AtFUT4 and AtFUT6 Are Arabinofuranose-Specific Fucosyltransferases
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...
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2021-02-01
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| Series: | Frontiers in Plant Science |
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| Online Access: | https://www.frontiersin.org/articles/10.3389/fpls.2021.589518/full |
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| author | Maria J. Soto Maria J. Soto Maria J. Soto Pradeep Kumar Prabhakar Pradeep Kumar Prabhakar Pradeep Kumar Prabhakar Hsin-Tzu Wang Hsin-Tzu Wang Hsin-Tzu Wang Jason Backe Jason Backe Digantkumar Chapla Digantkumar Chapla Max Bartetzko Ian M. Black Parastoo Azadi Parastoo Azadi Maria J. Peña Maria J. Peña Fabian Pfrengle Fabian Pfrengle Kelley W. Moremen Kelley W. Moremen Breeanna R. Urbanowicz Breeanna R. Urbanowicz Breeanna R. Urbanowicz Michael G. Hahn Michael G. Hahn Michael G. Hahn |
| author_facet | Maria J. Soto Maria J. Soto Maria J. Soto Pradeep Kumar Prabhakar Pradeep Kumar Prabhakar Pradeep Kumar Prabhakar Hsin-Tzu Wang Hsin-Tzu Wang Hsin-Tzu Wang Jason Backe Jason Backe Digantkumar Chapla Digantkumar Chapla Max Bartetzko Ian M. Black Parastoo Azadi Parastoo Azadi Maria J. Peña Maria J. Peña Fabian Pfrengle Fabian Pfrengle Kelley W. Moremen Kelley W. Moremen Breeanna R. Urbanowicz Breeanna R. Urbanowicz Breeanna R. Urbanowicz Michael G. Hahn Michael G. Hahn Michael G. Hahn |
| author_sort | Maria J. Soto |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-12-14T06:54:02Z |
| format | Article |
| id | doaj.art-d83692272c844322880fd51a97a0f8f3 |
| institution | Directory Open Access Journal |
| issn | 1664-462X |
| language | English |
| last_indexed | 2024-12-14T06:54:02Z |
| publishDate | 2021-02-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Plant Science |
| spelling | doaj.art-d83692272c844322880fd51a97a0f8f32022-12-21T23:12:48ZengFrontiers Media S.A.Frontiers in Plant Science1664-462X2021-02-011210.3389/fpls.2021.589518589518AtFUT4 and AtFUT6 Are Arabinofuranose-Specific FucosyltransferasesMaria J. Soto0Maria J. Soto1Maria J. Soto2Pradeep Kumar Prabhakar3Pradeep Kumar Prabhakar4Pradeep Kumar Prabhakar5Hsin-Tzu Wang6Hsin-Tzu Wang7Hsin-Tzu Wang8Jason Backe9Jason Backe10Digantkumar Chapla11Digantkumar Chapla12Max Bartetzko13Ian M. Black14Parastoo Azadi15Parastoo Azadi16Maria J. Peña17Maria J. Peña18Fabian Pfrengle19Fabian Pfrengle20Kelley W. Moremen21Kelley W. Moremen22Breeanna R. Urbanowicz23Breeanna R. Urbanowicz24Breeanna R. Urbanowicz25Michael G. Hahn26Michael G. Hahn27Michael G. Hahn28Lawrence Berkeley National Laboratory, DOE Joint Genome Institute, Berkeley, CA, United StatesThe Complex Carbohydrate Research Center, University of Georgia, Athens, GA, United StatesDepartment of Plant Biology, University of Georgia, Athens, GA, United StatesThe Complex Carbohydrate Research Center, University of Georgia, Athens, GA, United StatesCenter for Bioenergy Innovation, Oak Ridge National Laboratory, Oak Ridge, TN, United StatesDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, GA, United StatesThe Complex Carbohydrate Research Center, University of Georgia, Athens, GA, United StatesCenter for Bioenergy Innovation, Oak Ridge National Laboratory, Oak Ridge, TN, United StatesDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, GA, United