Expression of an apoplast-localized BURP-domain protein from soybean (GmRD22) enhances tolerance towards abiotic stress

Plant Cell Environ. 2012 Nov;35(11):1932-47. doi: 10.1111/j.1365-3040.2012.02526.x. Epub 2012 May 22.

Abstract

The BURP-domain protein family comprises a diverse group of plant-specific proteins that share a conserved BURP domain at the C terminus. However, there have been only limited studies on the functions and subcellular localization of these proteins. Members of the RD22-like subfamily are postulated to associate with stress responses due to the stress-inducible nature of some RD22-like genes. In this report, we used different transgenic systems (cells and in planta) to show that the expression of a stress-inducible RD22-like protein from soybean (GmRD22) can alleviate salinity and osmotic stress. We also performed detailed microscopic studies using both fusion proteins and immuno-electron microscopic techniques to demonstrate the apoplast localization of GmRD22, for which the BURP domain is a critical determinant of the subcellular localization. The apoplastic GmRD22 interacts with a cell wall peroxidase and the ectopic expression of GmRD22 in both transgenic Arabidopsis thaliana and transgenic rice resulted in increased lignin production when subjected to salinity stress. It is possible that GmRD22 regulates cell wall peroxidases and hence strengthens cell wall integrity under such stress conditions.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Motifs
  • Arabidopsis / genetics
  • Cloning, Molecular
  • Glycine max / genetics*
  • Glycine max / metabolism
  • Glycine max / physiology
  • Nicotiana / genetics
  • Oryza / genetics
  • Osmotic Pressure
  • Peroxidase / metabolism
  • Phylogeny
  • Plant Proteins / analysis
  • Plant Proteins / genetics
  • Plant Proteins / physiology*
  • Plant Roots / genetics
  • Plant Roots / growth & development
  • Plant Roots / physiology
  • Plants, Genetically Modified
  • Stress, Physiological*

Substances

  • Plant Proteins
  • Peroxidase