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J Biol Chem, Vol. 274, Issue 28, 19714-19722, July 9, 1999
From the Disruption of the two thioredoxin genes in yeast
dramatically affects cell viability and growth. Expression of
Arabidopsis thioredoxin AtTRX3 in the
Saccharomyces thioredoxin
In Vivo Characterization of a Thioredoxin h Target
Protein Defines a New Peroxiredoxin Family
,,, and
Laboratoire de Physiologie et de Biologie
Moléculaire des Plantes, UMR 5545, Université de
Perpignan, Avenue de Villeneuve, F 66025, Perpignan, France and the
¶ Laboratoire de Biologie Forestière, Associé
INRA, Université de Nancy 1, BP 239, F
54506, Vandoeuvre, France
strain EMY63 restores a
wild-type cell cycle, the ability to grow on methionine sulfoxide, and
H2O2 tolerance. In order to isolate thioredoxin targets related to these phenotypes, we prepared a C35S
(Escherichia coli numbering) thioredoxin mutant to
stabilize the intermediate disulfide bridged complex and we added a
polyhistidine N-terminal extension in order to purify the complex
rapidly. Expression of this mutant thioredoxin in the wild-type yeast
induces a reduced tolerance to H2O2, but only
limited change in the cell cycle and no change in methionine sulfoxide
utilization. Expression in the thioredoxin strain EMY63 allowed us
to isolate a complex of the thioredoxin with YLR109, an abundant yeast
protein related to PMP20, a peroxisomal protein of Candida.
No function has so far been attributed to this protein or to the other
numerous homologues described in plants, animals, fungi, and
prokaryotes. On the basis of the complementation and of low similarity
with peroxiredoxins, we produced YLR109 and one of its
Arabidopsis homologues in E. coli to test their
peroxiredoxins activity. We demonstrate that both recombinant proteins
present a thioredoxin-dependent peroxidase activity
in vitro. The possible functions of this new peroxiredoxin family are discussed.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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