Rice C2-domain proteins are induced and translocated to the plasma membrane in response to a fungal elicitor

Biochemistry. 2003 Oct 14;42(40):11625-33. doi: 10.1021/bi034576n.

Abstract

Hundreds of proteins involved in signaling pathways contain a Ca(2+)-dependent membrane-binding motif called the C2-domain. However, no small C2-domain proteins consisting of a single C2-domain have been reported in animal cells. We have isolated two cDNA clones, OsERG1a and OsERG1b, that encode two small C2-domain proteins of 156 and 159 amino acids, respectively, from a fungal elicitor-treated rice cDNA library. The clones are believed to have originated from a single gene by alternative splicing. Transcript levels of the OsERG1 gene are dramatically elevated by a fungal elicitor prepared from Magnaporthe grisea or by Ca(2+) ions. The OsERG1 protein produced in Escherichia coli binds to phospholipid vesicles in a Ca(2+)-dependent manner and is translocated to the plasma membrane of plant cells by treatment with either a fungal elicitor or a Ca(2+) ionophore. These results suggest that OsERG1 proteins containing a single C2-domain are involved in plant defense signaling systems.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Motifs / genetics
  • Amino Acid Sequence
  • Calcium Signaling / physiology
  • Cell Membrane / genetics
  • Cell Membrane / metabolism
  • Cell Membrane / microbiology
  • Cloning, Molecular
  • Cytosol / chemistry
  • Cytosol / metabolism
  • Gene Expression Regulation, Plant
  • Genes, Plant
  • Genome, Plant
  • Magnaporthe / pathogenicity*
  • Magnaporthe / physiology*
  • Membrane Proteins / biosynthesis*
  • Membrane Proteins / genetics
  • Membrane Proteins / isolation & purification
  • Membrane Proteins / metabolism*
  • Molecular Sequence Data
  • Oryza / chemistry*
  • Oryza / genetics
  • Oryza / microbiology*
  • Phospholipids / chemistry
  • Phospholipids / metabolism
  • Plant Diseases / microbiology
  • Plant Proteins / biosynthesis*
  • Plant Proteins / genetics
  • Plant Proteins / isolation & purification
  • Plant Proteins / metabolism*
  • Protein Binding / genetics
  • Protein Structure, Tertiary / genetics
  • Protein Transport

Substances

  • Membrane Proteins
  • Phospholipids
  • Plant Proteins

Associated data

  • GENBANK/AF512505