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http://dx.doi.org/10.14348/molcells.2016.2326

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

Toledano, Michel B. (CEA, DSV, IBITECS, SBIGEM, Laboratoire Stress Oxydant et Cancer(LSOC))
Huang, Bo (CEA, DSV, IBITECS, SBIGEM, Laboratoire Stress Oxydant et Cancer(LSOC))
Publication Information
Molecules and Cells / v.39, no.1, 2016 , pp. 31-39 More about this Journal
Abstract
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 $H_2O_2$ and as $H_2O_2$ receptors and transducers, 2-Cys Prxs have been highly instrumental to understand the biological impact of $H_2O_2$, 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 $H_2O_2$. 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 $H_2O_2$.
Keywords
chaperone; $H_2O_2$ scavenging; $H_2O_2$ signaling; peroxiredoxins;
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