The membrane-bound O-acyltransferase Ale1 transfers an acyl moiety to newly synthesized 2-alkyl-sn-glycero-3-phosphocholine in yeast
| Autor: | Hideyuki Kishino, Hidenori Watanabe, Shiho Morisada, Yusuke Ono, Hiroyuki Horiuchi, Naoki Mori, Teruhisa Kodaira, Ryo Ninomiya, Akinori Ohta, Ryouichi Fukuda |
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| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Saccharomyces cerevisiae Proteins Stereochemistry Saccharomyces cerevisiae Biophysics Biochemistry 03 medical and health sciences chemistry.chemical_compound Structural Biology Phosphatidylcholine Genetics Moiety Palmitoleic acid Molecular Biology Alkyl Phosphocholine chemistry.chemical_classification 030102 biochemistry & molecular biology biology Chemistry 1-Acylglycerophosphocholine O-Acyltransferase Cell Biology biology.organism_classification Yeast 030104 developmental biology Acyltransferase Phosphatidylcholines lipids (amino acids peptides and proteins) Gene Deletion |
| Zdroj: | FEBS letters. 592(11) |
| ISSN: | 1873-3468 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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