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Genetics, Vol. 179, 41-57, May 2008, Copyright © 2008
doi:10.1534/genetics.107.086041
The Peroxiredoxin and Glutathione Peroxidase Families in Chlamydomonas reinhardtii
Régine Dayer*,
Beat B. Fischer
,
Rik I. L. Eggen* and
Stéphane D. Lemaire
,1
Institut de Biotechnologie des Plantes, Unité Mixte de Recherche 8618, Centre National de la Recherche Scientifique, Université Paris-Sud 11, 91405 Orsay Cedex, France, * Department of Environmental Toxicology, Eawag, Swiss Federal Institute of Aquatic Science and Technology, Ueberlandstrasse 133, CH-8600, Duebendorf, Switzerland and Department of Plant and Microbial Biology, University of California, Berkeley, California 94720-3102
1 Corresponding author: Institut de Biotechnologie des Plantes, Bâtiment 630, Université Paris-Sud, F-91405 Orsay Cedex, France.
E-mail: stephane.lemaire{at}u-psud.fr
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.
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