Eukaryotic Cell
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Eukaryotic Cell, October 2006, p. 1748-1759, Vol. 5, No. 10
1535-9778/06/$08.00+0     doi:10.1128/EC.00216-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

A Peroxisomal Glutathione Transferase of Saccharomyces cerevisiae Is Functionally Related to Sulfur Amino Acid Metabolism{triangledown}

Lina Barreto,1 Ana Garcerá,1 Kristina Jansson,2 Per Sunnerhagen,2 and Enrique Herrero1*

Departament de Ciències Mèdiques Bàsiques, Facultat de Medicina, Universitat de Lleida, 25008 Lleida, Spain,1 Department of Cell and Molecular Biology, Lundberg Laboratory, Göteborg University, S-405 30 Göteborg, Sweden2

Received 11 July 2006/ Accepted 8 August 2006

Saccharomyces cerevisiae cells contain three omega-class glutathione transferases with glutaredoxin activity (Gto1, Gto2, and Gto3), in addition to two glutathione transferases (Gtt1 and Gtt2) not classifiable into standard classes. Gto1 is located at the peroxisomes, where it is targeted through a PTS1-type sequence, whereas Gto2 and Gto3 are in the cytosol. Among the GTO genes, GTO2 shows the strongest induction of expression by agents such as diamide, 1-chloro-2,4-dinitrobenzene, tert-butyl hydroperoxide or cadmium, in a manner that is dependent on transcriptional factors Yap1 and/or Msn2/4. Diamide and 1-chloro-2,4-dinitrobenzene (causing depletion of reduced glutathione) also induce expression of GTO1 over basal levels. Phenotypic analyses with single and multiple mutants in the S. cerevisiae glutathione transferase genes show that, in the absence of Gto1 and the two Gtt proteins, cells display increased sensitivity to cadmium. A gto1-null mutant also shows growth defects on oleic acid-based medium, which is indicative of abnormal peroxisomal functions, and altered expression of genes related to sulfur amino acid metabolism. As a consequence, growth of the gto1 mutant is delayed in growth medium without lysine, serine, or threonine, and the mutant cells have low levels of reduced glutathione. The role of Gto1 at the S. cerevisiae peroxisomes could be related to the redox regulation of the Str3 cystathionine ß-lyase protein. This protein is also located at the peroxisomes in S. cerevisiae, where it is involved in transulfuration of cysteine into homocysteine, and requires a conserved cysteine residue for its biological activity.

* Corresponding author. Mailing address: Departament de Ciències Mèdiques Bàsiques, Facultat de Medicina, Universitat de Lleida, Montserrat Roig 2, 25008 Lleida, Spain. Phone: (34) 973-702409. Fax: (34) 973-702426. E-mail: enric.herrero{at}cmb.udl.es.

{triangledown} Published ahead of print on 25 August 2006.

Eukaryotic Cell, October 2006, p. 1748-1759, Vol. 5, No. 10
1535-9778/06/$08.00+0     doi:10.1128/EC.00216-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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