Originally published as Genetics Published Articles Ahead of Print on December 6, 2006.

Genetics, Vol. 175, 77-91, January 2007, Copyright © 2007
doi:10.1534/genetics.106.064428

The Sensitivity of Yeast Mutants to Oleic Acid Implicates the Peroxisome and Other Processes in Membrane Function

Daniel Lockshon^*, Lauren E. Surface^*, Emily O. Kerr^*, Matt Kaeberlein^,1 and Brian K. Kennedy^*,2

^* Department of Biochemistry, University of Washington, Seattle, Washington 98195 and Department of Genome Sciences, University of Washington, Seattle, Washington 98195

² Corresponding author: Department of Biochemistry, Box 357350, University of Washington, Seattle, WA 98195.
E-mail: bkenn{at}u.washington.edu

The peroxisome, sole site of ß-oxidation in Saccharomyces cerevisiae, is known to be required for optimal growth in the presence of fatty acid. Screening of the haploid yeast deletion collection identified 130 genes, 23 encoding peroxisomal proteins, necessary for normal growth on oleic acid. Oleate slightly enhances growth of wild-type yeast and inhibits growth of all strains identified by the screen. Nonperoxisomal processes, among them chromatin modification by H2AZ, Pol II mediator function, and cell-wall-associated activities, also prevent oleate toxicity. The most oleate-inhibited strains lack Sap190, a putative adaptor for the PP2A-type protein phosphatase Sit4 (which is also required for normal growth on oleate) and Ilm1, a protein of unknown function. Palmitoleate, the other main unsaturated fatty acid of Saccharomyces, fails to inhibit growth of the sap190, sit4, and ilm1 strains. Data that suggest that oleate inhibition of the growth of a peroxisomal mutant is due to an increase in plasma membrane porosity are presented. We propose that yeast deficient in peroxisomal and other functions are sensitive to oleate perhaps because of an inability to effectively control the fatty acid composition of membrane phospholipids.

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