A galactosyltransferase acting on arabinogalactan protein glycans is essential for embryo development in Arabidopsis

Authors

  • Naomi Geshi,

    1. Department of Plant Biology and Biotechnology, University of Copenhagen, Copenhagen, Frederiksberg C, Denmark
    Search for more papers by this author
  • Jorunn N. Johansen,

    1. Institut National de la Recherche Agronomique, Unité Mixte de Recherche 1318, Institut Jean-Pierre Bourgin, Saclay Plant Sciences, Versailles, France
    2. AgroParisTech, Unité Mixte de Recherche 1318, Institut Jean-Pierre Bourgin, Saclay Plant Sciences, Versailles, France
    Current affiliation:
    1. Institute of Immunology, Oslo University Hospital HF, Rikshospitalet, Oslo, Norway
    Search for more papers by this author
  • Adiphol Dilokpimol,

    1. Department of Plant Biology and Biotechnology, University of Copenhagen, Copenhagen, Frederiksberg C, Denmark
    Search for more papers by this author
  • Aurélia Rolland,

    1. Institut National de la Recherche Agronomique, Unité Mixte de Recherche 1318, Institut Jean-Pierre Bourgin, Saclay Plant Sciences, Versailles, France
    2. AgroParisTech, Unité Mixte de Recherche 1318, Institut Jean-Pierre Bourgin, Saclay Plant Sciences, Versailles, France
    Current affiliation:
    1. Anjou Recherche Semences, UMR1191 Physiologie Moleculaire des Semences, Angers Cedex 01, France
    Search for more papers by this author
  • Katia Belcram,

    1. Institut National de la Recherche Agronomique, Unité Mixte de Recherche 1318, Institut Jean-Pierre Bourgin, Saclay Plant Sciences, Versailles, France
    2. AgroParisTech, Unité Mixte de Recherche 1318, Institut Jean-Pierre Bourgin, Saclay Plant Sciences, Versailles, France
    Search for more papers by this author
  • Stéphane Verger,

    1. Institut National de la Recherche Agronomique, Unité Mixte de Recherche 1318, Institut Jean-Pierre Bourgin, Saclay Plant Sciences, Versailles, France
    2. AgroParisTech, Unité Mixte de Recherche 1318, Institut Jean-Pierre Bourgin, Saclay Plant Sciences, Versailles, France
    Search for more papers by this author
  • Toshihisa Kotake,

    1. Division of Life Science, Graduate School of Science and Engineering, Saitama University, Saitama, Japan
    Search for more papers by this author
  • Yoichi Tsumuraya,

    1. Division of Life Science, Graduate School of Science and Engineering, Saitama University, Saitama, Japan
    Search for more papers by this author
  • Satoshi Kaneko,

    1. Food Biotechnology Division, National Food Research Institute, Tsukuba, Ibaraki, Japan
    Search for more papers by this author
  • Theodora Tryfona,

    1. Department of Biochemistry, Cambridge University, Cambridge, UK
    Search for more papers by this author
  • Paul Dupree,

    1. Department of Biochemistry, Cambridge University, Cambridge, UK
    Search for more papers by this author
  • Henrik V. Scheller,

    1. Department of Plant Biology and Biotechnology, University of Copenhagen, Copenhagen, Frederiksberg C, Denmark
    2. Joint BioEnergy Institute, Feedstocks Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA
    Search for more papers by this author
  • Herman Höfte,

    1. Institut National de la Recherche Agronomique, Unité Mixte de Recherche 1318, Institut Jean-Pierre Bourgin, Saclay Plant Sciences, Versailles, France
    2. AgroParisTech, Unité Mixte de Recherche 1318, Institut Jean-Pierre Bourgin, Saclay Plant Sciences, Versailles, France
    Search for more papers by this author
  • Gregory Mouille

    Corresponding author
    1. Institut National de la Recherche Agronomique, Unité Mixte de Recherche 1318, Institut Jean-Pierre Bourgin, Saclay Plant Sciences, Versailles, France
    2. AgroParisTech, Unité Mixte de Recherche 1318, Institut Jean-Pierre Bourgin, Saclay Plant Sciences, Versailles, France
    • Department of Plant Biology and Biotechnology, University of Copenhagen, Copenhagen, Frederiksberg C, Denmark
    Search for more papers by this author

For correspondence (e-mail gregory.mouille@versailles.inra.fr).

Summary

Arabinogalactan proteins (AGPs) are a complex family of cell-wall proteoglycans that are thought to play major roles in plant growth and development. Genetic approaches to studying AGP function have met limited success so far, presumably due to redundancy within the large gene families encoding AGP backbones. Here we used an alternative approach for genetic dissection of the role of AGPs in development by modifying their glycan side chains. We have identified an Arabidopsis glycosyltransferase of CAZY family GT31 (AtGALT31A) that galactosylates AGP side chains. A mutation in the AtGALT31A gene caused the arrest of embryo development at the globular stage. The presence of the transcript in the suspensor of globular-stage embryos is consistent with a role for AtGALT31A in progression of embryo development beyond the globular stage. The first observable defect in the mutant is perturbation of the formative asymmetric division of the hypophysis, indicating an essential role for AGP proteoglycans in either specification of the hypophysis or orientation of the asymmetric division plane.

Ancillary