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Chaperone activation and client binding of a 2-cysteine peroxiredoxin.

  • Author(s): Teixeira, Filipa;
  • Tse, Eric;
  • Castro, Helena;
  • Makepeace, Karl AT;
  • Meinen, Ben A;
  • Borchers, Christoph H;
  • Poole, Leslie B;
  • Bardwell, James C;
  • Tomás, Ana M;
  • Southworth, Daniel R;
  • Jakob, Ursula
  • et al.
Abstract

Many 2-Cys-peroxiredoxins (2-Cys-Prxs) are dual-function proteins, either acting as peroxidases under non-stress conditions or as chaperones during stress. The mechanism by which 2-Cys-Prxs switch functions remains to be defined. Our work focuses on Leishmania infantum mitochondrial 2-Cys-Prx, whose reduced, decameric subpopulation adopts chaperone function during heat shock, an activity that facilitates the transition from insects to warm-blooded host environments. Here, we have solved the cryo-EM structure of mTXNPx in complex with a thermally unfolded client protein, and revealed that the flexible N-termini of mTXNPx form a well-resolved central belt that contacts and encapsulates the unstructured client protein in the center of the decamer ring. In vivo and in vitro cross-linking studies provide further support for these interactions, and demonstrate that mTXNPx decamers undergo temperature-dependent structural rearrangements specifically at the dimer-dimer interfaces. These structural changes appear crucial for exposing chaperone-client binding sites that are buried in the peroxidase-active protein.

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