The oligomeric conformation of peroxiredoxins links redox state to function

Abstract 

Protein–protein associations, i.e. formation of permanent or transient protein complexes, are essential for protein functionality and regulation within the cellular context. Peroxiredoxins (Prx) undergo major redox-dependent conformational changes and the dynamics are linked to functional switches. While a large number of investigations have addressed the principles and functions of Prx oligomerization, understanding of the diverse in vivo roles of this conserved redox-dependent feature of Prx is slowly emerging. The review summarizes studies on Prx oligomerization, its tight connection to the redox state, and the knowledge and hypotheses on its physiological function in the cell as peroxidase, chaperone, binding partner, enzyme activator and/or redox sensor.

Abbreviations: HMW, high molecular weight, ITC, isothermal titration microcalorimetry, LMW, low molecular weight, Prx, peroxiredoxin, SEC, size exclusion chromatography

Keywords: Protein oligomerization, Peroxiredoxin, Sulfiredoxin, Chaperone activity, Dithiothreitol