Genome-wide identification of glycosyltransferases converting phloretin to phloridzin in Malus species

•A large-scale investigation of dihydrochalcones accumulations in leaves from 64 Malus species and cultivars.•Analyses of qRT-PCR and enzyme activity suggest that both MdUGT88F1 and MdUGT88F4 are the responsible P2′GTs in Malus.•Obtaining transgenic plants exhibiting reduced phloridzin and increased phloretin (and trilobatin) by gene silencing.

Phloridzin (phloretin 2′-O-glucoside) is the most abundant phenolic compound in Malus species, accounting for up to 18% of the dry weight in leaves. Glycosylation of phloretin at the 2′ position is the last and key step in phloridzin biosynthesis. It is catalyzed by a uridine diphosphate (UDP)-glucose:phloretin 2′-O-glucosyltransferase (P2′GT), which directly determines the concentration of phloridzin. However, this process is poorly understood. We conducted a large-scale investigation of phloridzin accumulations in leaves from 64 Malus species and cultivars. To identify the responsible P2′GT, we performed a genome-wide analysis of the expression patterns of UDP-dependent glycosyltransferase genes (UGTs). Two candidates were screened preliminarily in Malus spp. cv. Adams (North American Begonia). Results from further qRT-PCR analyses of the genotypes showed a divergence in phloridzin production. Our assays of enzyme activity also suggested that MdUGT88F4 and MdUGT88F1 regulate the conversion of phloretin to phloridzin in Malus plants. Finally, when they were silenced in 'GL-3' ('Royal Gala'), the concentrations of phloridzin and phloretin (and trilobatin) were significantly reduced and increased, respectively.