A novel patatin-like protein from cotton plant, GhPat1, is co-expressed with GhLox1 during Xanthomonas campestris-mediated hypersensitive cell death

Plant Cell Rep. 2009 Jan;28(1):155-64. doi: 10.1007/s00299-008-0622-x. Epub 2008 Oct 11.

Abstract

In cotton plant, Xanthomonas-induced hypersensitive response (HR) is accompanied by a lipid peroxidation process involving a 9-lipoxygenase (LOX), GhLox1. Initiation of this oxidative metabolism implies the release of the LOX substrates, or polyunsaturated fatty acids. Since patatin-like proteins (PLPs) are likely candidates for mediating the latter step, we searched for genes encoding such enzymes, identified and cloned one of them that we named GhPat1. Biochemical and molecular studies showed that GhPat1 expression was up-regulated during the incompatible interaction, prior to the onset of the corresponding galactolipase activity and cell death symptoms in tissues. Protein sequence analysis and modelling also revealed that GhPat1 catalytic amino acids and fold were conserved across plant PLPs. Based on these results and our previous work (Jalloul et al. in Plant J 32:1-12, 2002), a role for GhPat1, in synergy with GhLox1, during HR-specific lipid peroxidation is discussed.

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Carboxylic Ester Hydrolases / genetics
  • Carboxylic Ester Hydrolases / metabolism*
  • Cell Death*
  • Cloning, Molecular
  • DNA, Complementary / genetics
  • Expressed Sequence Tags
  • Gene Expression Profiling
  • Gene Expression Regulation, Plant
  • Genes, Plant
  • Gossypium / genetics*
  • Gossypium / metabolism
  • Gossypium / microbiology
  • Molecular Sequence Data
  • Plant Proteins / genetics
  • Plant Proteins / metabolism*
  • Protein Structure, Tertiary
  • RNA, Plant / genetics
  • Sequence Alignment
  • Sequence Analysis, Protein
  • Xanthomonas campestris / pathogenicity*

Substances

  • DNA, Complementary
  • Plant Proteins
  • RNA, Plant
  • Carboxylic Ester Hydrolases