Molecular cloning and expression of Arabidopsis fatty acid hydroperoxide lyase

Plant Cell Physiol. 1999 May;40(5):477-81. doi: 10.1093/oxfordjournals.pcp.a029567.

Abstract

Fatty acid hydroperoxide lyase (HPOL), an enzyme of the octadecanoid pathway that forms carbon-6 aldehydes such as n-hexanal or (Z)-3-hexenal, was cloned from Arabidopsis thaliana as a full-length cDNA. The HPOL activity obtained by expressing the cDNA in Escherichia coli formed n-hexanal from linoleic acid 13-hydroperoxide, whereas linoleic acid 9-hydroperoxide was not a substrate for the enzyme. The HPOL mRNA is expressed at low level in leaves; however, its accumulation can be found in the inflorescence. Wounding or methyl jasmonate treatments increase the mRNA level in leaves. These results indicate that the HPOL gene is up-regulated in leaves in response to wounding and that the enzyme may be an active component of the octadecanoid defense response.

MeSH terms

  • Aldehyde-Lyases / genetics*
  • Aldehyde-Lyases / metabolism
  • Arabidopsis / enzymology*
  • Arabidopsis / genetics*
  • Base Sequence
  • Cloning, Molecular
  • Cytochrome P-450 Enzyme System*
  • DNA Primers / genetics
  • DNA, Complementary / genetics
  • DNA, Plant / genetics
  • Escherichia coli / genetics
  • Gene Expression
  • Genes, Plant

Substances

  • DNA Primers
  • DNA, Complementary
  • DNA, Plant
  • Cytochrome P-450 Enzyme System
  • Aldehyde-Lyases
  • hydroperoxide lyase