ArticleThe Journal of biological chemistry2012
Glutathione degradation by the alternative pathway (DUG pathway) in Saccharomyces cerevisiae is initiated by (Dug2p-Dug3p)2 complex, a novel glutamine amidotransferase (GATase) enzyme acting on glutathione.
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.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
19 citing papers in PubMed, 55 citations in OpenAlex.
- tRF-21LeuTAA Promotes Oxidative Stress by Altering Glutathione Metabolic Enzymes to Support Prostate Cancer Progression.Cancer research · 2025Article
- Reappraisal of the DNA phosphorothioate modification machinery: uncovering neglected functional modalities and identification of new counter-invader defense systems.Nucleic acids research · 2024Article
- Discovery of a glutathione utilization pathway in Francisella that shows functional divergence between environmental and pathogenic species.Cell host & microbe · 2023Article
- The impact of hyperglycemia upon BeWo trophoblast cell metabolic function: A multi-OMICS and functional metabolic analysis.PloS one · 2023Article
- Stress Responses Elicited by Glucose Withdrawal inJournal of fungi (Basel, Switzerland) · 2022Article
- Glutathione degradation activity of γ-glutamyl peptidase 1 manifests its dual roles in primary and secondary sulfur metabolism in Arabidopsis.The Plant journal : for cell and molecular biology · 2022Article
- Glutathione production by Saccharomyces cerevisiae: current state and perspectives.Applied microbiology and biotechnology · 2022Review
- Defective in utilizing glutathione 3,microPublication biology · 2022Article
- Response to sulfur in Schizosaccharomyces pombe.FEMS yeast research · 2021Article
- The DUG Pathway Governs Degradation of Intracellular Glutathione in Aspergillus nidulans.Applied and environmental microbiology · 2021Article
- Tn-Seq reveals hidden complexity in the utilization of host-derived glutathione in Francisella tularensis.PLoS pathogens · 2020Article
- Disruption of a C69-Family Cysteine Dipeptidase Gene Enhances Heat Shock and UV-B Tolerances inFrontiers in microbiology · 2020Article
- Article
- Communicate and Fuse: How Filamentous Fungi Establish and Maintain an Interconnected Mycelial Network.Frontiers in microbiology · 2019Review
- Article
- Functions and cellular compartmentation of the thioredoxin and glutathione pathways in yeast.Antioxidants & redox signaling · 2013Review
- Clades of γ-glutamyltransferases (GGTs) in the ascomycota and heterologous expression of Colletotrichum graminicola CgGGT1, a member of the pezizomycotina-only GGT clade.Journal of microbiology (Seoul, Korea) · 2013Article
- Genome wide association identifies novel loci involved in fungal communication.PLoS genetics · 2013Article
- Mammalian proapoptotic factor ChaC1 and its homologues function as γ-glutamyl cyclotransferases acting specifically on glutathione.EMBO reports · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The recently identified, fungi-specific alternative pathway of glutathione degradation requires the participation of three genes, DUG1, DUG2, and DUG3. Dug1p has earlier been shown to function as a Cys-Gly-specific dipeptidase. In the present study, we describe the characterization of Dug2p and Dug3p. Dug3p has a functional glutamine amidotransferase (GATase) II domain that is catalytically important for glutathione degradation as demonstrated through mutational analysis. Dug2p, which has an N-terminal WD40 and a C-terminal M20A peptidase domain, has no peptidase activity. The previously demonstrated Dug2p-Dug3p interaction was found to be mediated through the WD40 domain of Dug2p. Dug2p was also shown to be able to homodimerize, and this was mediated by its M20A peptidase domain. In vitro reconstitution assays revealed that Dug2p and Dug3p were required together for the cleavage of glutathione into glutamate and Cys-Gly. Purification through gel filtration chromatography confirmed the formation of a Dug2p-Dug3p complex. The functional complex had a molecular weight that corresponded to (Dug2p-Dug3p)(2) in addition to higher molecular weight oligomers and displayed Michaelis-Menten kinetics. (Dug2p-Dug3p)(2) had a K(m) for glutathione of 1.2 mm, suggesting a novel GATase enzyme that acted on glutathione. Dug1p activity in glutathione degradation was found to be restricted to its Cys-Gly peptidase activity, which functioned downstream of the (Dug2p-Dug3p)(2) GATase. The DUG2 and DUG3 genes, but not DUG1, were derepressed by sulfur limitation. Based on these studies and the functioning of GATases, a mechanism is proposed for the functioning of the Dug proteins in the degradation of glutathione.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.