Moonlighting by different stressors: crystal structure of the chaperone species of a 2-Cys peroxiredoxin.

Fulvio Saccoccia (1) , Patrizio Di Micco (1) , Giovanna Boumis (1) , Maurizio Brunori (1) , Ilias Koutris (1) , Adriana E Miele (1) , Veronica Morea (2) , Palita Sriratana (3) , David L Williams (3) , Andrea Bellelli (1) , Francesco Angelucci (1, 4)

1 Department of Biochemical Sciences "Rossi Fanelli"
2 CNR - National Research Council of Italy | Consiglio Nazionale delle Ricerche
3 Department of Immunology/Microbiology -
4 Department of Life, Health and Environmental Sciences -

2-Cys peroxiredoxins (Prxs) play two different roles depending on the physiological status of the cell. They are thioredoxin-dependent peroxidases under low oxidative stress and ATP-independent chaperones upon exposure to high peroxide concentrations. These alternative functions have been associated with changes in the oligomerization state from low-(LMW) to high-molecular-weight (HMW) species. Here we present the structures of Schistosoma mansoni PrxI in both states: the LMW decamer and the HMW 20-mer formed by two stacked decamers. The latter is the structure of a 2-Cys Prx chaperonic form. Comparison of the structures sheds light on the mechanism by which chemical stressors, such as high H(2)O(2) concentration and acidic pH, are sensed and translated into a functional switch in this protein family. We also propose a model to account for the in vivo formation of long filaments of stacked Prx rings.

Domaines: Biochimie, Biologie Moléculaire

Fulvio Saccoccia, Patrizio Di Micco, Giovanna Boumis, Maurizio Brunori, Ilias Koutris, et al.. Moonlighting by different stressors: crystal structure of the chaperone species of a 2-Cys peroxiredoxin.. Structure, 2012, 20 (3), pp.429-39. ⟨10.1016/j.str.2012.01.004⟩. ⟨pasteur-00952065⟩