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The bulk of plant biomass is comprised of plant cell walls, which are complex polymeric networks, composed of diverse polysaccharides, proteins, polyphenolics, and hydroxyproline-rich glycoproteins (HRGPs). Glycosyltransferases (GTs) work together to synthesize the saccharide components of the plant cell wall. The  Arabidopsis thaliana  fucosyltransferases (FUTs),  At FUT4, and  At FUT6, are members of the plant-specific GT family 37 (GT37).  At FUT4 and  At FUT6 transfer fucose (Fuc) onto arabinose (Ara) residues of arabinogalactan (AG) proteins (AGPs) and have been postulated to be non-redundant AGP-specific FUTs.  At FUT4 and  At FUT6 were recombinantly expressed in mammalian HEK293 cells and purified for biochemical analysis. We report an updated understanding on the specificities of  At FUT4 and  At FUT6 that are involved in the synthesis of wall localized AGPs. Our findings suggest that they are selective enzymes that can utilize various arabinogalactan (AG)-like and non-AG-like oligosaccharide acceptors, and only require a free, terminal arabinofuranose. We also report with GUS promoter-reporter gene studies that  AtFUT4  and  AtFUT6  gene expression is sub-localized in different parts of developing  A. thaliana  roots.

AtFUT4 and AtFUT6 Are Arabinofuranose-Specific Fucosyltransferases