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Mol Cells. 2016 Jan;39(1):31-9. doi: 10.14348/molcells.2016.2326. Epub 2016 Jan 25.

Microbial 2-Cys Peroxiredoxins: Insights into Their Complex Physiological Roles.

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CEA, DSV, IBITECS, SBIGEM, Laboratoire Stress Oxydant et Cancer (LSOC), CEA-Saclay, 91191 Gif-sur-Yvette, France.


The peroxiredoxins (Prxs) constitute a very large and highly conserved family of thiol-based peroxidases that has been discovered only very recently. We consider here these enzymes through the angle of their discovery, and of some features of their molecular and physiological functions, focusing on complex phenotypes of the gene mutations of the 2-Cys Prxs subtype in yeast. As scavengers of the low levels of H2O2 and as H2O2 receptors and transducers, 2-Cys Prxs have been highly instrumental to understand the biological impact of H2O2, and in particular its signaling function. 2-Cys Prxs can also become potent chaperone holdases, and unveiling the in vivo relevance of this function, which is still not established, should further increase our knowledge of the biological impact and toxicity of H2O2. The diverse molecular functions of 2-Cys Prx explain the often-hard task of relating them to peroxiredoxin genes phenotypes, which underscores the pleiotropic physiological role of these enzymes and complex biologic impact of H2O2.


H2O2 scavenging; H2O2 signaling; chaperone; peroxiredoxins

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