Hetero-oligomerization drives structural plasticity of eukaryotic peroxiredoxins
Jannik Zimmermann1, Lukas Lang2, Julia Malo Pueyo3,4,5
1Institute of Biochemistry, Center for Human and Molecular Biology (ZHMB), Saarland University, Saarbrücken, Germany.
Nature Chemical Biology
|March 11, 2026
Summary
Peroxiredoxins (Prx1/AhpC) can form functional hetero-oligomers, not just homo-oligomers, across eukaryotes. This discovery challenges existing models and reveals new insights into redox biology and cellular adaptation.
Area of Science:
- Redox Biology
- Molecular Cell Biology
- Biochemistry
Background:
- Peroxiredoxins (Prx1/AhpC) are crucial thiol peroxidases involved in peroxide detoxification, redox signaling, and chaperone functions.
- Eukaryotic cells contain multiple Prx1/AhpC isoforms within the same compartment, previously assumed to form only homo-oligomeric complexes.
Purpose of the Study:
- To investigate the potential for hetero-oligomerization among Prx1/AhpC-type peroxiredoxins.
- To determine if hetero-oligomerization is a conserved and functionally significant property across different eukaryotic organisms.
Main Methods:
- Biochemical reconstitution assays
- Native mass photometry
- Electron microscopy
- Live-cell assays
Main Results:
- Demonstrated the formation of heterodimers and heterodecamers with varied subunit stoichiometries for peroxiredoxin pairs from different eukaryotic kingdoms.
- Observed that oxidative stress induces Tsa1-Tsa2 heterodecamerization in Saccharomyces cerevisiae, with minimal Tsa2 stabilizing the decamer.
- Confirmed functional hetero-oligomer formation in human, plant, and Leishmania peroxiredoxins.
Conclusions:
- Hetero-oligomerization is a conserved and functionally relevant property of Prx1/AhpC-type peroxiredoxins, challenging the established paradigm of homo-oligomerization.
- These findings expand our understanding of peroxiredoxin structural plasticity and have broad implications for redox biology, stress responses, and cellular adaptation.
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