Differential roles of tau class glutathione S-transferases in oxidative stress
Research output: Contribution to journal › Journal article › Research › peer-review
The plant glutathione S-transferase BI-GST has been identified as a potent inhibitor of Bax lethality in yeast, a phenotype associated with oxidative stress and disruption of mitochondrial functions. Screening of a tomato two-hybrid library for BI-GST interacting proteins identified five homologous Tau class GSTs, which readily form heterodimers between them and BI-GST. All six LeGSTUs were found to be able to protect yeast cells from prooxidant-induced cell death. The efficiency of each LeGSTU was prooxidant-specific, indicating a different role for each LeGSTU in the oxidative stress-response mechanism. The prooxidant protective effect of all six proteins was suppressed in the absence of YAP1, a transcription factor that regulates hydroperoxide homeostasis in Saccharomyces cerevisiae, suggesting a role for the LeGSTUs in the context of the YAP1-dependent stress-responsive machinery. The different LeGSTUs exhibited varied substrate specificity and showed activity against oxidative stress by-products, indicating that their prooxidant protective function is likely related to the minimization of oxidative damage. Taken together, these results indicate that Tau class GSTs participate in a broad network of catalytic and regulatory functions involved in the oxidative stress response.
Original language | English |
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Journal | The Journal of Biological Chemistry |
Volume | 279 |
Issue number | 23 |
Pages (from-to) | 24540-51 |
Number of pages | 12 |
ISSN | 0021-9258 |
DOIs | |
Publication status | Published - 4 Jun 2004 |
- Amino Acid Sequence, Catalysis, Dimerization, Dose-Response Relationship, Drug, Glutathione, Glutathione Disulfide, Glutathione Transferase, Hydrogen-Ion Concentration, Kinetics, Lycopersicon esculentum, Models, Molecular, Molecular Sequence Data, Oxidants, Oxidative Stress, Phenotype, Precipitin Tests, Protein Binding, Protein Structure, Secondary, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-bcl-2, Saccharomyces cerevisiae, Sequence Homology, Amino Acid, Substrate Specificity, Two-Hybrid System Techniques, bcl-2-Associated X Protein
Research areas
ID: 159085347