ArticleThe Journal of biological chemistry2015
How pH modulates the dimer-decamer interconversion of 2-Cys peroxiredoxins from the Prx1 subfamily.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Hetero-oligomerization drives structural plasticity of eukaryotic peroxiredoxins.Nature chemical biology · 2026Article
- Role of aspartate 42 and histidine 79 in the aiPLAScientific reports · 2025Article
- Role of Aspartate 42 and Histidine 79 in the aiPLA2 activity and oligomeric status of Prdx6 at low pH.Research square · 2024Article
- Antioxidant Enzymes and Their Potential Use in Breast Cancer Treatment.International journal of molecular sciences · 2024Review
- Overoxidation and Oligomerization ofPathogens (Basel, Switzerland) · 2023Article
- Disulfide-Bond-Induced Structural Frustration and Dynamic Disorder in a Peroxiredoxin from MAS NMR.Journal of the American Chemical Society · 2023Article
- Effects of Serine or Threonine in the Active Site of Typical 2-Cys Prx on Hyperoxidation Susceptibility and on Chaperone Activity.Antioxidants (Basel, Switzerland) · 2021Article
- The cytosolic tryparedoxin peroxidase from Trypanosoma cruzi induces a pro-inflammatory Th1 immune response in a peroxidatic cysteine-dependent manner.Immunology · 2021Article
- Unique Cellular and Biochemical Features of Human Mitochondrial Peroxiredoxin 3 Establish the Molecular Basis for Its Specific Reaction with Thiostrepton.Antioxidants (Basel, Switzerland) · 2021Article
- Real-time monitoring of peroxiredoxin oligomerization dynamics in living cells.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Peroxiredoxins and Beyond; Redox Systems Regulating Lung Physiology and Disease.Antioxidants & redox signaling · 2019Review
- Quaternary structure of α-amino-β-carboxymuconate-ϵ-semialdehyde decarboxylase (ACMSD) controls its activity.The Journal of biological chemistry · 2019Article
- Chaperone activation and client binding of a 2-cysteine peroxiredoxin.Nature communications · 2019Article
- Signals Getting Crossed in the Entanglement of Redox and Phosphorylation Pathways: Phosphorylation of Peroxiredoxin Proteins Sparks Cell Signaling.Antioxidants (Basel, Switzerland) · 2019Review
- Peroxiredoxins in Cancer and Response to Radiation Therapies.Antioxidants (Basel, Switzerland) · 2019Review
- The multiple roles of peroxiredoxins in tick blood feeding.Experimental & applied acarology · 2018Review
- Peroxiredoxins and Redox Signaling in Plants.Antioxidants & redox signaling · 2018Review
- Thioredoxin system-mediated regulation of mutant Kras associated pancreatic neoplasia and cancer.Oncotarget · 2017Article
- Calcium and magnesium ions modulate the oligomeric state and function of mitochondrial 2-Cys peroxiredoxins inThe Journal of biological chemistry · 2017Article
- Catalytic Thr or Ser Residue Modulates Structural Switches in 2-Cys Peroxiredoxin by Distinct Mechanisms.Scientific reports · 2016Article
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7 authors.
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Abstract
2-Cys peroxiredoxins belonging to the Prx1 subfamily are Cys-based peroxidases that control the intracellular levels of H2O2 and seem to assume a chaperone function under oxidative stress conditions. The regulation of their peroxidase activity as well as the observed functional switch from peroxidase to chaperone involves changes in their quaternary structure. Multiple factors can modulate the oligomeric transitions of 2-Cys peroxiredoxins such as redox state, post-translational modifications, and pH. However, the molecular basis for the pH influence on the oligomeric state of these enzymes is still elusive. Herein, we solved the crystal structure of a typical 2-Cys peroxiredoxin from Leishmania in the dimeric (pH 8.5) and decameric (pH 4.4) forms, showing that conformational changes in the catalytic loop are associated with the pH-induced decamerization. Mutagenesis and biophysical studies revealed that a highly conserved histidine (His(113)) functions as a pH sensor that, at acidic conditions, becomes protonated and forms an electrostatic pair with Asp(76) from the catalytic loop, triggering the decamerization. In these 2-Cys peroxiredoxins, decamer formation is important for the catalytic efficiency and has been associated with an enhanced sensitivity to oxidative inactivation by overoxidation of the peroxidatic cysteine. In eukaryotic cells, exposure to high levels of H2O2 can trigger intracellular pH variations, suggesting that pH changes might act cooperatively with H2O2 and other oligomerization-modulator factors to regulate the structure and function of typical 2-Cys peroxiredoxins in response to oxidative stress.
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