Journal Article

At FUT4 and At FUT6 Are Arabinofuranose-Specific Fucosyltransferases

Black, Ian M, Pfrengle, Fabian, Chapla, Digantkumar, Moremen, Kelley W, Urbanowicz, Breeanna R, Peña, Maria J, Backe, Jason, Soto, Maria J, Wang, Hsin-Tzu, Prabhakar, Pradeep Kumar, Hahn, Michael G, Bartetzko, Max, Azadi, Parastoo

2021

Overview

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 fucosyltransferases (FUTs), FUT4, and FUT6, are members of the plant-specific GT family 37 (GT37). FUT4 and FUT6 transfer fucose (Fuc) onto arabinose (Ara) residues of arabinogalactan (AG) proteins (AGPs) and have been postulated to be non-redundant AGP-specific FUTs. FUT4 and FUT6 were recombinantly expressed in mammalian HEK293 cells and purified for biochemical analysis. We report an updated understanding on the specificities of FUT4 and 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 and gene expression is sub-localized in different parts of developing roots.