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Papers In Press, published online ahead of print December 12, 2003
J. Biol. Chem, 10.1074/jbc.M312421200
Submitted on November 12, 2003
Revised on December 12, 2003
Accepted on December 12, 2003

Alternative start sites in the S. cerevisiae GLR1 gene are responsible for mitochondrial and cytosolic isoforms of glutathione reductase

Caryn E. Outten and Valeria C. Culotta

Depts. of Environmental Health Sci. & Biochemistry, Johns Hopkins University School of Public Health, Baltimore, MD 21205-2179

Corresponding Author: vculotta{at}jhsph.edu

In order to combat oxidative damage, eukaryotic cells have evolved with numerous anti-oxidant factors that are often distributed between cytosolic and mitochondrial pools. Glutathione reductase, which regenerates the reduced form of glutathione, represents one such anti-oxidant factor, yet nothing is known regarding the partitioning of this enzyme within the cell. Using the bakers’ yeast Saccharomyces cerevisiae as a model, we provide evidence that a single gene, namely GLR1, encodes both the mitochondrial and cytosolic forms of glutathione reductase. A deletion in GLR1 drastically increases levels of oxidized glutathione in these two subcellular compartments. The GLR1 gene has two in-frame start codons that are both used as translation initiation sites. Translation from the 1st codon generates the mitochondrial form that includes a mitochondrial targeting signal, while translation from the 2nd codon produces the cytosolic form that lacks this sequence. Our results indicate that the sequence context of the two AUG codons influences the efficiency of translation initiation at each site, which in turn affects the relative levels of cytosolic and mitochondrial Glr1p. This method of subcellular distribution of glutathione reductase may be conserved in mammalian cells as well.


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