ArticleThe Biochemical journal2006
Saccharomyces cerevisiae cells have three Omega class glutathione S-transferases acting as 1-Cys thiol transferases.
Article in The Biochemical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 96 citations in OpenAlex.
- The yeast peroxisomal proteome at absolute quantitative scale.Histochemistry and cell biology · 2026Article
- Testing the Capability of Embedding-Based Alignments on the GST Superfamily Classification: The Role of Protein Length.Molecules (Basel, Switzerland) · 2024Article
- Altered S-AdenosylMethionine availability impacts dNTP pools in Saccharomyces cerevisiae.Yeast (Chichester, England) · 2024Article
- β-Dicarbonyls Facilitate Engineered Microbial Bromoform Biosynthesis.ACS synthetic biology · 2024Article
- Profiling the compendium of changes in Saccharomyces cerevisiae due to mutations that alter availability of the main methyl donor S-Adenosylmethionine.G3 (Bethesda, Md.) · 2024Article
- Genome and Transcriptome Analysis to Elucidate the Biocontrol Mechanism ofMicroorganisms · 2023Article
- mRNA Sequencing Reveals Upregulation of Glutathione S-Transferase Genes duringMicroorganisms · 2023Article
- Biochemical and Structural Insights on the Poplar Tau Glutathione Transferase GSTU19 and 20 Paralogs Binding Flavonoids.Frontiers in molecular biosciences · 2022Article
- A Comprehensive Insight into Fungal Enzymes: Structure, Classification, and Their Role in Mankind's Challenges.Journal of fungi (Basel, Switzerland) · 2021Review
- Screening and Genetic Network Analysis of Genes Involved in Freezing and Thawing Resistance inGenes · 2021Article
- Yeast glutaredoxin, GRX4, functions as a glutathione S-transferase required for red ade pigment formation inJournal of biosciences · 2020Article
- Characterization of Xi-class mycothiol S-transferase from Corynebacterium glutamicum and its protective effects in oxidative stress.Microbial cell factories · 2019Article
- Structural Characterization of the Xi Class Glutathione Transferase From the Haloalkaliphilic ArchaeonFrontiers in microbiology · 2019Article
- Identification, Expression, and Regulation of an Omega Class Glutathione S-transferase inFrontiers in physiology · 2018Article
- Omega Class Glutathione S-Transferase: Antioxidant Enzyme in Pathogenesis of Neurodegenerative Diseases.Oxidative medicine and cellular longevity · 2017Review
- Crystal Structure of Saccharomyces cerevisiae ECM4, a Xi-Class Glutathione Transferase that Reacts with Glutathionyl-(hydro)quinones.PloS one · 2016Article
- Cth2 Protein Mediates Early Adaptation of Yeast Cells to Oxidative Stress Conditions.PloS one · 2016Article
- Identification of Saccharomyces cerevisiae Genes Whose Deletion Causes Synthetic Effects in Cells with Reduced Levels of the Nuclear Pif1 DNA Helicase.G3 (Bethesda, Md.) · 2015Article
- Characterization of glutathione transferases involved in the pathogenicity of Alternaria brassicicola.BMC microbiology · 2015Article
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5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Saccharomyces cerevisiae genome encodes three proteins that display similarities with human GSTOs (Omega class glutathione S-transferases) hGSTO1-1 and hGSTO2-2. The three yeast proteins have been named Gto1, Gto2 and Gto3, and their purified recombinant forms are active as thiol transferases (glutaredoxins) against HED (beta-hydroxyethyl disulphide), as dehydroascorbate reductases and as dimethylarsinic acid reductases, while they are not active against the standard GST substrate CDNB (1-chloro-2,4-dinitrobenzene). Their glutaredoxin activity is also detectable in yeast cell extracts. The enzyme activity characteristics of the Gto proteins contrast with those of another yeast GST, Gtt1. The latter is active against CDNB and also displays glutathione peroxidase activity against organic hydroperoxides such as cumene hydroperoxide, but is not active as a thiol transferase. Analysis of point mutants derived from wild-type Gto2 indicates that, among the three cysteine residues of the molecule, only the residue at position 46 is required for the glutaredoxin activity. This indicates that the thiol transferase acts through a monothiol mechanism. Replacing the active site of the yeast monothiol glutaredoxin Grx5 with the proposed Gto2 active site containing Cys46 allows Grx5 to retain some activity against HED. Therefore the residues adjacent to the respective active cysteine residues in Gto2 and Grx5 are important determinants for the thiol transferase activity against small disulphide-containing molecules.
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