ArticleBiochemistry2012
Conservation of oxidative protein stabilization in an insect homologue of parkinsonism-associated protein DJ-1.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 39 citations in OpenAlex.
- Glyoxalase activities of Parkinson's disease relevant protein DJ-1/PARK7: Past discoveries and future perspectives.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2026Review
- Genomic identification, characterization, and stress-induced expression profiling of glyoxalase and D-lactate dehydrogenase gene families in Capsicum annuum.BMC plant biology · 2024Article
- Resolving DJ-1 Glyoxalase Catalysis Using Mix-and-Inject Serial Crystallography at a Synchrotron.bioRxiv : the preprint server for biology · 2024Article
- Article
- Self-oxidation of cysteine to sulfinic acid in an engineered T67C myoglobin: structure and reactivity.RSC chemical biology · 2023Article
- Review
- Persulfidation of DJ-1: Mechanism and Consequences.Biomolecules · 2022Article
- DJ-1 is not a deglycase and makes a modest contribution to cellular defense against methylglyoxal damage in neurons.Journal of neurochemistry · 2022Article
- cDNA Cloning and Partial Characterization of theAntioxidants (Basel, Switzerland) · 2021Article
- DJ-1 in Parkinson's Disease: Clinical Insights and Therapeutic Perspectives.Journal of clinical medicine · 2019Review
- The effect of cysteine oxidation on DJ-1 cytoprotective function in human alveolar type II cells.Cell death & disease · 2019Article
- Bifunctional Chloroplastic DJ-1B fromAntioxidants (Basel, Switzerland) · 2019Article
- Article
- Epigallocatechin-3-Gallate Protects and Prevents Paraquat-Induced Oxidative Stress and Neurodegeneration in Knockdown dj-1-β Drosophila melanogaster.Neurotoxicity research · 2018Article
- Genome-Wide Identification of Glyoxalase Genes inFrontiers in plant science · 2017Article
- Presence of unique glyoxalase III proteins in plants indicates the existence of shorter route for methylglyoxal detoxification.Scientific reports · 2016Article
- Transient sampling of aggregation-prone conformations causes pathogenic instability of a parkinsonian mutant of DJ-1 at physiological temperature.Protein science : a publication of the Protein Society · 2015Article
- A role for the Parkinson's disease protein DJ-1 as a chaperone and antioxidant in the anhydrobiotic nematode Panagrolaimus superbus.Cell stress & chaperones · 2015Article
- Use of cysteine-reactive cross-linkers to probe conformational flexibility of human DJ-1 demonstrates that Glu18 mutations are dimers.Journal of neurochemistry · 2014Article
- DJ-1-dependent regulation of oxidative stress in the retinal pigment epithelium (RPE).PloS one · 2013Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
DJ-1 is a conserved, disease-associated protein that protects against oxidative stress and mitochondrial damage in multiple organisms. Human DJ-1 contains a functionally essential cysteine residue (Cys106) whose oxidation is important for regulating protein function by an unknown mechanism. This residue is well-conserved in other DJ-1 homologues, including two (DJ-1α and DJ-1β) in Drosophila melanogaster. Because D. melanogaster is a powerful model system for studying DJ-1 function, we have determined the crystal structure and impact of cysteine oxidation on Drosophila DJ-1β. The structure of D. melanogaster DJ-1β is similar to that of human DJ-1, although two important residues in the human protein, Met26 and His126, are not conserved in DJ-1β. His126 in human DJ-1 is substituted with a tyrosine in DJ-1β, and this residue is not able to compose a putative catalytic dyad with Cys106 that was proposed to be important in the human protein. The reactive cysteine in DJ-1 is oxidized readily to the cysteine-sulfinic acid in both flies and humans, and this may regulate the cytoprotective function of the protein. We show that the oxidation of this conserved cysteine residue to its sulfinate form (Cys-SO(2)(-)) results in considerable thermal stabilization of both Drosophila DJ-1β and human DJ-1. Therefore, protein stabilization is one potential mechanism by which cysteine oxidation may regulate DJ-1 function in vivo. More generally, most close DJ-1 homologues are likely stabilized by cysteine-sulfinic acid formation but destabilized by further oxidation, suggesting that they are biphasically regulated by oxidative modification.
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