ArticlePlant physiology2010
Identification and characterization of in vitro galactosyltransferase activities involved in arabinogalactan-protein glycosylation in tobacco and Arabidopsis.
Article in Plant physiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 34 citations in OpenAlex.
- Intracellular trafficking and glycosylation of hydroxyproline-O-glycosylation module in tobacco BY-2 cells is dependent on medium composition and transcriptome analysis.Scientific reports · 2023Article
- Polymer Nanocomposites of Selenium Biofabricated Using Fungi.Molecules (Basel, Switzerland) · 2021Review
- Elucidating the roles of three β-glucuronosyltransferases (GLCATs) acting on arabinogalactan-proteins using a CRISPR-Cas9 multiplexing approach in Arabidopsis.BMC plant biology · 2020Article
- Identification of Hydroxyproline-Containing Proteins and Hydroxylation of Proline Residues in Rice.Frontiers in plant science · 2020Article
- Engineering 'designer' glycomodules for boosting recombinant protein secretion in tobacco hairy root culture and studying hydroxyproline-O-glycosylation process in plants.Plant biotechnology journal · 2019Article
- A small multigene hydroxyproline-O-galactosyltransferase family functions in arabinogalactan-protein glycosylation, growth and development in Arabidopsis.BMC plant biology · 2015Article
- Article
- Identification of Novel Peptidyl Serine α-Galactosyltransferase Gene Family in Plants.The Journal of biological chemistry · 2014Article
- Cell wall O-glycoproteins and N-glycoproteins: aspects of biosynthesis and function.Frontiers in plant science · 2014Review
- Biochemical and physiological characterization of fut4 and fut6 mutants defective in arabinogalactan-protein fucosylation in Arabidopsis.Journal of experimental botany · 2013Article
- A gene responsible for prolyl-hydroxylation of moss-produced recombinant human erythropoietin.Scientific reports · 2013Article
- Functional identification of a hydroxyproline-o-galactosyltransferase specific for arabinogalactan protein biosynthesis in Arabidopsis.The Journal of biological chemistry · 2013Article
- Article
- Toward stable genetic engineering of human O-glycosylation in plants.Plant physiology · 2012Article
- Engineering mammalian mucin-type O-glycosylation in plants.The Journal of biological chemistry · 2012Article
- Characterization of the arabinogalactan protein 31 (AGP31) of Arabidopsis thaliana: new advances on the Hyp-O-glycosylation of the Pro-rich domain.The Journal of biological chemistry · 2012Article
- Arabinogalactan-proteins and the research challenges for these enigmatic plant cell surface proteoglycans.Frontiers in plant science · 2012Article
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6 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Arabinogalactan-proteins (AGPs) are highly glycosylated hydroxyproline (Hyp)-rich glycoproteins that are frequently characterized by the presence of [Alanine-Hyp] ([AO]) repetitive units. AGP galactosyltransferase (GalT) activities in tobacco (Nicotiana tabacum) and Arabidopsis (Arabidopsis thaliana) microsomal membranes were studied here with an in vitro GalT reaction system, which used acceptor substrates composed of [AO] repetitive units, specifically, a chemically synthesized [AO](7) acceptor and a transgenically produced and deglycosylated d[AO](51) acceptor. Incorporation of [(14)C]Gal from UDP-[(14)C]Gal into the [AO](7) and d[AO](51) acceptors was observed following HPLC fractionation of the reaction products. Hyp-[(14)C]Gal monosaccharide and Hyp-[(14)C]Gal disaccharide were identified in the base hydrolysates of the GalT reaction products, indicating the presence of two distinct GalT activities for the addition of the first and second Gal residues to the [AO] peptide in both tobacco and Arabidopsis. Examination of the Arabidopsis Hyp:GalT activity using various acceptor substrates, including two extensin sequences containing SO(4) modules and a [AP](7) peptide, indicated this activity was specific for peptidyl Hyp in AGP sequences. Mass spectrometry analysis demonstrated that only one Gal was added per peptide molecule to the C-terminal or penultimate Hyp residue of the [AO](7) peptide. In addition, [AO](7):GalT and d[AO](51):GalT activities were localized to the endomembrane system of Arabidopsis suspension-cultured cells following sucrose density gradient centrifugation. The in vitro assay reported here to detect GalT activities using AGP peptide and glycopeptide acceptor substrates provides a useful tool for the identification and verification of AGP-specific GalT proteins/genes and an entry point for elucidation of arabinogalactan biosynthesis for AGPs.
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