Intermolecular interactions between glycomodules of plant cell wall arabinogalactan-proteins and extensins

Abstract

Hydroxyproline-rich glycoproteins (HRGPs) are a unique component of plant cell walls, undergoing extensive posttranslational modification such as proline hydroxylation and hydroxyproline-O-glycosylation. Arabinogalactan proteins (AGPs) and extensins are major members of the HRGP superfamily. AGPs have repetitive AlaHyp, SerHyp, and ThrHyp peptides, the Hyp residues being glycosylated with large type II arabinogalactan polysaccharides, while extensins contain characteristic SerHyp4 and SerHyp2 motifs with arabinosylated (1–4 residues) Hyp. Although they are less than ten percent in all wall materials, AGPs and extensins play important roles in all aspects of plant growth and development. The detailed mechanisms of their functions are still under investigation. However, many of the functions may be attributed to their adhesive properties. Here, we used a forced unbinding technique to measure relative adhesive potential of the well characterized (AlaHyp)51 and (SerHyp4)18 glycomodules representing AGPs and extensins, respectively. In the presence of different wall ions such as protons, Ca2+, and boron, the glycomodules exhibited different adhesive patterns, suggesting that the wall ion-regulated intermolecular interactions/adhesions between AGPs and/or extensins may be involved in maintaining wall-plasma membrane integrity during wall loosening processes such as wall elongation or expansion. This research applies a biophysical approach to understand the biological function of plant cell wall glycoproteins.