Functional analysis of a beta-ketoacyl-CoA synthase gene, MpFAE2, by gene silencing in the liverwort Marchantia polymorpha L

Biosci Biotechnol Biochem. 2003 Mar;67(3):605-12. doi: 10.1271/bbb.67.605.

Abstract

We have isolated a beta-ketoacyl CoA synthase (KCS) gene, MpFAE2, from a liverwort, Marchantia polymorpha, and identified its substrate specificity using the technique of dsRNA-mediated gene silencing and overexpression. KCS catalyzes an essential reaction in the fatty acid elongation process, i.e., condensation of malonyl-CoA with acyl-CoA. By introducing a construct with a hairpin structure containing a partial MpFAE2 gene, the level of the MpFAE2 gene expression was suppressed constitutively. The transgenic plants showed a specific accumulation of fatty acid 18:0. In contrast, in transgenic M. polymorpha plants overexpressing the MpFAE2 gene, fatty acid 22:0 is accumulated. These results indicate that the MpFAE2 gene product catalyzes the elongation steps of 18:0 to 20:0 and possibly also of 20:0 to 22:0.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 3-Oxoacyl-(Acyl-Carrier-Protein) Synthase / genetics*
  • 3-Oxoacyl-(Acyl-Carrier-Protein) Synthase / metabolism*
  • Acetyl Coenzyme A / chemistry
  • Acetyl Coenzyme A / metabolism
  • Amino Acid Sequence
  • Blotting, Northern
  • Blotting, Southern
  • Fatty Acids / analysis
  • Fatty Acids / metabolism
  • Gene Silencing*
  • Hepatophyta / enzymology*
  • Hepatophyta / genetics*
  • Malonyl Coenzyme A / chemistry
  • Malonyl Coenzyme A / metabolism
  • Molecular Sequence Data
  • Nucleic Acid Conformation
  • Plants, Genetically Modified
  • RNA Interference
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Substrate Specificity

Substances

  • Fatty Acids
  • Malonyl Coenzyme A
  • Acetyl Coenzyme A
  • 3-Oxoacyl-(Acyl-Carrier-Protein) Synthase