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The membrane‐bound O ‐acyltransferase Ale1 transfers an acyl moiety to newly synthesized 2‐alkyl‐ sn ‐glycero‐3‐phosphocholine in yeast
Author(s) -
Morisada Shiho,
Ono Yusuke,
Kodaira Teruhisa,
Kishino Hideyuki,
Ninomiya Ryo,
Mori Naoki,
Watanabe Hidenori,
Ohta Akinori,
Horiuchi Hiroyuki,
Fukuda Ryouichi
Publication year - 2018
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13103
Subject(s) - moiety , alkyl , acyltransferase , phosphocholine , chemistry , yeast , membrane , stereochemistry , biochemistry , medicinal chemistry , organic chemistry , phospholipid , phosphatidylcholine , enzyme
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 ALE 1 , which encodes a membrane‐bound O ‐acyltransferase, than in that with extracts from the wild‐type strain. In addition, deletion of ALE 1 causes reductions in the molecular species containing acyl residues in HHPC . These results reveal that ALE 1 is involved in acyl chain transfer to the sn ‐1 position of HHPC in yeast.