Peroxiredoxins in Plants and Cyanobacteria

Abstract

Peroxiredoxins (Prx) are central elements of the antioxidant defense system and the dithiol-disulfide redox regulatory network of the plant and cyanobacterial cell. They employ a thiol-based catalytic mechanism to reduce H 2 O 2 , alkylhydroperoxide, and peroxinitrite. In plants and cyanobacteria, there exist 2-CysPrx, 1-CysPrx, PrxQ, and type II Prx. Higher plants typically contain at least one plastid 2-CysPrx, one nucleo-cytoplasmic 1-CysPrx, one chloroplast PrxQ, and one each of cytosolic, mitochondrial, and plastidic type II Prx. Cyanobacteria express variable sets of three or more Prxs. The catalytic cycle consists of three steps: (i) peroxidative reduction, (ii) resolving step, and (iii) regeneration using diverse electron donors such as thioredoxins, glutaredoxins, cyclophilins, glutathione, and ascorbic acid. Prx proteins undergo major conformational changes in dependence of their redox state. Thus, they not only modulate cellular reactive oxygen species-and reactive nitrogen speciesdependent signaling, but depending on the Prx type they sense the redox state, transmit redox information to binding partners, and function as chaperone. They serve in context of photosynthesis and respiration, but also in metabolism and development of all tissues, for example, in nodules as well as during seed and fruit development. The article surveys the current literature and attempts a mostly comprehensive coverage of present day knowledge and concepts on Prx mechanism, regulation, and function and thus on the whole Prx systems in plants. Antioxid. Redox Signal. 15, 1129-1159

Glutathione – linking cell proliferation to oxidative stress

“…However, this is not the case for 2-cys peroxiredoxins, in which the sulfinic form of the catalytic cysteine can be reduced to the sulfenic acid form by proteins such as sulfiredoxin or sestrin (14)(15)(16).…”

Existing and emerging cyanocidal compounds: new perspectives for cyanobacterial bloom mitigation

“…In defence against toxic Aquat Ecol (2016) 50:443-460 449 reactive oxygen species (ROS), green algae possess a wide repertoire of superoxide and peroxide neutralizing enzymes and the complementary reducing substrates. Examples include the co-substrate-dependent enzymes ascorbate oxidase and thioreductase, next to the reducing co-substrate-independent superoxide dismutase and catalase enzymes (Dietz 2011;Schmitt et al 2014). The possible algicidal and cyanocidal and/ or cyanostatical activity of HP as formed during decay of barley and rice straw have been mentioned already in ''Barley straw'' and ''Rice straw'' sections of this review.…”

A Chloroplast Light-Regulated Oxidative Sensor for Moderate Light Intensity in Arabidopsis

“…Studies of bacteria, plants, and animals revealed that ROS signals could be perceived directly by specific sensors (Storz et al, 1990;D'Autréaux and Toledano, 2007) or by the use of antioxidative enzymes, such as peroxiredoxins (Prxs) (D'Autréaux and Toledano, 2007;Fourquet et al, 2008;Dietz, 2011;Fomenko et al, 2011). Prxs are ancient conserved enzymes that catalytically reduce hydrogen peroxide and organic peroxides and in turn oxidize their electron donors, such as Trxs, to regenerate their activity (Hall et al, 2009;Dietz, 2011).…”

“…Prxs are ancient conserved enzymes that catalytically reduce hydrogen peroxide and organic peroxides and in turn oxidize their electron donors, such as Trxs, to regenerate their activity (Hall et al, 2009;Dietz, 2011). Plant Prxs were implicated as redox sensors, linking the redox signaling and ROS networks of cells (Dietz, 2011). Recent findings identified particular 2-Cys Prxs as a circadian rhythmic biomarker in algae cells and mammalian red blood cells and as a regulator of Drosophila melanogaster embryo development (Degennaro et al, 2011).…”