Characterization of the Arabidopsis lecRK-a genes: members of a superfamily encoding putative receptors with an extracellular domain homologous to legume lectins

Plant Mol Biol. 1999 Mar;39(4):671-82. doi: 10.1023/a:1006136701595.

Abstract

An Arabidopsis cDNA clone that defines a new class of plant serine/threonine receptor kinases was found to be a member of a family of four clustered genes (lecRK-a1-a4) which have been cloned, sequenced and mapped on chromosome 3. This family belongs to a large superfamily encoding putative receptors with an extracellular domain homologous to legume lectins and appears to be conserved at least among dicots. In the Columbia ecotype only the lecRK-a1 and perhaps the lecRK-a3 gene is functional, since lecRK-a2 is disrupted by a Ty-copia retroelement and lecRK-a4 contains a frameshift mutation. Structural analysis of the lecRK-al and lecRK-a3 deduced amino-acid sequences suggests that the lectin domain is unlikely to be involved in binding monosaccharides but could interact with complex glycans and/or with hydrophobic ligands. Immunodetection of lecRK gene products in plasma membranes purified by free-flow electrophoresis showed that the lecRK-a proteins are probably highly glycosylated integral plasma membrane components.

MeSH terms

  • Amino Acid Sequence
  • Arabidopsis / genetics*
  • Binding Sites
  • Chromosome Mapping
  • Evolution, Molecular
  • Fabaceae / genetics
  • Genes, Plant
  • Lectins / chemistry
  • Models, Molecular
  • Molecular Sequence Data
  • Multigene Family
  • Phylogeny
  • Plant Lectins
  • Plant Proteins / genetics*
  • Plants, Medicinal
  • Protein Conformation
  • Receptors, Mitogen / genetics*
  • Restriction Mapping
  • Sequence Alignment
  • Sequence Homology, Amino Acid

Substances

  • Lectins
  • Plant Lectins
  • Plant Proteins
  • Receptors, Mitogen