AtDGAT2 is a functional acyl-CoA:diacylglycerol acyltransferase and displays different acyl-CoA substrate preferences than AtDGAT1

FEBS Lett. 2013 Aug 2;587(15):2371-6. doi: 10.1016/j.febslet.2013.06.003. Epub 2013 Jun 13.

Abstract

Demonstration of the function of the Arabidopsis thaliana acyl-CoA:diacylglycerol acyltransferase 2 (AtDGAT2) has remained elusive despite biochemical testing of genetic mutants and overexpression lines. We show that transiently expressed AtDGAT2 in the Nicotiana benthamiana leaf resulted in an increase in triacylglycerol twice as great as the increase observed following parallel expression of AtDGAT1. AtDGAT2 showed higher conversion from labeled diacylglycerol to triacylglycerol compared to AtDGAT1, and was acyl-CoA dependent. In addition, AtDGAT2 had different acyl-CoA substrate preference than AtDGAT1. These results allow us to conclude that AtDAGT2 is a functional acyl-CoA:diacylglycerol acyltransferase enzyme that can catalyse substantial increase in TAG synthesis.

Keywords: Acyltransferase; DGAT2; Leaf fatty acid; Nicotiana benthamiana infiltration; Oil increase; TAG.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Arabidopsis / embryology*
  • Arabidopsis Proteins / physiology*
  • Base Sequence
  • DNA Primers
  • Diacylglycerol O-Acyltransferase / physiology*
  • Substrate Specificity

Substances

  • Arabidopsis Proteins
  • DNA Primers
  • DGAT2 protein, Arabidopsis
  • Diacylglycerol O-Acyltransferase