Peroxiredoxins: a less studied component of hydrogen peroxide detoxification in photosynthetic organisms

Abstract

Peroxiredoxins (Prx) are ubiquitous thiol-dependent peroxidases capable of reducing a broad range of toxic peroxides and peroxinitrites. A cysteinyl residue of peroxiredoxins reacts with the peroxides as primary catalytic center and oxidizes to sulfenic acid. The regeneration of the reduced form of Prx is required as a next step to allow its entry into next catalytic cycle. Several proteins, such as thioredoxin, glutaredoxin, cyclophilin, among others, are known to facilitate the regeneration of the reduced (catalytically active) form of Prx in plants. Based on the cysteine residues conserved in the deduced amino acid sequence and their catalytic mechanisms, four groups of peroxiredoxins have been distinguished in plants, namely, 1-Cys Prx, 2-Cys Prx, Type II Prx and Prx Q. Peroxiredoxins are known to play an important role in combating the reactive oxygen species generated at the level of electron transport activities in the plant exposed to different types of biotic and abiotic stresses. In addition to their role in antioxidant defense mechanisms in plants, they also modulate redox signaling during development and adaptation. Besides these general properties, peroxiredoxins have been shown to protect DNA from damage in vitro and in vivo. They also regulate metabolism in thylakoids and mitochondria. The present review summarizes the most updated information on the structure and catalysis of Prx and their functional importance in plant metabolism.

Phytotoxic metabolites from Neofusicoccum parvum, a pathogen of Botryosphaeria dieback of grapevine

“…Thiols play a major role in maintaining the redox state of cells (homeostasis) and in the activity of an important part of enzymes that catalyse redox reactions, similarly to enzymes implicated in an antioxidant system. Two proteomicbased studies described the responses in woody tissues from fieldgrown grapevines (Magnin-Robert et al, 2014;Spagnolo et al, 2014b) and described the differential perturbations (at the protein and transcript levels) of the detoxification systems: glutathione-S-transferase (Cummins et al, 2011), peroxiredoxins (Tripathi et al, 2009), and epoxide hydrolase (Mowbray et al, 2006). These responses may indicate the presence and the activity of these toxins in woody tissues, leading to disruption of antioxidant systems.…”

Effect of Plant Growth Stimulants on Alfalfa Response to Salt Stress

“…Potassium plays a key role in plants through the activation of enzymes by stabilizing the pH between 7 and 8 and changing the conformation of enzymes by binding to their surfaces [73]. Tripathi et al [74] reported that proteins, such as thioredoxin, glutaredoxin, and cyclophilin, facilitated the regeneration of the catalytically active form of peroxiredoxins that played an important role in reducing the formation of reactive oxygen species in plants under biotic and abiotic stress.…”

Cytosolic and Chloroplastic DHARs Cooperate in Oxidative Stress-Driven Activation of the Salicylic Acid Pathway

“…Glutathione accumulation, largely in the form of GSSG, has long been known to occur in response to increased intracellular H 2 O 2 (Smith et al, 1984;May and Leaver, 1993), but the extent to which such effects are DHA dependent is not known (Rahantaniaina et al, 2013). Other systems, such as GSTs or glutaredoxinperoxiredoxins, may couple ROS removal to GSH oxidation (Rouhier et al, 2002;Dixon et al, 2009;Tripathi et al, 2009). Although the ascorbate-glutathione pathway has become accepted as an important route for ROS metabolism in plants, the extent to which the two antioxidants interact in vivo remains to be established (Noctor et al, 2000;Foyer and Noctor, 2011).…”

“…When produced inside the cell, the accumulation of ROS is limited by their reactivity with multiple antioxidant systems found in plants. In the aqueous phase, such systems include catalases, ascorbate, glutathione, and peroxiredoxins (Rouhier et al, 2002;Tripathi et al, 2009;Mhamdi et al, 2010b;Foyer and Noctor, 2011;Smirnoff, 2011;Awad et al, 2015). At least some of the signaling effects of ROS may involve secondary changes in such antioxidative systems (Han et al, 2013a).…”