandiflorus (PgFPS) with an
ORF of 1260 bp, encoding 419 amino acids with a deduced molecular
weight and theoretical pI of 46,200.98 Da and 6.52, respectively.
The squalene content of overexpressed PgFPS in tobacco
leaves and yeast cells extract was 1.88-fold and 1.21-fold higher
than that of the control group, respectively, and the total saponin
content was also increased by 1.15 times in yeast cells extract, which
verified the biological function of PgFPS in terpenoid
synthesis. After 48 h of MeJA treatment and 6 h of ethephon treatment,
the expression of the PgFPS gene in roots and stems
reached its peak, showing a 3.125-fold and 3.236-fold increase compared
to the untreated group, respectively. Interestingly, the expression
of the PgFPS gene in leaves showed a decreasing trend
after exogenous elicitors treatment. The discovery of this enzyme
will provide a novel perspective for enhancing the efficient synthesis
of platycodins.