Wall-associated kinase WAK1 interacts with cell wall pectins in a calcium-induced conformation

Annabelle Decreux, Johan Messiaen

Research output: Contribution to journalArticle

Abstract

Wall-associated kinase 1 (WAK1) is a transmembrane protein containing a cytoplasmic Ser/Thr kinase domain and an extracellular domain in contact with the pectin fraction of the plant cell walls. In order to characterize further the interaction of WAK1 with pectin, a 564 bp DNA sequence corresponding to amino acids 67'254 of the extracellular domain of WAK1 from Arabidopsis thaliana was cloned and expressed as a soluble recombinant peptide in yeast. Using enzyme-linked immunosorbent assays (ELISA), we show that peptide WAK67'254 binds to polygalacturonic acid (PGA), oligogalacturonides, pectins extracted from A. thaliana cell walls and to structurally related alginates. Our results suggest that both ionic and steric interactions are required to match the relatively linear pectin backbone. Binding of WAK67'254 to PGA, oligogalacturonides and alginates occurred only in the presence of calcium and in ionic conditions promoting the formation of calcium bridges between oligo-and polymers (also known as 'egg-boxes'). The conditions inhibiting the formation of calcium bridges (EDTA treatment, calcium substitution, high NaCl concentrations, depolymerization and methylesterification of pectins) also inhibited the binding of WAK67'254 to calciuminduced egg-boxes. The relevance of this non-covalent link between WAK67'254 and cell wall pectins is discussed in terms of cell elongation, cell differentiation and host'pathogen interactions.
Original languageEnglish
Pages (from-to)268-278
Number of pages11
JournalPlant Cell Physiol,
Volume46
Issue number2
Publication statusPublished - 2005

Fingerprint

Pectins
pectins
Cell Wall
phosphotransferases (kinases)
Phosphotransferases
Alginates
cell walls
Calcium
calcium
Arabidopsis
Ovum
alginates
Host-Pathogen Interactions
Peptides
Plant Cells
Arabidopsis thaliana
Edetic Acid
peptides
Cell Differentiation
Polymers

Keywords

  • Arabidopsis thaliana ¿ Cell wall ¿ Egg-box ¿ Pectin ¿ Receptor kinase ¿ Wall-associated kinase

Cite this

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title = "Wall-associated kinase WAK1 interacts with cell wall pectins in a calcium-induced conformation",
abstract = "Wall-associated kinase 1 (WAK1) is a transmembrane protein containing a cytoplasmic Ser/Thr kinase domain and an extracellular domain in contact with the pectin fraction of the plant cell walls. In order to characterize further the interaction of WAK1 with pectin, a 564 bp DNA sequence corresponding to amino acids 67'254 of the extracellular domain of WAK1 from Arabidopsis thaliana was cloned and expressed as a soluble recombinant peptide in yeast. Using enzyme-linked immunosorbent assays (ELISA), we show that peptide WAK67'254 binds to polygalacturonic acid (PGA), oligogalacturonides, pectins extracted from A. thaliana cell walls and to structurally related alginates. Our results suggest that both ionic and steric interactions are required to match the relatively linear pectin backbone. Binding of WAK67'254 to PGA, oligogalacturonides and alginates occurred only in the presence of calcium and in ionic conditions promoting the formation of calcium bridges between oligo-and polymers (also known as 'egg-boxes'). The conditions inhibiting the formation of calcium bridges (EDTA treatment, calcium substitution, high NaCl concentrations, depolymerization and methylesterification of pectins) also inhibited the binding of WAK67'254 to calciuminduced egg-boxes. The relevance of this non-covalent link between WAK67'254 and cell wall pectins is discussed in terms of cell elongation, cell differentiation and host'pathogen interactions.",
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Wall-associated kinase WAK1 interacts with cell wall pectins in a calcium-induced conformation. / Decreux, Annabelle; Messiaen, Johan.

In: Plant Cell Physiol, , Vol. 46, No. 2, 2005, p. 268-278.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Wall-associated kinase WAK1 interacts with cell wall pectins in a calcium-induced conformation

AU - Decreux, Annabelle

AU - Messiaen, Johan

PY - 2005

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N2 - Wall-associated kinase 1 (WAK1) is a transmembrane protein containing a cytoplasmic Ser/Thr kinase domain and an extracellular domain in contact with the pectin fraction of the plant cell walls. In order to characterize further the interaction of WAK1 with pectin, a 564 bp DNA sequence corresponding to amino acids 67'254 of the extracellular domain of WAK1 from Arabidopsis thaliana was cloned and expressed as a soluble recombinant peptide in yeast. Using enzyme-linked immunosorbent assays (ELISA), we show that peptide WAK67'254 binds to polygalacturonic acid (PGA), oligogalacturonides, pectins extracted from A. thaliana cell walls and to structurally related alginates. Our results suggest that both ionic and steric interactions are required to match the relatively linear pectin backbone. Binding of WAK67'254 to PGA, oligogalacturonides and alginates occurred only in the presence of calcium and in ionic conditions promoting the formation of calcium bridges between oligo-and polymers (also known as 'egg-boxes'). The conditions inhibiting the formation of calcium bridges (EDTA treatment, calcium substitution, high NaCl concentrations, depolymerization and methylesterification of pectins) also inhibited the binding of WAK67'254 to calciuminduced egg-boxes. The relevance of this non-covalent link between WAK67'254 and cell wall pectins is discussed in terms of cell elongation, cell differentiation and host'pathogen interactions.

AB - Wall-associated kinase 1 (WAK1) is a transmembrane protein containing a cytoplasmic Ser/Thr kinase domain and an extracellular domain in contact with the pectin fraction of the plant cell walls. In order to characterize further the interaction of WAK1 with pectin, a 564 bp DNA sequence corresponding to amino acids 67'254 of the extracellular domain of WAK1 from Arabidopsis thaliana was cloned and expressed as a soluble recombinant peptide in yeast. Using enzyme-linked immunosorbent assays (ELISA), we show that peptide WAK67'254 binds to polygalacturonic acid (PGA), oligogalacturonides, pectins extracted from A. thaliana cell walls and to structurally related alginates. Our results suggest that both ionic and steric interactions are required to match the relatively linear pectin backbone. Binding of WAK67'254 to PGA, oligogalacturonides and alginates occurred only in the presence of calcium and in ionic conditions promoting the formation of calcium bridges between oligo-and polymers (also known as 'egg-boxes'). The conditions inhibiting the formation of calcium bridges (EDTA treatment, calcium substitution, high NaCl concentrations, depolymerization and methylesterification of pectins) also inhibited the binding of WAK67'254 to calciuminduced egg-boxes. The relevance of this non-covalent link between WAK67'254 and cell wall pectins is discussed in terms of cell elongation, cell differentiation and host'pathogen interactions.

KW - Arabidopsis thaliana ¿ Cell wall ¿ Egg-box ¿ Pectin ¿ Receptor kinase ¿ Wall-associated kinase

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