Attractive but Toxic: Emerging Roles of Glycosidically Bound Volatiles and Glycosyltransferases Involved in Their Formation.

Plants emit an overabundance of volatile compounds, which act in their producers either as appreciated attractants to lure beneficial animals or as repellent toxins to deter pests in a species-specific and concentration-dependent manner. Plants have evolved solutions to provide sufficient volatiles without poisoning themselves. Uridine-diphosphate sugar-dependent glycosyltransferases (UGTs) acting on volatiles is one important part of this sophisticated system, which balances the levels of bioactive metabolites and prepares them for cellular and long-distance transport and storage but enables the remobilization of disarmed toxins for the benefit of plant protection. This review provides an overview of the research history of glycosidically bound volatiles (GBVs), a relatively new group of plant secondary metabolites, and discusses the role of UGTs in the production of GBVs for plant protection.

Structural and Functional Analysis of UGT92G6 Suggests an Evolutionary Link Between Mono- and Disaccharide Glycoside-Forming Transferases.

Glycosylation mediated by UDP-dependent glycosyltransferase (UGT) is one of the most common reactions for the biosynthesis of small molecule glycosides. As glycosides have various biological roles, we characterized UGT genes from grapevine (Vitis vinifera). In silico analysis of VvUGT genes that were highly expressed in leaves identified UGT92G6 which showed sequence similarity to both monosaccharide and disaccharide glucoside-forming transferases. The recombinant UGT92G6 glucosylated phenolics, among them caffeic acid, carvacrol, eugenol and raspberry ketone, and also accepted geranyl glucoside and citronellyl glucoside. Thus, UGT92G6 formed mono- and diglucosides in vitro from distinct compounds. The enzyme specificity constant Vmax/Km ratios indicated that UGT92G6 exhibited the highest specificity towards caffeic acid, producing almost equal amounts of the 3- and 4-O-glucoside. Transient overexpression of UGT92G6 in Nicotiana benthamiana leaves confirmed the production of caffeoyl glucoside; however, the level of geranyl diglucoside was not elevated upon overexpression of UGT92G6, even after co-expression of genes encoding geraniol synthase and geraniol UGT to provide sufficient precursor. Comparative sequence and 3-D structure analysis identified a sequence motif characteristic for monoglucoside-forming UGTs in UGT92G6, suggesting an evolutionary link between mono- and disaccharide glycoside UGTs. Thus, UGT92G6 functions as a mono- and diglucosyltransferase in vitro, but acts as a caffeoyl glucoside UGT in N. benthamiana.