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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
23
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pubmed:dateCreated |
2004-5-31
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pubmed:databankReference |
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
4
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pubmed:volume |
279
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
24540-51
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15037622-Amino Acid Sequence,
pubmed-meshheading:15037622-Catalysis,
pubmed-meshheading:15037622-Dimerization,
pubmed-meshheading:15037622-Dose-Response Relationship, Drug,
pubmed-meshheading:15037622-Glutathione,
pubmed-meshheading:15037622-Glutathione Disulfide,
pubmed-meshheading:15037622-Glutathione Transferase,
pubmed-meshheading:15037622-Hydrogen-Ion Concentration,
pubmed-meshheading:15037622-Kinetics,
pubmed-meshheading:15037622-Lycopersicon esculentum,
pubmed-meshheading:15037622-Models, Molecular,
pubmed-meshheading:15037622-Molecular Sequence Data,
pubmed-meshheading:15037622-Oxidants,
pubmed-meshheading:15037622-Oxidative Stress,
pubmed-meshheading:15037622-Phenotype,
pubmed-meshheading:15037622-Precipitin Tests,
pubmed-meshheading:15037622-Protein Binding,
pubmed-meshheading:15037622-Protein Structure, Secondary,
pubmed-meshheading:15037622-Proto-Oncogene Proteins,
pubmed-meshheading:15037622-Proto-Oncogene Proteins c-bcl-2,
pubmed-meshheading:15037622-Saccharomyces cerevisiae,
pubmed-meshheading:15037622-Sequence Homology, Amino Acid,
pubmed-meshheading:15037622-Substrate Specificity,
pubmed-meshheading:15037622-Two-Hybrid System Techniques,
pubmed-meshheading:15037622-bcl-2-Associated X Protein
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pubmed:year |
2004
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pubmed:articleTitle |
Differential roles of tau class glutathione S-transferases in oxidative stress.
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pubmed:affiliation |
Mediterranean Agronomic Institute of Chania, Alsyllion Agrokepiou, Chania 73100, Greece.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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