Preliminary Characterization of Yor180Cp: Identification of a Novel Peroxisomal Protein of Saccharomyces cerevisiae Involved in Fatty Acid Metabolism

• Published in: Biochemical and biophysical research communications Vol. 260; no. 1; pp. 28 - 34
• Main Authors: Geisbrecht, Brian V., Schulz, Kerstin, Nau, Katja, Geraghty, Michael T., Schulz, Horst, Erdmann, Ralf, Gould, Stephen J.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 24.06.1999
• Subjects: Amino Acid Sequence; Base Sequence; Carbon-Carbon Double Bond Isomerases - metabolism; Cell Fractionation; Dodecenoyl-CoA Isomerase; Fatty Acids - metabolism; Mass Spectrometry; Membrane Proteins - chemistry; Membrane Proteins - genetics; Microbodies - metabolism; Molecular Sequence Data; plant biochemistry; plant physiology; Saccharomyces cerevisiae; Saccharomyces cerevisiae - genetics; Saccharomyces cerevisiae Proteins; Time Factors
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1006/bbrc.1999.0860

Here we report the preliminary characterization of Yor180Cp, a novel peroxisomal protein involved in fatty acid metabolism in the yeast Saccharomyces cerevisiae. A computer-based screen identified Yor180Cp as a putative peroxisomal protein, and Yor180Cp targeted GFP to peroxisomes in a PEX8-dependent manner. Yor180Cp was also detected by mass spectrometric analysis of an HPLC-separated extract of yeast peroxisomal matrix proteins. YOR180C is upregulated during growth on oleic acid, and deletion of YOR180C from the yeast genome resulted in a mild but significant growth defect on oleic acid, indicating a role for Yor180Cp in fatty acid metabolism. In addition, we observed that yor180cΔ cells fail to efficiently import the enzyme Δ3,Δ2-enoyl-CoA isomerase (Eci1p) to peroxisomes. This result suggested that Yor180Cp might associate with Eci1p in vivo, and a Yor180Cp–Eci1p interaction was detected using the yeast two-hybrid system. Potential roles for Yor180Cp in peroxisomal fatty acid metabolism are discussed.