SGD Paper 
Porras P, et al. (2006) One single in-frame AUG codon is responsible for a diversity of subcellular localizations of glutaredoxin 2 in Saccharomyces cerevisiae. J Biol Chem 281(24):16551-62
Abstract: Glutaredoxins belong to a family of small proteins with glutathione dependent disulfide oxidoreductase activity involved in cellular defence against oxidative stress. The product of the yeast GRX2 gene is a protein that is localized both in the cytosol and mitochondria. To throw light onto the mechanism responsible for the dual subcellular distribution of Grx2 we analysed mutant constructs containing different targeting information. By altering amino acid residues around the two in-frame translation initiation start sites (TSS) of the GRX2 gene, we could demonstrate that the cytosolic isoform of Grx2 was synthesized from the second AUG, lacking an amino-terminal extension. Translation from the first AUG resulted in a long isoform carrying a mitochondrial targeting presequence. The mitochondrial targeting properties of the presequence and the influence of the mature part of Grx2 were analysed by the characterization of the import kinetics of specific fusion proteins. Import of the mitochondrial isoform is relatively inefficient and results in the accumulation of a substantial amount of unprocessed form in the mitochondrial outer membrane. Substitution of Met35, the second TSS, to Val resulted in an exclusive targeting to the mitochondrial matrix. Our results show that a plethora of Grx2 subcellular localizations could spread its antioxidant functions all over the cell, but one single A to G mutation converts Grx2 into a typical protein of the mitochondrial matrix.
| Status: Published | Type: Journal Article | PubMed ID: 16606613 |
Topics addressed in this paper
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| Topics | Genes linked to topics |
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| GRX2 | |
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