The membrane‐bound O‐acyltransferase Ale1 transfers an acyl moiety to newly synthesized 2‐alkyl‐sn‐glycero‐3‐phosphocholine in yeast. Issue 11 (28th May 2018)

• Record Type: Journal Article
• Authors: Morisada, Shiho; Ono, Yusuke; Kodaira, Teruhisa; Kishino, Hideyuki; Ninomiya, Ryo; Mori, Naoki; Watanabe, Hidenori; Ohta, Akinori; Horiuchi, Hiroyuki; Fukuda, Ryouichi
• Is Part Of: FEBS letters. Volume 592:Issue 11(2018)
• Page Start: 1829
• Page End: 1836
• Publication Date: 2018-05-28
• Subjects: acyl chain -- acyltransferase -- phosphatidylcholine -- remodeling -- Saccharomyces cerevisiae -- sn‐1 position; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1002/1873-3468.13103
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : To elucidate the mechanism of acyl chain remodeling at the sn ‐1 position of phosphatidylcholine (PC), we investigated acyl chain introduction using a newly synthesized 1‐hydroxy‐2‐hexadecyl‐ sn ‐glycero‐3‐phosphocholine (HHPC) in Saccharomyces cerevisiae . HHPC is incorporated into yeast cells and converted to a PC species containing acyl residues of 16 or 18 carbons. The efficiency of palmitoleic acid introduction to HHPC in vitro is lower in the reaction with the extract from the deletion mutant of ALE1, which encodes a membrane‐bound O ‐acyltransferase, than in that with extracts from the wild‐type strain. In addition, deletion of ALE1 causes reductions in the molecular species containing acyl residues in HHPC. These results reveal that ALE1 is involved in acyl chain transfer to the sn ‐1 position of HHPC in yeast. Abstract :