Thioredoxins, glutaredoxins, and glutathionylation: new crosstalks to explore

Michelet, Laure; Zaffagnini, Mirko; Massot, Vincent; Kéryer, Eliane; Vanacker, Hélène; Miginiac‐Maslow, Myroslawa; Issakidis‐Bourguet, Emmanuelle; Lemaire, Stéphane D.

doi:10.1007/s11120-006-9096-2

Cited by 97 publications

(83 citation statements)

References 232 publications

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“…Therefore, glutathionylation might be required for the GRX-dependent reduction of the enzyme as previously observed for mammalian 1-cys PRX, which interacts with PGST and undergoes glutathionylation (Manevich et al 2004). Alternatively, glutathionylation, which occurs under oxidative stress, might constitute a mechanism of regulation of the activity of PRXs, as observed for many other enzymes (reviewed in Michelet et al 2006).…”

Section: The Peroxiredoxin Familymentioning

confidence: 63%

“…Both types of enzymes may function as thiol oxidoreductases playing a role in redox signaling and oxidant scavenging, just like TRXs and GRXs. In photosynthetic organisms, proteomic approaches have allowed identification of nearly 300 putative targets of TRX and GRX (Buchanan and Balmer 2005;Michelet et al 2006;Lemaire et al 2007). In the coming years, similar approaches may be crucial to unravel the cellular targets and the multiple functions of PRXs and GPXs in Chlamydomonas and other organisms.…”

Section: Physiological Function Of Gpx and Prxmentioning

confidence: 99%

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The Peroxiredoxin and Glutathione Peroxidase Families in Chlamydomonas reinhardtii

et al. 2008

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Thiol/selenol peroxidases are ubiquitous nonheme peroxidases. They are divided into two major subfamilies: peroxiredoxins (PRXs) and glutathione peroxidases (GPXs). PRXs are present in diverse subcellular compartments and divided into four types: 2-cys PRX, 1-cys PRX, PRX-Q , and type II PRX (PRXII). In mammals, most GPXs are selenoenzymes containing a highly reactive selenocysteine in their active site while yeast and land plants are devoid of selenoproteins but contain nonselenium GPXs. The presence of a chloroplastic 2-cys PRX, a nonselenium GPX, and two selenium-dependent GPXs has been reported in the unicellular green alga Chlamydomonas reinhardtii. The availability of the Chlamydomonas genome sequence offers the opportunity to complete our knowledge on thiol/selenol peroxidases in this organism. In this article, Chlamydomonas PRX and GPX families are presented and compared to their counterparts in Arabidopsis, human, yeast, and Synechocystis sp. A summary of the current knowledge on each family of peroxidases, especially in photosynthetic organisms, phylogenetic analyses, and investigations of the putative subcellular localization of each protein and its relative expression level, on the basis of EST data, are presented. We show that Chlamydomonas PRX and GPX families share some similarities with other photosynthetic organisms but also with human cells. The data are discussed in view of recent results suggesting that these enzymes are important scavengers of reactive oxygen species (ROS) and reactive nitrogen species (RNS) but also play a role in ROS signaling. L IFE in an oxygen-rich environment has to deal with the danger of oxidative stress. During normal cell metabolism, reactive oxygen species (ROS) and reactive nitrogen species (RNS) are constantly produced, essentially by respiratory and photosynthetic electron transfer chains. These highly reactive molecules can react with many cell components and damage DNA, proteins, and lipids. Thus, their concentration has to be strictly controlled. For this purpose, aerobic organisms are equipped with nonenzymatic (ascorbate, glutathione, tocopherol, and carotenoid) or enzymatic (catalase, ascorbate peroxidase, superoxide dismutase, glutathione peroxidase, and peroxiredoxin) antioxidant systems to remove ROS from the cells. To control their concentrations, ROS and RNS have to be sensed. It has been established in many organisms that ROS, and especially hydrogen peroxide, are signaling molecules that diffuse across membranes and induce specific signal transduction pathways. Furthermore, ROS can also be produced on purpose by cells in response to several stimuli to function as second messengers inside the cell. Finally, ROS and RNS can control enzyme activities by triggering several post-translational modifications such as disulfide bond formation, thiol oxidation to sulfenic/sulfinic/sulfonic acid, glutathionylation, nitrosylation, or carbonylation.Thiol/selenol peroxidases have emerged, during recent years, as important scavengers of ROS/RNS but they ...

