Journalartikel

Jahr der Veröffentlichung: 2002

Seiten: 11521-11526

Zeitschrift: Journal of Biological Chemistry

Bandnummer: 277

Heftnummer: 13

ISSN: 0021-9258

eISSN: 1083-351X

Open Access Status: Hybrid

DOI Link: https://doi.org/10.1074/jbc.M111692200

Verlag: Elsevier

Abstract: 
Defense against oxidative stress in mammals includes the regeneration of the major thiol reductants glutathione and thioredoxin by glutathione reductase and thioredoxin reductase (TrxR), respectively. In contrast, Drosophila, and possibly insects in general, lacks glutathione reductase and must rely solely on the TrxR system. The mammalian TrxRs described so far are selenoproteins that utilize NADPH to reduce protein as well as nonprotein substrates in mitochondria and cytoplasm of cells. We show that a single Drosophila gene, Trxr-1, encodes non-selenocysteine-containing cytoplasmic and mitochondrial TrxR isoforms that differ with respect to their N termini. We generated transcript-specific mutants and used in vivo approaches to explore the biological functions of the two enzyme variants by introducing the corresponding transgenes into different Trxr-1 mutants. The results show that, although the two TrxR isoforms have similar biochemical properties, their biological functions are not interchangeable.

Harvard-Zitierstil: Missirlis, F., Ulschmid, J., Hirosawa-Takamori, M., Grönke, S., Schäfer, U., Becker, K., et al. (2002) Mitochondrial and cytoplasmic thioredoxin reductase variants encoded by a single Drosophila gene are both essential for viability, Journal of Biological Chemistry, 277(13), pp. 11521-11526. https://doi.org/10.1074/jbc.M111692200

APA-Zitierstil: Missirlis, F., Ulschmid, J., Hirosawa-Takamori, M., Grönke, S., Schäfer, U., Becker, K., Phillips, J., & Jäckle, H. (2002). Mitochondrial and cytoplasmic thioredoxin reductase variants encoded by a single Drosophila gene are both essential for viability. Journal of Biological Chemistry. 277(13), 11521-11526. https://doi.org/10.1074/jbc.M111692200