Yeast cells accumulate excess endogenous palmitate in phosphatidylcholine by acyl chain remodeling involving the phospholipase B Plb1p

Autor: De Smet, C.H., Cox, R., Brouwers, J.F.H.M., de Kroon, A.I.P.M., Membrane Biochemistry and Biophysics, Strategic Infection Biology, Sub Membrane Enzymology begr. 01-06-12, Dep Biochemie en Celbiologie, Sub Membrane Biochemistry & Biophysics
Rok vydání: 2012
Předmět:
Zdroj: Biochimica et Biophysica Acta-Molecular and Cell Biology of Lipids, 1831(6), 1167. Elsevier
ISSN: 0006-3002
1388-1981
Popis: In the yeast Saccharomyces cerevisiae, the molecular species profile of the major membrane glycerophospholipid phosphatidylcholine (PC) is determined by the molecular species-selectivity of the biosynthesis routes and by acyl chain remodeling. Overexpression of the glycerol-3-phosphate acyltransferase Sct1p was recently shown to induce a strong increase in the cellular content of palmitate (C16:0). Using stable isotope labeling and mass spectrometry, the present study shows that wild type yeast overexpressing Sct1p incorporates excess C16:0 into PC via the methylation of PE, the CDP-choline route, and post-synthetic acyl chain remodeling. Overexpression of Sct1p increased the extent of remodeling of PE-derived PC, providing a novel tool to perform mechanistic studies on PC acyl chain exchange. The exchange of acyl chains occurred at both the sn-1 and sn-2 positions of the glycerol backbone of PC, and required the phospholipase B Plb1p for optimal efficiency. Sct1p-catalyzed acyl chain exchange, the acyl-CoA binding protein Acb1p, the Plb1p homologue Plb2p, and the glycerophospholipid:triacylglycerol transacylase Lro1p were not required for PC remodeling. The results indicate that PC serves as a buffer for excess cellular C16:0.
Databáze: OpenAIRE