The oligomeric conformation of peroxiredoxins links redox state to function.
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.
Barranco-Medina
Sergio
S
Biochemistry and Physiology of Plants, Bielefeld University, Bielefeld, Germany. sbarranco-medina@biochem.wustl.edu
Lázaro
Juan-José
JJ
Dietz
Karl-Josef
KJ
D001419:Bacteria / Q000201:enzymology; D020134:Catalytic Domain; D003545:Cysteine / Q000737:chemistry; D019281:Dimerization; D008954:Models, Biological; D008958:Models, Molecular; D008970:Molecular Weight; D010084:Oxidation-Reduction; D054464:Peroxiredoxins / Q000737:chemistry* / Q000378:metabolism*; D011487:Protein Conformation; D020836:Protein Structure, Quaternary
D054464:Peroxiredoxins; D003545:Cysteine