Chaperone activation and client binding of a 2-cysteine peroxiredoxin

Filipa Teixeira, Eric Tse, Helena Castro, Karl A. T. Makepeace, Ben A. Meinen, Christoph H. Borchers, Leslie B. Poole, James C. Bardwell, Ana M. Tomás, Daniel R. Southworth () and Ursula Jakob ()
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Filipa Teixeira: University of Michigan
Eric Tse: Institute for Neurodegenerative Diseases, University of California
Helena Castro: Universidade do Porto
Karl A. T. Makepeace: University of Victoria
Ben A. Meinen: University of Michigan
Christoph H. Borchers: University of Victoria
Leslie B. Poole: Wake Forest School of Medicine
James C. Bardwell: University of Michigan
Ana M. Tomás: Universidade do Porto
Daniel R. Southworth: Institute for Neurodegenerative Diseases, University of California
Ursula Jakob: University of Michigan

Nature Communications, 2019, vol. 10, issue 1, 1-14

Abstract: 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.

Date: 2019
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DOI: 10.1038/s41467-019-08565-8

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