Arabidopsis CLV3 peptide directly binds CLV1 ectodomain

Science. 2008 Jan 18;319(5861):294. doi: 10.1126/science.1150083.

Abstract

CLV1, which encodes a leucine-rich repeat receptor kinase, and CLV3, which encodes a secreted peptide, function in the same genetic pathway to maintain stem cell populations in Arabidopsis shoot apical meristem. Here, we show biochemical evidence, by ligand binding assay and photoaffinity labeling, that the CLV3 peptide directly binds the CLV1 ectodomain with a dissociation constant of 17.5 nM. The CLV1 ectodomain also interacts with the structurally related CLE peptides, with distinct affinities depending on the specific amino acid sequence. Our results provide direct evidence that CLV3 and CLV1 function as a ligand-receptor pair involved in stem cell maintenance.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Arabidopsis / cytology
  • Arabidopsis / genetics
  • Arabidopsis / metabolism*
  • Arabidopsis Proteins / chemistry
  • Arabidopsis Proteins / metabolism*
  • Cell Line
  • Genes, Plant
  • Ligands
  • Meristem / cytology
  • Meristem / metabolism
  • Nicotiana
  • Peptides / chemistry
  • Peptides / metabolism
  • Plants, Genetically Modified
  • Protein Binding
  • Protein Serine-Threonine Kinases
  • Protein Structure, Tertiary
  • Receptor Protein-Tyrosine Kinases / chemistry
  • Receptor Protein-Tyrosine Kinases / metabolism*

Substances

  • AT2G27250 protein, Arabidopsis
  • Arabidopsis Proteins
  • Ligands
  • Peptides
  • Receptor Protein-Tyrosine Kinases
  • CLV1 protein, Arabidopsis
  • Protein Serine-Threonine Kinases