A tomato lipase homologous to DAD1 (LeLID1) is induced in post-germinative growing stage and encodes a triacylglycerol lipase

FEBS Lett. 2004 Jul 2;569(1-3):195-200. doi: 10.1016/j.febslet.2004.05.064.

Abstract

A tomato lipase gene homologous to Arabidopsis DAD1 (lipase homologous to DAD1; LeLID1) was cloned and characterized. The corresponding transcript increased rapidly during germination of the seeds and reached a maximum level at four days after germination. Thereafter, it decreased rapidly. Little expression could be found in flowers or fruits. Immunoblot analyses showed that the gene products could be found in the cotyledons and hypocotyls, but not in the roots. In the cotyledons most LeLID1 could be recovered in a soluble fraction. The recombinant LeLID1 protein showed maximum lipase activity at pH 8.0. It showed high activity against triacylglycerols (TAGs) with long acyl chains, but little activity with phosphatidylcholine or monogalactosyldiacylglycerol. TAGs composed of short acyl chains could not be a substrate for the enzyme. A possible involvement of LeLID1 in fat mobilization during seed germination is discussed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Carboxylic Ester Hydrolases / chemistry
  • Carboxylic Ester Hydrolases / genetics*
  • Carboxylic Ester Hydrolases / metabolism
  • Cloning, Molecular
  • Conserved Sequence
  • Germination
  • Kinetics
  • Lipase / chemistry
  • Lipase / genetics*
  • Lipase / metabolism
  • Molecular Sequence Data
  • Open Reading Frames
  • Plant Proteins / chemistry
  • Plant Proteins / genetics
  • Plant Proteins / isolation & purification
  • Plant Proteins / metabolism
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / isolation & purification
  • Recombinant Proteins / metabolism
  • Reverse Transcriptase Polymerase Chain Reaction
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Solanum lycopersicum / enzymology
  • Solanum lycopersicum / physiology*
  • Substrate Specificity

Substances

  • Plant Proteins
  • Recombinant Proteins
  • Carboxylic Ester Hydrolases
  • Lipase