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Substitution of the Thioredoxin System for Glutathione Reductase in Drosophila melanogaster

Science  26 Jan 2001:
Vol. 291, Issue 5504, pp. 643-646
DOI: 10.1126/science.291.5504.643

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Abstract

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.

  • * 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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