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Lipid particles/droplets of the yeast Saccharomyces cerevisiae revisited: Lipidome meets Proteome

In the yeast Saccharomyces cerevisiae as in other eukaryotes non-polar lipids are a reservoir of energy and building blocks for membrane lipid synthesis. The yeast non-polar lipids, triacylglycerols (TG) and steryl esters (SE) are stored in so-called lipid particles/droplets (LP) as biologically ine...

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Autores principales: Grillitsch, Karlheinz, Connerth, Melanie, Köfeler, Harald, Arrey, Tabiwang N., Rietschel, Benjamin, Wagner, Brigitte, Karas, Michael, Daum, Günther
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier Pub. Co 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3229976/
https://www.ncbi.nlm.nih.gov/pubmed/21820081
http://dx.doi.org/10.1016/j.bbalip.2011.07.015
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author Grillitsch, Karlheinz
Connerth, Melanie
Köfeler, Harald
Arrey, Tabiwang N.
Rietschel, Benjamin
Wagner, Brigitte
Karas, Michael
Daum, Günther
author_facet Grillitsch, Karlheinz
Connerth, Melanie
Köfeler, Harald
Arrey, Tabiwang N.
Rietschel, Benjamin
Wagner, Brigitte
Karas, Michael
Daum, Günther
author_sort Grillitsch, Karlheinz
collection PubMed
description In the yeast Saccharomyces cerevisiae as in other eukaryotes non-polar lipids are a reservoir of energy and building blocks for membrane lipid synthesis. The yeast non-polar lipids, triacylglycerols (TG) and steryl esters (SE) are stored in so-called lipid particles/droplets (LP) as biologically inert form of fatty acids and sterols. To understand LP structure and function in more detail we investigated the molecular equipment of this compartment making use of mass spectrometric analysis of lipids (TG, SE, phospholipids) and proteins. We addressed the question whether or not lipid and protein composition of LP influence each other and performed analyses of LP from cells grown on two different carbon sources, glucose and oleate. Growth of cells on oleate caused dramatic cellular changes including accumulation of TG at the expense of SE, enhanced the amount of glycerophospholipids and strongly increased the degree of unsaturation in all lipid classes. Most interestingly, oleate as a carbon source led to adaptation of the LP proteome resulting in the appearance of several novel LP proteins. Localization of these new LP proteins was confirmed by cell fractionation. Proteomes of LP variants from cells grown on glucose or oleate, respectively, were compared and are discussed with emphasis on the different groups of proteins detected through this analysis. In summary, we demonstrate flexibility of the yeast LP lipidome and proteome and the ability of LP to adapt to environmental changes.
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spelling pubmed-32299762011-12-28 Lipid particles/droplets of the yeast Saccharomyces cerevisiae revisited: Lipidome meets Proteome Grillitsch, Karlheinz Connerth, Melanie Köfeler, Harald Arrey, Tabiwang N. Rietschel, Benjamin Wagner, Brigitte Karas, Michael Daum, Günther Biochim Biophys Acta Article In the yeast Saccharomyces cerevisiae as in other eukaryotes non-polar lipids are a reservoir of energy and building blocks for membrane lipid synthesis. The yeast non-polar lipids, triacylglycerols (TG) and steryl esters (SE) are stored in so-called lipid particles/droplets (LP) as biologically inert form of fatty acids and sterols. To understand LP structure and function in more detail we investigated the molecular equipment of this compartment making use of mass spectrometric analysis of lipids (TG, SE, phospholipids) and proteins. We addressed the question whether or not lipid and protein composition of LP influence each other and performed analyses of LP from cells grown on two different carbon sources, glucose and oleate. Growth of cells on oleate caused dramatic cellular changes including accumulation of TG at the expense of SE, enhanced the amount of glycerophospholipids and strongly increased the degree of unsaturation in all lipid classes. Most interestingly, oleate as a carbon source led to adaptation of the LP proteome resulting in the appearance of several novel LP proteins. Localization of these new LP proteins was confirmed by cell fractionation. Proteomes of LP variants from cells grown on glucose or oleate, respectively, were compared and are discussed with emphasis on the different groups of proteins detected through this analysis. In summary, we demonstrate flexibility of the yeast LP lipidome and proteome and the ability of LP to adapt to environmental changes. Elsevier Pub. Co 2011-12 /pmc/articles/PMC3229976/ /pubmed/21820081 http://dx.doi.org/10.1016/j.bbalip.2011.07.015 Text en © 2011 Elsevier B.V. https://creativecommons.org/licenses/by-nc-nd/3.0/ Open Access under CC BY-NC-ND 3.0 (https://creativecommons.org/licenses/by-nc-nd/3.0/) license
spellingShingle Article
Grillitsch, Karlheinz
Connerth, Melanie
Köfeler, Harald
Arrey, Tabiwang N.
Rietschel, Benjamin
Wagner, Brigitte
Karas, Michael
Daum, Günther
Lipid particles/droplets of the yeast Saccharomyces cerevisiae revisited: Lipidome meets Proteome
title Lipid particles/droplets of the yeast Saccharomyces cerevisiae revisited: Lipidome meets Proteome
title_full Lipid particles/droplets of the yeast Saccharomyces cerevisiae revisited: Lipidome meets Proteome
title_fullStr Lipid particles/droplets of the yeast Saccharomyces cerevisiae revisited: Lipidome meets Proteome
title_full_unstemmed Lipid particles/droplets of the yeast Saccharomyces cerevisiae revisited: Lipidome meets Proteome
title_short Lipid particles/droplets of the yeast Saccharomyces cerevisiae revisited: Lipidome meets Proteome
title_sort lipid particles/droplets of the yeast saccharomyces cerevisiae revisited: lipidome meets proteome
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3229976/
https://www.ncbi.nlm.nih.gov/pubmed/21820081
http://dx.doi.org/10.1016/j.bbalip.2011.07.015
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