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Submitted on September 8, 2004
Revised on February 11, 2005
Accepted on February 16, 2005

The spatial organization of lipid synthesis in the yeast Saccharomyces cerevisiae derived from large-scale green fluorescent protein tagging and high-resolution microscopy

Klaus Natter, Peter Leitner, Alexander Faschinger, Heimo Wolinski, Stephen McCraith, Stanley Fields, and Sepp D. Kohlwein

Institute of Molecular Biosciences, University of Graz, Graz A8010

Corresponding Author: sepp.kohlwein{at}uni-graz.at

The localization pattern of proteins involved in lipid metabolism in the yeast Saccharomyces cerevisiae was determined using C-terminal green fluorescent protein (GFP) tagging and high resolution confocal laser scanning microscopy. A list of 493 candidate proteins (~ 9 % of the yeast proteome) was assembled based on proteins of known function in lipid metabolism, their interacting proteins, proteins defined by genetic interactions, and regulatory factors acting on selected genes or proteins. Overall, 400 (81%) transformants yielded a positive GFP signal and of these, 248 (62% of the 400) displayed a localization pattern which was not cytosolic. Observations for 52% of the proteins (209 clones) were consistent with published data derived from cell fractionation or other large-scale localization approaches. However, high-resolution microscopy provided additional information for 61 proteins, indicating localization to multiple subcellular locations, and localization patterns for 43 proteins were determined for the first time. The majority of tagged proteins localized to the endoplasmic reticulum (92), but mitochondria (27), peroxisomes (17), lipid droplets (23) and vesicles (53) also contribute substantially to lipid metabolism. We assembled enzyme localization patterns for phospholipid, sterol and sphingolipid biosynthetic pathways and propose a model, based on enzyme localization, for concerted regulation of sterol, sphingolipid and neutral lipid metabolism that involves shuttling of key enzymes between ER, lipid droplets, vesicles, or Golgi.


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