The membrane-bound O-acyltransferase Ale1 transfers an acyl moiety to newly synthesized 2-alkyl-sn-glycero-3-phosphocholine in yeast

Shiho Morisada; Yusuke Ono; Teruhisa Kodaira; Hideyuki Kishino; Ryo Ninomiya; Naoki Mori; Hidenori Watanabe; Akinori Ohta; Hiroyuki Horiuchi; Ryouichi Fukuda

doi:10.1002/1873-3468.13103

The membrane-bound O-acyltransferase Ale1 transfers an acyl moiety to newly synthesized 2-alkyl-sn-glycero-3-phosphocholine in yeast

Shiho Morisada, Yusuke Ono, Teruhisa Kodaira, Hideyuki Kishino, Ryo Ninomiya, Naoki Mori, Hidenori Watanabe, Akinori Ohta, Hiroyuki Horiuchi, Ryouichi Fukuda

Research output: Contribution to journal › Article › peer-review

3 Citations (Scopus)

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 HHPCin 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.

Original language	English
Pages (from-to)	1829-1836
Number of pages	8
Journal	FEBS Letters
Volume	592
Issue number	11
DOIs	https://doi.org/10.1002/1873-3468.13103
Publication status	Published - 2018 Jun
Externally published	Yes

Keywords

Saccharomyces cerevisiae
acyl chain
acyltransferase
phosphatidylcholine
remodeling
sn-1 position

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

Access to Document

10.1002/1873-3468.13103

Cite this

@article{39e0748bcfb5451480b298277273452b,

title = "The membrane-bound O-acyltransferase Ale1 transfers an acyl moiety to newly synthesized 2-alkyl-sn-glycero-3-phosphocholine in yeast",

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 HHPCin 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.",

keywords = "Saccharomyces cerevisiae, acyl chain, acyltransferase, phosphatidylcholine, remodeling, sn-1 position",

author = "Shiho Morisada and Yusuke Ono and Teruhisa Kodaira and Hideyuki Kishino and Ryo Ninomiya and Naoki Mori and Hidenori Watanabe and Akinori Ohta and Hiroyuki Horiuchi and Ryouichi Fukuda",

note = "Funding Information: This work was partly supported by JSPS KAKENHI Grant Number 23580104 and a grant from Noda Institute for Scientific Research. This work was done using the facilities of the Biotechnology Research Center of the University of Tokyo. Publisher Copyright: {\textcopyright} 2018 Federation of European Biochemical Societies",

year = "2018",

month = jun,

doi = "10.1002/1873-3468.13103",

language = "English",

volume = "592",

pages = "1829--1836",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "Elsevier",

number = "11",

}

TY - JOUR

T1 - The membrane-bound O-acyltransferase Ale1 transfers an acyl moiety to newly synthesized 2-alkyl-sn-glycero-3-phosphocholine in yeast

AU - Morisada, Shiho

AU - Ono, Yusuke

AU - Kodaira, Teruhisa

AU - Kishino, Hideyuki

AU - Ninomiya, Ryo

AU - Mori, Naoki

AU - Watanabe, Hidenori

AU - Ohta, Akinori

AU - Horiuchi, Hiroyuki

AU - Fukuda, Ryouichi

N1 - Funding Information: This work was partly supported by JSPS KAKENHI Grant Number 23580104 and a grant from Noda Institute for Scientific Research. This work was done using the facilities of the Biotechnology Research Center of the University of Tokyo. Publisher Copyright: © 2018 Federation of European Biochemical Societies

PY - 2018/6

Y1 - 2018/6

N2 - 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 HHPCin 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.

AB - 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 HHPCin 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.

KW - Saccharomyces cerevisiae

KW - acyl chain

KW - acyltransferase

KW - phosphatidylcholine

KW - remodeling

KW - sn-1 position

UR - http://www.scopus.com/inward/record.url?scp=85047741962&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85047741962&partnerID=8YFLogxK

U2 - 10.1002/1873-3468.13103

DO - 10.1002/1873-3468.13103

M3 - Article

C2 - 29782033

AN - SCOPUS:85047741962

SN - 0014-5793

VL - 592

SP - 1829

EP - 1836

JO - FEBS Letters

JF - FEBS Letters

IS - 11

ER -

The membrane-bound O-acyltransferase Ale1 transfers an acyl moiety to newly synthesized 2-alkyl-sn-glycero-3-phosphocholine in yeast

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this