Distinct Roles of ADP and Magnesium in the Structural Remodeling and Higher-Order Assembly of Peroxiredoxin 2

Mg disassembles PS-induced Prx2 oligomers, while ADP alone predominantly disassembles WT, and combined Mg-ADP enables captured remodeling plus HMW assembly differences.

• Why it matters: Nucleotide and cation roles in lipid-dependent Prx2 oligomer transitions are unclear, limiting understanding of how functional switching and higher-order assembly are coordinated.
• What they did: Using biochemical assays and HS-AFM, the study tested phosphatidylserine-driven oligomers of WT Prx2 and P44A/S76A mutant, then compared Mg, ADP, and Mg-ADP effects and assessed HMW assembly via Mant-ADP co-elution.
• The result: Mg disassembled both oligomers, ADP mainly disassembled WT, and Mg-ADP conditions directly showed disassembly in both proteins; WT HMW assemblies were taller and showed stronger Mant-ADP co-elution than MT.

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