Atypical Thioredoxins in Poplar: The Glutathione-Dependent Thioredoxin-Like 2.1 Supports the Activity of Target Enzymes Possessing a Single Redox Active Cysteine1[W]
نویسندگان
چکیده
UMR 1136 Lorraine University-INRA, Interactions Arbres-Microorganismes, Institut Fédératif de Recherche 110 Ecosystèmes Forestiers, Agroressources, Bioprocédés, et Alimentation, Faculté des Sciences, 54506 Vandoeuvre-lès-Nancy cedex, France (K.C., L.T., J.-P.J., N.R.); Department of Forest Genetics and Plant Physiology, Swedish University of Agricultural Sciences, Umea Plant Science Centre, 90183 Umea, Sweden (K.C., G.W.); Institut de Biologie Moléculaire des Plantes, CNRS-UPR 2357, 67084 Strasbourg, France (J.M.G.); Commissariat à l9Energie Atomique et aux Energies Alternative, Direction des Sciences du Vivant; Institut de Biologie Environnementale et Biotechnologie, Laboratoire d9Ecophysiologie Moléculaire des Plantes, Saint-Paul-lez-Durance F-13108, France (P.R.); CNRS, UMR 7265 Biologie Végétale et Microbiologie Environnementales, Saint-Paul-lez-Durance, F-13108, France (P.R.); and Aix-Marseille Université, Saint-Paul-lez-Durance, F-13108, France (P.R.)
منابع مشابه
Atypical thioredoxins in poplar: the glutathione-dependent thioredoxin-like 2.1 supports the activity of target enzymes possessing a single redox active cysteine.
Plant thioredoxins (Trxs) constitute a complex family of thiol oxidoreductases generally sharing a WCGPC active site sequence. Some recently identified plant Trxs (Clot, Trx-like1 and -2, Trx-lilium1, -2, and -3) display atypical active site sequences with altered residues between the two conserved cysteines. The transcript expression patterns, subcellular localizations, and biochemical propert...
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