Thioredoxins in Arabidopsis and other plants.
Regulation of disulfide dithiol exchange has become increasingly important in our knowledge of plant life. Initially discovered as regulators of light-dependent malate biosynthesis in the chloroplast, plant thioredoxins are now implicated in a large panel of reactions related to metabolism, defense and development. In this review we describe the numerous thioredoxin types encoded by the Arabidopsis genome, and provide evidence that they are present in all higher plants. Some results suggest cross-talk between thioredoxins and glutaredoxins, the second family of disulfide dithiol reductase. The development of proteomics in plants revealed an unexpectedly large number of putative target proteins for thioredoxins and glutaredoxins. Nevertheless, we are far from a clear understanding of the actual function of each thioredoxin in planta. Although hampered by functional redundancies between genes, genetic approaches are probably unavoidable to define which thioredoxin interacts with which target protein and evaluate the physiological consequences.
Meyer
Yves
Y
Laboratoire de Physiologie et Biologie Moléculaire des Plantes, Université UMR CNRS 5096 Genome et Développement des Plantes, 52, Av Paul Alduy , 66860 Perpignan, France. ymeyer@univ-perp.fr
Reichheld
Jean Philippe
JP
Vignols
Florence
F
D000818:Animals; D017360:Arabidopsis / Q000235:genetics / Q000378:metabolism*; D005979:Glutathione Peroxidase / Q000378:metabolism; D010802:Phylogeny; D040901:Proteomics; D013880:Thioredoxin-Disulfide Reductase / Q000378:metabolism; D013879:Thioredoxins / Q000235:genetics / Q000378:metabolism*
D013879:Thioredoxins; D005979:Glutathione Peroxidase; D013880:Thioredoxin-Disulfide Reductase