AtFUT4 and AtFUT6 Are Arabinofuranose-Specific Fucosyltransferases
Abstract
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.
- Authors:
-
- 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
- Publication Date:
- Research Org.:
- 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 Org.:
- 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)
- OSTI Identifier:
- 1787964
- Alternate Identifier(s):
- OSTI ID: 1798752; OSTI ID: 1963816
- Grant/Contract Number:
- AC05-00OR22725; PF850-1/1; SC0015662; IOS-0923992; P01GM107012; P41GM103390; R01GM130915; AC02-05CH11231
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Frontiers in Plant Science
- Additional Journal Information:
- Journal Volume: 12; Journal ID: ISSN 1664-462X
- Publisher:
- Frontiers Research Foundation
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; Fucosyltransferase; arabinogalactan protein; AtFUT1; AtFUT4; AtFUT6; GT37; plant cell wall; hydroxyproline-rich glycoprotein; fucosyltransferase, arabinogalactan protein, AtFUT1, AtFUT4, AtFUT6, GT37, plant cell wall, hydroxyproline-rich glycoprotein
Citation Formats
Soto, Maria J., Prabhakar, Pradeep Kumar, Wang, Hsin-Tzu, Backe, Jason, Chapla, Digantkumar, Bartetzko, Max, Black, Ian M., Azadi, Parastoo, Peña, Maria J., Pfrengle, Fabian, Moremen, Kelley W., Urbanowicz, Breeanna R., and Hahn, Michael G. AtFUT4 and AtFUT6 Are Arabinofuranose-Specific Fucosyltransferases. United States: N. p., 2021.
Web. doi:10.3389/fpls.2021.589518.
Soto, Maria J., Prabhakar, Pradeep Kumar, Wang, Hsin-Tzu, Backe, Jason, Chapla, Digantkumar, Bartetzko, Max, Black, Ian M., Azadi, Parastoo, Peña, Maria J., Pfrengle, Fabian, Moremen, Kelley W., Urbanowicz, Breeanna R., & Hahn, Michael G. AtFUT4 and AtFUT6 Are Arabinofuranose-Specific Fucosyltransferases. United States. https://doi.org/10.3389/fpls.2021.589518
Soto, Maria J., Prabhakar, Pradeep Kumar, Wang, Hsin-Tzu, Backe, Jason, Chapla, Digantkumar, Bartetzko, Max, Black, Ian M., Azadi, Parastoo, Peña, Maria J., Pfrengle, Fabian, Moremen, Kelley W., Urbanowicz, Breeanna R., and Hahn, Michael G. Tue .
"AtFUT4 and AtFUT6 Are Arabinofuranose-Specific Fucosyltransferases". United States. https://doi.org/10.3389/fpls.2021.589518. https://www.osti.gov/servlets/purl/1787964.
@article{osti_1787964,
title = {AtFUT4 and AtFUT6 Are Arabinofuranose-Specific Fucosyltransferases},
author = {Soto, Maria J. and Prabhakar, Pradeep Kumar and Wang, Hsin-Tzu and Backe, Jason and Chapla, Digantkumar and Bartetzko, Max and Black, Ian M. and Azadi, Parastoo and Peña, Maria J. and Pfrengle, Fabian and Moremen, Kelley W. and Urbanowicz, Breeanna R. and Hahn, Michael G.},
abstractNote = {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.},
doi = {10.3389/fpls.2021.589518},
journal = {Frontiers in Plant Science},
number = ,
volume = 12,
place = {United States},
year = {Tue Feb 09 00:00:00 EST 2021},
month = {Tue Feb 09 00:00:00 EST 2021}
}
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