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Title: Biochemical and physiological characterization of fut4 and fut6 mutants defective in arabinogalactan-protein fucosylation in Arabidopsis

Journal Article · · Journal of Experimental Botany
DOI:https://doi.org/10.1093/jxb/ert321· OSTI ID:1625382
 [1];  [2];  [3];  [4];  [4];  [5];  [2];  [6];  [2]
  1. Ohio Univ., Athens, OH (United States). Dept. of Environmental and Plant Biology; Ohio Univ., Athens, OH (United States). Molecular and Cellular Biology Program; Joint BioEnergy Institute (JBEI), Emeryville, CA (United States)
  2. Ohio Univ., Athens, OH (United States). Dept. of Environmental and Plant Biology; Ohio Univ., Athens, OH (United States). Molecular and Cellular Biology Program
  3. Univ. of Georgia, Athens, GA (United States). Complex Carbohydrate Research Center
  4. Ohio Univ., Athens, OH (United States). Dept. of Environmental and Plant Biology
  5. SAS Inst., Cary, NC (United States)
  6. Univ. of Georgia, Athens, GA (United States). Complex Carbohydrate Research Center; Univ. of Georgia, Athens, GA (United States). Dept. of Plant Biology
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Arabinogalactan-proteins (AGPs) are highly glycosylated hydroxyproline-rich glycoproteins present in plant cell walls. AGPs are characterized by arabinose-/galactose-rich side chains, which define their interactive molecular surface. Fucose residues are found in some dicotyledon AGPs, and AGP fucosylation is developmentally regulated. We previously identified Arabidopsis thaliana FUT4 and FUT6 genes as AGP-specific fucosyltransferases (FUTs) based on their enzymatic activities when heterologously expressed in tobacco (Nicotiana tabacum) BY2 suspension-cultured cells. Here, the functions of FUT4 and FUT6 and the physiological roles of fucosylated AGPs were further investigated using Arabidopsis fut4, fut6, and fut4/fut6 mutant plants. All mutant plants showed no phenotypic differences compared to wild-type plants under physiological conditions, but showed reduced root growth in the presence of elevated NaCl. However, roots of wild-type and fut4 mutant plants contained terminal fucose epitopes, which were absent in fut6 and fut4/fut6 mutant plants as indicated by eel lectin staining. Monosaccharide analysis showed fucose was present in wild-type leaf and root AGPs, but absent in fut4 leaf AGPs and in fut4/fut6 double mutant leaf and root AGPs, indicating that FUT4 was required for fucosylation of leaf AGPs while both FUT4 and FUT6 contributed to fucosylation of root AGPs. Glycome profiling of cell wall fractions from mutant roots and leaves showed distinct glycome profiles compared to wild-type plants, indicating that fucosyl residues on AGPs may regulate intermolecular interactions between AGPs and other wall components. The current work exemplifies the possibilities of refinement of cell wall structures by manipulation of a single or a few cell wall biosynthetic genes.

Research Organization:
Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States). National Energy Research Scientific Computing Center (NERSC)
Sponsoring Organization:
USDOE Office of Science (SC), Biological and Environmental Research (BER). Biological Systems Science Division; USDA; National Science Foundation (NSF)
Grant/Contract Number:
AC02-05CH11231; PS02-06ER64304; 2008-35318-04563; 2008-35318-04572; DBI-0421683
OSTI ID:
1625382
Journal Information:
Journal of Experimental Botany, Vol. 64, Issue 18; ISSN 0022-0957
Publisher:
Oxford University PressCopyright Statement
Country of Publication:
United States
Language:
English

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Arabinogalactan proteins: focus on carbohydrate active enzymes journal June 2014
Growth of the Fucus embryo: insights into wall-mediated cell expansion through mechanics and transcriptomics posted_content January 2020
Immunological Approaches to Biomass Characterization and Utilization journal October 2015
Plant Fucosyltransferases and the Emerging Biological Importance of Fucosylated Plant Structures journal July 2019
A small multigene hydroxyproline-O-galactosyltransferase family functions in arabinogalactan-protein glycosylation, growth and development in Arabidopsis journal December 2015
Control of stem-cell niche establishment in Arabidopsis flowers by REVOLUTA and the LEAFY-RAX1 module posted_content January 2018
An important role of l ‐fucose biosynthesis and protein fucosylation genes in Arabidopsis immunity journal January 2019
Extensin and Arabinogalactan-Protein Biosynthesis: Glycosyltransferases, Research Challenges, and Biosensors journal June 2016
The Arabidopsis Golgi-localized GDP-L-fucose transporter is required for plant development journal July 2016
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Two Hydroxyproline Galactosyltransferases, GALT5 and GALT2, Function in Arabinogalactan-Protein Glycosylation, Growth and Development in Arabidopsis journal May 2015
Post-Synthetic Defucosylation of AGP by Aspergillus nidulans α-1,2-Fucosidase Expressed in Arabidopsis Apoplast Induces Compensatory Upregulation of α-1,2-Fucosyltransferases journal July 2016
Characterisation of FUT4 and FUT6 α-(1 → 2)-fucosyltransferases reveals that absence of root arabinogalactan fucosylation increases Arabidopsis root growth salt sensitivity. text January 2014
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54 ENVIRONMENTAL SCIENCES
plant sciences
arabidopsis
arabinogalactan-proteins
fucosyltransferase
glycosylation
hydroxyproline-rich proteins
plant cell wall