A mutation in the yeast mitochondrial ribosomal protein Rml2p is associated with a defect in catalase gene expression.

Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, Texas 78712, USA.
Yeast strains containing a new temperature-sensitive allele of the RML2 gene, encoding a component of the large subunit of the mitochondrial ribosome, display normal growth on acetate, slowed growth on glycerol and an inability to grow on oleic acid. These cells, denoted rml2(fat21), have an apparent inability to induce peroxisomal function, as evidenced by a deficiency in oleic acid induction of beta-oxidation. However, the oleic acid regulation of genes encoding core enzymes of peroxisomal beta-oxidation is normal. In contrast, up-regulation of CTA1 (catalase) mRNA expression and enzyme activity is interrupted. Upon comparison of the induction requirements of catalase and the genes of beta-oxidation, we hypothesized that the rml2(fat21) mutation alters the activity of the transcription factor Adr1p. In support of this hypothesis, over-expression of ADR1 in rml2(fat21) cells restores CTA1 induction. Several assays of mitochondria from rml2(fat21) strains suggest normal mitochondrial function. Thus, the modulation of Adr1p-associated gene regulation is not due to overt mitochondrial dysfunction.
Mesh Terms:
Alleles, Blotting, Northern, Catalase, DNA-Binding Proteins, Electron Transport Complex IV, Gene Expression Regulation, Enzymologic, Gene Expression Regulation, Fungal, Glycerol, Intracellular Membranes, Membrane Potentials, Mitochondria, Mitochondrial Proteins, Mutation, Oleic Acid, Peroxisomes, Phenotype, RNA, Fungal, Ribosomal Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Time Factors, Transcription Factors, Up-Regulation
Mol. Cell Biol. Res. Commun. Sep. 01, 2001; 4(5);299-306 [PUBMED:11529680]
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