Alkyl-dihydroxyacetone phosphate synthase and dihydroxyacetone phosphate acyltransferase form a protein complex in peroxisomes

Eur J Biochem. 1999 Apr;261(2):492-9. doi: 10.1046/j.1432-1327.1999.00295.x.

Abstract

Dihydroxyacetone phosphate (GrnP) acyltransferase and alkyl-GrnP synthase are the key enzymes involved in the biosynthesis of ether phospholipids. Both enzymes are located on the inside of the peroxisomal membrane. Here we report evidence for a direct interaction between these enzymes obtained by the use of chemical cross-linking. After cross-linking and immunoblot analysis alkyl-GrnP synthase could be detected in a 210-kDa complex which was located entirely on the lumenal side of the peroxisomal membrane. Two-dimensional SDS/PAGE demonstrated that GrnP-acyltransferase is also cross-linked in a 210-kDa complex. Co-immunoprecipitation confirmed that the two enzymes interact, in a heterotrimeric complex. Furthermore, alkyl-GrnP synthase can form a homotrimeric complex in the absence of GrnP-acyltransferase as was demonstrated by immunoblot analysis after cross-linking experiments with either GrnP-acyltransferase deficient human fibroblast homogenates or recombinant (His)6-tagged alkyl-GrnP synthase. We conclude that alkyl-GrnP synthase interacts selectively with GrnP-acyltransferase in a heterotrimeric complex and in the absence of GrnP-acyltransferase can also form a homotrimeric complex.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acyltransferases / deficiency
  • Acyltransferases / metabolism*
  • Alkyl and Aryl Transferases / metabolism*
  • Animals
  • Fibroblasts
  • Guinea Pigs
  • Humans
  • Immunoblotting
  • Liver / enzymology*
  • Microbodies / enzymology*
  • Precipitin Tests
  • Protein Conformation
  • Trypsin / metabolism

Substances

  • Acyltransferases
  • glycerone-phosphate O-acyltransferase
  • Alkyl and Aryl Transferases
  • alkylglycerone-phosphate synthase
  • Trypsin