The C-Terminal Extension of Chloroplast 2-Cys Peroxiredoxin Is Critical for Interaction with ATP

Abstract

2-Cys peroxiredoxins (2-Cys Prxs) are ubiquitous enzymes that have been implicated in peroxide-mediated signaling of markedly different processes, such as cancer and photosynthesis. A highly conserved C-terminal extension of eukaryotic homologues modulates both the overoxidation of cysteines and the formation of oligomers. Here, we reveal that the plant counterpart regulates the self-polymerization of 2-Cys Prx triggered by ATP and Mg(2+). This feature is of particular importance under oxidative stress because the interaction of ATP with 2-Cys Prx rapidly integrates nonredox chemistry of signaling pathways into a network hub governed by multiple redox transformations at cysteine residues.

Elucidation of the Binding Mechanism of Anionic Phospholipids to Antioxidant Protein Peroxiredoxin 2

“…The formation of the spherical HMW complex by plant Prx requires only Mg 2+ /ATP, and this process is not affected by its redox state. , In addition, the C-terminal region of plant Prx (residues 183–200) is important for the formation of these spherical complexes . In contrast, we previously showed that the Prx2 oligomer lacking phospholipids did not interact with Mg 2+ /ATP or Mg 2+ /ADP to form the HMW complex .…”

“…22,23 In addition, the C-terminal region of plant Prx (residues 183− 200) is important for the formation of these spherical complexes. 24 In contrast, we previously showed that the Prx2 oligomer lacking phospholipids did not interact with Mg 2+ / ATP or Mg 2+ /ADP to form the HMW complex. 19 To investigate the role of the C-terminus in the formation of the Prx2 HMW complex, we prepared a C-terminal-truncated Prx2 (Prx2 Δ181−198 ).…”