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Section: The Peroxiredoxin Familymentioning

confidence: 63%

Section: Physiological Function Of Gpx and Prxmentioning

confidence: 99%

The Peroxiredoxin and Glutathione Peroxidase Families in Chlamydomonas reinhardtii

et al. 2008

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“…In a recent work, Naher et al [2013] evaluated the antioxidant capacity of seminal plasma by measuring MDA and GSH levels. Protein-S-thionylation/S-cystenylation by these low molecular weight thiols mainly prevents irreversible oxidation of cys residues during the oxidative stress and plays a pivotal role in redox regulation of SH-containing protein [Dickinson and Forman 2002;Michelet et al 2006]. However, in the case of extensive oxidative stress as observed in seminal plasma of RPL males, the PSH are irreversibly oxidized and as a result NPSH are not properly utilized in S-cysteinylation.…”

Section: Resultsmentioning

confidence: 99%

Histone retention, protein carbonylation, and lipid peroxidation in spermatozoa: Possible role in recurrent pregnancy loss

Mohanty

Swain

Goswami

et al. 2016

Systems Biology in Reproductive Medicine

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Contribution from a defective paternal genome has been attributed to be an important cause for spontaneous recurrent pregnancy loss (RPL). Increased oxidative stress results in decreased detoxification and is a cause for damage to chromatin, proteins, and membrane lipids. The present study aimed to explore if there is a significant relationship between retained histones due to defective packaging of DNA in spermatozoa and oxidative stress. RPL patients (n=16) with a history of ≥2 embryo losses before the 20th week of gestation and no female factor abnormality, and fertile healthy volunteers (n=20) as controls were included in the study. A significant difference in the levels of protein carbonylation and lipid peroxidation together with an increased retention of histones in the experimental groups was noticed. Histone carrying sites for oxidative modification such as arginine and lysine might be responsible for disturbing the paternal epigenomic control during early stages of embryonic differentiation leading to abortion. ARTICLE HISTORY

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“…It is mainly controlled by TRXs, which play a major role in redox signaling and oxidative stress responses. In photosynthetic organisms, different approaches led to the identification of ϳ400 putative TRX targets implicated in nearly all cell processes (1,2).…”

mentioning

confidence: 99%

Regulation by Glutathionylation of Isocitrate Lyase from Chlamydomonas reinhardtii

Bedhomme

Zaffagnini

Marchand

et al. 2009

Journal of Biological Chemistry

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Post-translational modification of protein cysteine residues is emerging as an important regulatory and signaling mechanism. We have identified numerous putative targets of redox regulation in the unicellular green alga Chlamydomonas reinhardtii. One enzyme, isocitrate lyase (ICL), was identified both as a putative thioredoxin target and as an S-thiolated protein in vivo. ICL is a key enzyme of the glyoxylate cycle that allows growth on acetate as a sole source of carbon. The aim of the present study was to clarify the molecular mechanism of the redox regulation of Chlamydomonas ICL using a combination of biochemical and biophysical methods. The results clearly show that purified C. reinhardtii ICL can be inactivated by glutathionylation and reactivated by glutaredoxin, whereas thioredoxin does not appear to regulate ICL activity, and no inter-or intramolecular disulfide bond could be formed under any of the conditions tested. Glutathionylation of the protein was investigated by mass spectrometry analysis, Western blotting, and site-directed mutagenesis. The enzyme was found to be protected from irreversible oxidative inactivation by glutathionylation of its catalytic Cys 178 , whereas a second residue, Cys 247 , becomes artifactually glutathionylated after prolonged incubation with GSSG. The possible functional significance of this post-translational modification of ICL in Chlamydomonas and other organisms is discussed.

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Thioredoxins, glutaredoxins, and glutathionylation: new crosstalks to explore

Cited by 97 publications

References 232 publications

The Peroxiredoxin and Glutathione Peroxidase Families in Chlamydomonas reinhardtii

The Peroxiredoxin and Glutathione Peroxidase Families in Chlamydomonas reinhardtii

Histone retention, protein carbonylation, and lipid peroxidation in spermatozoa: Possible role in recurrent pregnancy loss

Regulation by Glutathionylation of Isocitrate Lyase from Chlamydomonas reinhardtii

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