Abstract

The budding yeast ALE1 gene encodes a lysophospholipid acyltransferase (LPLAT) with broad specificity. We show that yeast LPLAT (ScLPLAT) belongs to a distinct protein family that includes human MBOAT1, MBOAT2, MBOAT4, and several closely related proteins from other eukaryotes. We further show that two plant proteins within this family, the Arabidopsis proteins AtLPLAT1 and AtLPLAT2, possess lysophospholipid acyltransferase activities similar to SeLPLAT. We propose that other members of this protein family, which we refer to as the LPLAT family, also are likely to possess LPLAT activity. Finally, we show that ScLPLAT differs from the specific lysophosphatidic acid acyltransferase that is encoded by SLC1 in that it cannot efficiently use lysophosphatidic acid produced by acylation of glycerol-3-phosphate in vitro. (C) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Keywords

Ale1; lysophospholipid acyltransferase; LPLAT; MBOAT protein; phospholipid remodeling; Slc1; yeast; arabidopsis

Published in

FEBS Letters
2008, Volume: 582, number: 2, pages: 305-309
Publisher: ELSEVIER SCIENCE BV

SLU Authors

• Ståhl, Ulf

  • Department of Plant Biology, Swedish University of Agricultural Sciences
    

• Stålberg, Kjell

  • Department of Plant Biology, Swedish University of Agricultural Sciences
    

• Stymne, Sten

  • Department of Plant Breeding, Swedish University of Agricultural Sciences
    

UKÄ Subject classification

Renewable Bioenergy Research
Agricultural Science


Publication identifier

DOI: https://doi.org/10.1016/j.febslet.2007.12.020

Permanent link to this page (URI)

https://res.slu.se/id/publ/16374