AtFUT4 and AtFUT6 Are Arabinofuranose-Specific Fucosyltransferases
- Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States); USDOE Joint Genome Institute (JGI), Berkeley, CA (United States); Univ. of Georgia, Athens, GA (United States). The Complex Carbohydrate Research Center; Univ. of Georgia, Athens, GA (United States). Dept. of Plant Biology
- Univ. of Georgia, Athens, GA (United States). The Complex Carbohydrate Research Center; Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). Center for Bioenergy Innovation; Univ. of Georgia, Athens, GA (United States). Dept. of Biochemistry and Molecular Biology
- Univ. of Georgia, Athens, GA (United States). The Complex Carbohydrate Research Center; Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). Center for Bioenergy Innovation
- Univ. of Georgia, Athens, GA (United States). The Complex Carbohydrate Research Center; Univ. of Georgia, Athens, GA (United States). Dept. of Biochemistry and Molecular Biology
- Max-Planck-Inst. of Colloids and Interfaces, Potsdam (Germany). Dept. of Biomolecular Systems
- Univ. of Georgia, Athens, GA (United States). The Complex Carbohydrate Research Center
- Max-Planck-Inst. of Colloids and Interfaces, Potsdam (Germany). Dept. of Biomolecular Systems; Univ. of Natural Resources and Life Sciences, Vienna (Austria). Dept. of Chemistry
- Univ. of Georgia, Athens, GA (United States). The Complex Carbohydrate Research Center; Univ. of Georgia, Athens, GA (United States). Dept. of Plant Biology; Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). Center for Bioenergy Innovation
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), AtFUT4, and AtFUT6, are members of the plant-specific GT family 37 (GT37). AtFUT4 and AtFUT6 transfer fucose (Fuc) onto arabinose (Ara) residues of arabinogalactan (AG) proteins (AGPs) and have been postulated to be non-redundant AGP-specific FUTs. AtFUT4 and AtFUT6 were recombinantly expressed in mammalian HEK293 cells and purified for biochemical analysis. We report an updated understanding on the specificities of AtFUT4 and AtFUT6 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.
- Research Organization:
- Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States); Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States); Univ. of Georgia, Athens, GA (United States). Complex Carbohydrate Research Center
- Sponsoring Organization:
- USDOE Office of Science (SC), Basic Energy Sciences (BES). Chemical Sciences, Geosciences & Biosciences Division; German Research Foundation (DFG); National Institutes of Health (NIH); National Science Foundation (NSF); USDOE Office of Science (SC), Biological and Environmental Research (BER)
- Grant/Contract Number:
- AC05-00OR22725; PF850-1/1; SC0015662; IOS-0923992; P01GM107012; P41GM103390; R01GM130915; AC02-05CH11231
- OSTI ID:
- 1787964
- Alternate ID(s):
- OSTI ID: 1798752; OSTI ID: 1963816
- Journal Information:
- Frontiers in Plant Science, Vol. 12; ISSN 1664-462X
- Publisher:
- Frontiers Research FoundationCopyright Statement
- Country of Publication:
- United States
- Language:
- English
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