StatesThe Complex Carbohydrate Research Center, University of Georgia, Athens, GA, United StatesCenter for Bioenergy Innovation, Oak Ridge National Laboratory, Oak Ridge, TN, United StatesThe Complex Carbohydrate Research Center, University of Georgia, Athens, GA, United StatesDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, GA, United StatesDepartment of Biomolecular Systems, Max-Planck-Institute of Colloids and Interfaces, Potsdam, GermanyThe Complex Carbohydrate Research Center, University of Georgia, Athens, GA, United StatesThe Complex Carbohydrate Research Center, University of Georgia, Athens, GA, United StatesDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, GA, United StatesThe Complex Carbohydrate Research Center, University of Georgia, Athens, GA, United StatesCenter for Bioenergy Innovation, Oak Ridge National Laboratory, Oak Ridge, TN, United StatesDepartment of Biomolecular Systems, Max-Planck-Institute of Colloids and Interfaces, Potsdam, GermanyDepartment of Chemistry, University of Natural Resources and Life Sciences, Vienna, AustriaThe Complex Carbohydrate Research Center, University of Georgia, Athens, GA, United StatesDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, GA, United StatesThe Complex Carbohydrate Research Center, University of Georgia, Athens, GA, United StatesCenter for Bioenergy Innovation, Oak Ridge National Laboratory, Oak Ridge, TN, United StatesDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, GA, United StatesThe Complex Carbohydrate Research Center, University of Georgia, Athens, GA, United StatesDepartment of Plant Biology, University of Georgia, Athens, GA, United StatesCenter for Bioenergy Innovation, Oak Ridge National Laboratory, Oak Ridge, TN, United StatesThe 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.https://www.frontiersin.org/articles/10.3389/fpls.2021.589518/fullFucosyltransferasearabinogalactan proteinAtFUT1AtFUT4AtFUT6GT37 |
| spellingShingle | Maria J. Soto Maria J. Soto Maria J. Soto Pradeep Kumar Prabhakar Pradeep Kumar Prabhakar Pradeep Kumar Prabhakar Hsin-Tzu Wang Hsin-Tzu Wang Hsin-Tzu Wang Jason Backe Jason Backe Digantkumar Chapla Digantkumar Chapla Max Bartetzko Ian M. Black Parastoo Azadi Parastoo Azadi Maria J. Peña Maria J. Peña Fabian Pfrengle Fabian Pfrengle Kelley W. Moremen Kelley W. Moremen Breeanna R. Urbanowicz Breeanna R. Urbanowicz Breeanna R. Urbanowicz Michael G. Hahn Michael G. Hahn Michael G. Hahn AtFUT4 and AtFUT6 Are Arabinofuranose-Specific Fucosyltransferases Frontiers in Plant Science Fucosyltransferase arabinogalactan protein AtFUT1 AtFUT4 AtFUT6 GT37 |
| title | AtFUT4 and AtFUT6 Are Arabinofuranose-Specific Fucosyltransferases |
| title_full | AtFUT4 and AtFUT6 Are Arabinofuranose-Specific Fucosyltransferases |
| title_fullStr | AtFUT4 and AtFUT6 Are Arabinofuranose-Specific Fucosyltransferases |
| title_full_unstemmed | AtFUT4 and AtFUT6 Are Arabinofuranose-Specific Fucosyltransferases |
| title_short | AtFUT4 and AtFUT6 Are Arabinofuranose-Specific Fucosyltransferases |
| title_sort | atfut4 and atfut6 are arabinofuranose specific fucosyltransferases |
| topic | Fucosyltransferase arabinogalactan protein AtFUT1 AtFUT4 AtFUT6 GT37 |
| url | https://www.frontiersin.org/articles/10.3389/fpls.2021.589518/full |
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