Identification and characterization of the major lysophosphatidylethanolamine acyltransferase in Saccharomyces cerevisiae

Wayne R. Riekhof, James Wu, Jennifer L. Jones, Dennis R. Voelker

Research output: Contribution to journalArticle

110 Citations (Scopus)

Abstract

We recently demonstrated that yeast actively import lysophosphatidylethanolamine (lyso-PtdEtn) through the action of plasma membrane P-type ATPases and rapidly acylate it to form PtdEtn. The predominant lyso-PtdEtn acyltransferase (LPEAT) activity present in cellular extracts is acyl-CoA dependent, but the identity of the gene encoding this activity was unknown. We now demonstrate that a previously uncharacterized open reading frame, YOR175C, encodes the major acyl-CoA-dependent LPEAT activity in yeast and henceforth refer to it as ALE1 (acyltransferase for lyso-PtdEtn). Ale1p is an integral membrane protein and is highly enriched in the mitochondria-associated endoplasmic reticulum membrane. It is a member of the membrane-bound O-acyltransferase family and possesses a dibasic motif at its C terminus that is likely responsible for Golgi retrieval and retention in the endoplasmic reticulum. An ale1Δ strain retains only trace amounts of acyl-CoA-dependent LPEAT activity, and strains lacking the capacity for PtdEtn synthesis via the phosphatidylserine decarboxylase and Kennedy pathways show a stringent requirement for both exogenous lyso-PtdEtn and a functional ALE1 gene for viability. Ale1p catalytic activity has a pH optimum between pH 7 and 7.5 and a strong preference for unsaturated acyl-CoA substrates.

Original languageEnglish (US)
Pages (from-to)28344-28352
Number of pages9
JournalJournal of Biological Chemistry
Volume282
Issue number39
DOIs
StatePublished - Sep 28 2007

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Acyl Coenzyme A
Acyltransferases
Yeast
Saccharomyces cerevisiae
Endoplasmic Reticulum
Yeasts
Membranes
Mitochondria
Gene encoding
Cell membranes
Open Reading Frames
Genes
Adenosine Triphosphatases
Catalyst activity
Membrane Proteins
Cell Membrane
lysophosphatidylethanolamine acyltransferase
Substrates
lysophosphatidylethanolamine

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Identification and characterization of the major lysophosphatidylethanolamine acyltransferase in Saccharomyces cerevisiae. / Riekhof, Wayne R.; Wu, James; Jones, Jennifer L.; Voelker, Dennis R.

In: Journal of Biological Chemistry, Vol. 282, No. 39, 28.09.2007, p. 28344-28352.

Research output: Contribution to journalArticle

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