Hetero-oligomerization drives structural plasticity of eukaryotic peroxiredoxins - PubMed
a day ago
- #redox biology
- #peroxiredoxins
- #hetero-oligomerization
- Peroxiredoxins (Prx1/AhpC-type) are thiol peroxidases with roles in detoxifying peroxides, redox signaling, and chaperone activity.
- Eukaryotic peroxiredoxins can form hetero-oligomers (heterodimers and heterodecamers) with diverse subunit stoichiometries, contrary to the previous belief of exclusive homo-oligomerization.
- Oxidative stress in Saccharomyces cerevisiae induces Tsa1-Tsa2 heterodecamer formation, where even substoichiometric Tsa2 stabilizes the decameric state.
- Hetero-oligomerization is conserved across eukaryotes, including humans, plants, and Leishmania peroxiredoxins.
- The findings redefine peroxiredoxin structural plasticity, impacting redox biology, stress responses, and cellular adaptation.