ArticleThe Journal of biological chemistry2012
Characterization of a Phanerochaete chrysosporium glutathione transferase reveals a novel structural and functional class with ligandin properties.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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19 citing papers in PubMed, 37 citations in OpenAlex.
- Detoxification of deoxynivalenol by pathogen-inducible tau-class glutathione transferases from wheat.The Journal of biological chemistry · 2025Article
- The Effect of Broccoli Glucosinolates Hydrolysis Products onInternational journal of molecular sciences · 2024Article
- Structural and Functional Characterization of One Unclassified Glutathione S-Transferase in Xenobiotic Adaptation ofInternational journal of molecular sciences · 2021Article
- Effects of Glucosinolate-Derived Isothiocyanates on Fungi: A Comprehensive Review on Direct Effects, Mechanisms, Structure-Activity Relationship Data and Possible Agricultural Applications.Journal of fungi (Basel, Switzerland) · 2021Review
- A reverse chemical ecology approach to explore wood natural durability.Microbial biotechnology · 2020Article
- Conserved white-rot enzymatic mechanism for wood decay in the Basidiomycota genus Pycnoporus.DNA research : an international journal for rapid publication of reports on genes and genomes · 2020Article
- Selective and competitive inhibition of kynurenine aminotransferase 2 by glycyrrhizic acid and its analogues.Scientific reports · 2019Article
- The structure of Trametes versicolor glutathione transferase Omega 3S bound to its conjugation product glutathionyl-phenethylthiocarbamate reveals plasticity of its active site.Protein science : a publication of the Protein Society · 2019Article
- A heterodimeric glutathioneThe Journal of biological chemistry · 2019Article
- Comparative transcriptome analysis reveals different strategies for degradation of steam-exploded sugarcane bagasse by Aspergillus niger and Trichoderma reesei.BMC genomics · 2017Article
- Structural Basis of Stereospecificity in the Bacterial Enzymatic Cleavage of β-Aryl Ether Bonds in Lignin.The Journal of biological chemistry · 2016Article
- Combination of six enzymes of a marine Novosphingobium converts the stereoisomers of β-O-4 lignin model dimers into the respective monomers.Scientific reports · 2015Article
- Characterization of glutathione transferases involved in the pathogenicity of Alternaria brassicicola.BMC microbiology · 2015Article
- Article
- Transcriptomic responses of Phanerochaete chrysosporium to oak acetonic extracts: focus on a new glutathione transferase.Applied and environmental microbiology · 2014Article
- The still mysterious roles of cysteine-containing glutathione transferases in plants.Frontiers in pharmacology · 2014Review
- Xenomic networks variability and adaptation traits in wood decaying fungi.Microbial biotechnology · 2013Review
- Diversification of fungal specific class a glutathione transferases in saprotrophic fungi.PloS one · 2013Article
- Article
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14 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glutathione S-transferases (GSTs) form a superfamily of multifunctional proteins with essential roles in cellular detoxification processes. A new fungal specific class of GST has been highlighted by genomic approaches. The biochemical and structural characterization of one isoform of this class in Phanerochaete chrysosporium revealed original properties. The three-dimensional structure showed a new dimerization mode and specific features by comparison with the canonical GST structure. An additional β-hairpin motif in the N-terminal domain prevents the formation of the regular GST dimer and acts as a lid, which closes upon glutathione binding. Moreover, this isoform is the first described GST that contains all secondary structural elements, including helix α4' in the C-terminal domain, of the presumed common ancestor of cytosolic GSTs (i.e. glutaredoxin 2). A sulfate binding site has been identified close to the glutathione binding site and allows the binding of 8-anilino-1-naphtalene sulfonic acid. Competition experiments between 8-anilino-1-naphtalene sulfonic acid, which has fluorescent properties, and various molecules showed that this GST binds glutathionylated and sulfated compounds but also wood extractive molecules, such as vanillin, chloronitrobenzoic acid, hydroxyacetophenone, catechins, and aldehydes, in the glutathione pocket. This enzyme could thus function as a classical GST through the addition of glutathione mainly to phenethyl isothiocyanate, but alternatively and in a competitive way, it could also act as a ligandin of wood extractive compounds. These new structural and functional properties lead us to propose that this GST belongs to a new class that we name GSTFuA, for fungal specific GST class A.
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