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Science 26 January 2001:
Vol. 291. no. 5504, pp. 643 - 646
DOI: 10.1126/science.291.5504.643
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Reports

Substitution of the Thioredoxin System for Glutathione Reductase in Drosophila melanogaster

Stefan M. Kanzok,12 Anke Fechner,12 Holger Bauer,1 Julia K. Ulschmid,2 Hans-Michael Müller,3 José Botella-Munoz,4 Stephan Schneuwly,4 R. Heiner Schirmer,1 Katja Becker12*

The disulfide reducing enzymes glutathione reductase and thioredoxin reductase are highly conserved among bacteria, fungi, worms, and mammals. These proteins maintain intracellular redox homeostasis to protect the organism from oxidative damage. Here we demonstrate the absence of glutathione reductase in Drosophila melanogaster, identify a new type of thioredoxin reductase, and provide evidence that a thioredoxin system supports GSSG reduction. Our data suggest that antioxidant defense in Drosophila, and probably in related insects, differs fundamentally from that in other organisms.

1 Center of Biochemistry, Im Neuenheimer Feld 328, Heidelberg University, D-69120 Heidelberg, Germany.
2 Interdisciplinary Research Center, Heinrich-Buff-Ring 26-32, Giessen University, D-35392 Giessen, Germany.
3 European Molecular Biology Laboratory, D-69117 Heidelberg, Germany.
4 Institute of Zoology, Regensburg University, D-93040 Regensburg, Germany.
*   To whom correspondence should be addressed at the Interdisciplinary Research Center, Heinrich-Buff-Ring 26-32, Giessen University, D-35392 Giessen, Germany. E-mail: becker.katja{at}gmx.de

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