ArticleNature plants2022
Polymerization of the backbone of the pectic polysaccharide rhamnogalacturonan I.
Article in Nature plants, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 45 citations in OpenAlex.
- Ultrasonic Degradation Improves the In Vitro Utilization of Oolong Tea Pectic Polysaccharides: Structure Characterization and Multi-Omics Insights.Foods (Basel, Switzerland) · 2026Article
- Transcriptome study ofMicrobiology spectrum · 2026Article
- Synthesis, Structural Characterization and In Vitro Immunosuppressive Activity of Quinoa Bran Soluble Dietary Fiber-Gallium Complex.Foods (Basel, Switzerland) · 2026Article
- A characterization of recombinant Arabidopsis FRIABLE1 (FRB1) reveals robust rhamnogalacturonan-I rhamnosyltransferase activity and critical catalytic residues.The Journal of biological chemistry · 2026Article
- Generating 3D models of complex carbohydrates with GLYCAM-Web.Nature methods · 2026Article
- Comparative multi "omics" profiling ofFrontiers in plant science · 2026Article
- A high spatial resolution transcriptomics of tension wood reveals the genetic program of contractile G-layer formation.Frontiers in plant science · 2026Article
- Beyond FERONIA: Gene Expression Profiling Reveals Functional Diversification of Malectin/Malectin-Like Proteins in Tissues with Cell Walls Differing in Pectin Content.Doklady. Biochemistry and biophysics · 2025Article
- Cell wall-related glycosyltransferases and wall architecture in the model liverwort Marchantia polymorpha.The Plant journal : for cell and molecular biology · 2025Article
- Galactan mobilization during carbon starvation compromises plant cell wall-mediated resistance to fungal infection.The Plant journal : for cell and molecular biology · 2025Article
- Mucilicious methods: Navigating the tools developed to Arabidopsis Seed Coat Mucilage analysis.Cell surface (Amsterdam, Netherlands) · 2025Review
- Gibberellin signaling regulates pectin biosynthesis in Arabidopsis.Nature communications · 2025Article
- How it all begins: molecular players of the early graviresponse in the non-elongating part of flax stem.Plant molecular biology · 2025Article
- A Fresh Look at Celery Collenchyma and Parenchyma Cell Walls Through a Combination of Biochemical, Histochemical, and Transcriptomic Analyses.International journal of molecular sciences · 2025Article
- Daily glycome and transcriptome profiling reveals polysaccharide structures and correlated glycosyltransferases critical for cotton fiber growth.The Plant journal : for cell and molecular biology · 2024Article
- Pull the fuzes: Processing protein precursors to generate apoplastic danger signals for triggering plant immunity.Plant communications · 2024Review
- Putative rhamnogalacturonan-II glycosyltransferase identified through callus gene editing which bypasses embryo lethality.Plant physiology · 2024Article
- The plant cell wall-dynamic, strong, and adaptable-is a natural shapeshifter.The Plant cell · 2024Review
- Biochemical data documenting variations in mucilage polysaccharides in a range of glycosyltransferase mutants.Scientific data · 2023Article
- Valorization of polyphenolic compounds from food industry by-products for application in polysaccharide-based nanoparticles.Frontiers in nutrition · 2023Review
Corrections and comments
- Erratum issued
Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
Rhamnogalacturonan I (RG-I) is a major plant cell wall pectic polysaccharide defined by its repeating disaccharide backbone structure of [4)-α-D-GalA-(1,2)-α-L-Rha-(1,]. A family of RG-I:Rhamnosyltransferases (RRT) has previously been identified, but synthesis of the RG-I backbone has not been demonstrated in vitro because the identity of Rhamnogalacturonan I:Galaturonosyltransferase (RG-I:GalAT) was unknown. Here a putative glycosyltransferase, At1g28240/MUCI70, is shown to be an RG-I:GalAT. The name RGGAT1 is proposed to reflect the catalytic activity of this enzyme. When incubated together with the rhamnosyltransferase RRT4, the combined activities of RGGAT1 and RRT4 result in elongation of RG-I acceptors in vitro into a polymeric product. RGGAT1 is a member of a new GT family categorized as GT116, which does not group into existing GT-A clades and is phylogenetically distinct from the GALACTURONOSYLTRANSFERASE (GAUT) family of GalA transferases that synthesize the backbone of the pectin homogalacturonan. RGGAT1 has a predicted GT-A fold structure but employs a metal-independent catalytic mechanism that is rare among glycosyltransferases with this fold type. The identification of RGGAT1 and the 8-member Arabidopsis GT116 family provides a new avenue for studying the mechanism of RG-I synthesis and the function of RG-I in plants.
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