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J Biol Chem, Vol. 275, Issue 18, 13398-13405, May 5, 2000

Transcriptional Regulation of Glutaredoxin and Thioredoxin Pathways and Related Enzymes in Response to Oxidative Stress*

María-José Prieto-ÁlamoDagger , Juan JuradoDagger §, Rafaela Gallardo-MadueñoDagger , Fernando Monje-CasasDagger , Arne Holmgren||, and Carmen PueyoDagger **

From the Dagger  Departamento de Bioquímica y Biología Molecular, Universidad de Córdoba, 14071-Córdoba, España and the || Medical Nobel Institute for Biochemistry, Department of Medical Biochemistry and Biophysics, Karolinska Institute, S-171 77, Stockholm, Sweden

We examined the in vivo expression of up to 16 genes encoding for components of both glutaredoxin and thioredoxin systems and for members of the OxyR and SoxRS regulons. We demonstrated that grxA (Grx1) transcription is triggered in bacteria lacking Trx1 (trxA) and GSH (gshA) in an OxyR-dependent manner. We also indicated that, unlike OxyR, SoxR is not constitutively activated in the oxidizing environment of trxA gshA mutants. We discovered that the lack of Trx1 plus GSH increases the steady-state levels of Trx reductase (trxB) and Trx2 (trxC) transcripts. This increase and the trxB and trxC up-regulation caused by the constitutive oxyR2 allele indicate that OxyR also plays a role in the regulation of the thioredoxin pathway. On the contrary, no change in the expression of genes for Trx1, Grx2, and Grx3 was observed. Transcription of nrdAB (RRase) was not induced by oxidative stress yet was induced by hydroxyurea (RRase inhibitor). Induction level was as the enhanced nrdAB basal expression of trxA grxA mutants, indicating that RRase operation without Trx1 and Grx1 must lead to disturbances sensed as those caused by hydroxyurea. We also demonstrated an inverse relation between nrdAB expression and that of genes coding for components of both glutaredoxin (grxA, gorA) and thioredoxin (trxB, trxC) systems.

* This work was supported by Junta de Andalucía (group CVI 0187) Grants PB95-0557-CO2-01 and PB98-1627 (to D. G. E. S.) and by the Swedish Cancer Society.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Recipient of a postdoctoral contract from the Ministerio de Educación y Cultura.

Recipient of a predoctoral fellowship from Junta de Andalucía.

** To whom correspondence and reprint requests should be addressed: C. Pueyo, Departamento de Bioquímica y Biología Molecular, Avda. de Medina Azahara s/n, Universidad de Córdoba, 14071 Córdoba, España. Tel.: 34-957-218695; Fax: 34-957-218688; E-mail: bb1pucuc@uco.es.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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