ArticleProceedings of the National Academy of Sciences of the United States of America2020
Real-time monitoring of peroxiredoxin oligomerization dynamics in living cells.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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27 citing papers in PubMed, 49 citations in OpenAlex.
- Fungal oxidative stress tolerance depends on peroxiredoxin PrxA-mediated redox signaling to mitochondrial cytochrome c peroxidase Ccp1.The Journal of biological chemistry · 2026Article
- Chimerization expands peroxiredoxin scope.Nature chemical biology · 2026Article
- Hetero-oligomerization drives structural plasticity of eukaryotic peroxiredoxins.Nature chemical biology · 2026Article
- PRDX5 and PRDX6 translocation and oligomerization in bull sperm: a response to cryopreservation-induced oxidative stress.Cell communication and signaling : CCS · 2025Article
- Redox regulation in lifespan determination.The Journal of biological chemistry · 2024Review
- The architecture of redox microdomains: Cascading gradients and peroxiredoxins' redox-oligomeric coupling integrate redox signaling and antioxidant protection.Redox biology · 2024Article
- 50 shades of oxidative stress: A state-specific cysteine redox pattern hypothesis.Redox biology · 2023Article
- Modelling the Decamerisation Cycle of PRDX1 and the Inhibition-like Effect on Its Peroxidase Activity.Antioxidants (Basel, Switzerland) · 2023Article
- Biophysical tools to study the oligomerization dynamics of Prx1-class peroxiredoxins.Biophysical reviews · 2023Review
- Disulfide-Bond-Induced Structural Frustration and Dynamic Disorder in a Peroxiredoxin from MAS NMR.Journal of the American Chemical Society · 2023Article
- Peroxiredoxin 2: An Important Element of the Antioxidant Defense of the Erythrocyte.Antioxidants (Basel, Switzerland) · 2023Review
- sGRP78 enhances selective autophagy of monomeric TLR4 to regulate myeloid cell death.Cell death & disease · 2022Article
- Defining roles of specific reactive oxygen species (ROS) in cell biology and physiology.Nature reviews. Molecular cell biology · 2022Review
- Peroxiredoxin-2 recycling is slower in denser and pediatric sickle cell red cells.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2022Article
- Reactive Oxygen Species Differentially Modulate the Metabolic and Transcriptomic Response of Endothelial Cells.Antioxidants (Basel, Switzerland) · 2022Article
- Effect of 2-Cys Peroxiredoxins Inhibition on Redox Modifications of Bull Sperm Proteins.International journal of molecular sciences · 2021Article
- Thiol-disulphide independent in-cell trapping for the identification of peroxiredoxin 2 interactors.Redox biology · 2021Article
- A comparison of Prx- and OxyR-based HThe Journal of biological chemistry · 2021Article
- 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
- Peroxiredoxins-The Underrated Actors during Virus-Induced Oxidative Stress.Antioxidants (Basel, Switzerland) · 2021Review
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4 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Peroxiredoxins are central to cellular redox homeostasis and signaling. They serve as peroxide scavengers, sensors, signal transducers, and chaperones, depending on conditions and context. Typical 2-Cys peroxiredoxins are known to switch between different oligomeric states, depending on redox state, pH, posttranslational modifications, and other factors. Quaternary states and their changes are closely connected to peroxiredoxin activity and function but so far have been studied, almost exclusively, outside the context of the living cell. Here we introduce the use of homo-FRET (Förster resonance energy transfer between identical fluorophores) fluorescence polarization to monitor dynamic changes in peroxiredoxin quaternary structure inside the crowded environment of living cells. Using the approach, we confirm peroxide- and thioredoxin-related quaternary transitions to take place in cellulo and observe that the relationship between dimer-decamer transitions and intersubunit disulfide bond formation is more complex than previously thought. Furthermore, we demonstrate the use of the approach to compare different peroxiredoxin isoforms and to identify mutations and small molecules affecting the oligomeric state inside cells. Mutagenesis experiments reveal that the dimer-decamer equilibrium is delicately balanced and can be shifted by single-atom structural changes. We show how to use this insight to improve the design of peroxiredoxin-based redox biosensors.
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