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Originally published In Press as doi:10.1074/jbc.M011728200 on February 23, 2001

J. Biol. Chem., Vol. 276, Issue 21, 18031-18037, May 25, 2001
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Expression Analysis of the nrdHIEF Operon from Escherichia coli
CONDITIONS THAT TRIGGER THE TRANSCRIPT LEVEL IN VIVO*

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

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

Escherichia coli has two aerobic ribonucleotide reductases encoded by the nrdAB and nrdHIEF operons. While NrdAB is active during aerobiosis, NrdEF is considered a cryptic enzyme with no obvious function. Here, we present evidence that nrdHIEF expression might be important under certain circumstances. Basal transcript levels were dramatically enhanced (25-75-fold), depending on the growth-phase and the growth-medium composition. Likewise, a large increase of >100-fold in nrdHIEF mRNA was observed in bacteria lacking Trx1 and Grx1, the two main NrdAB reductants. Moreover, nrdHIEF expression was triggered in response to oxidative stress, particularly in mutants missing hydroperoxidase I and alkyl-hydroperoxide reductase activities (69.7-fold) and in cells treated with oxidants (up to 23.4-fold over the enhanced transcript level possessed by cells grown on minimal medium). The mechanism(s) that triggers nrdHIEF expression remains unknown, but our findings exclude putative global regulators like RpoS, Fis, cAMP, OxyR, SoxR/S, or RecA. What we have learned about nrdHIEF expression indicates strong differences between its regulation and that of the nrdAB operon and of genes coding for components of both thioredoxin/glutaredoxin pathways. We propose that E. coli might optimize the responses to different stimuli by co-evolving the expression levels for its multiple reductases and electron donors.

* This work was supported by Dirección General de Enseñanza Superior Grant PB98-1627, by Junta de Andalucía Group CVI 0187, and by Swedish Cancer Society Grant 961.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 predoctoral fellowship from Junta de Andalucía.

Recipients of postdoctoral contracts from the Ministerio de Educación y Cultura.

** To whom correspondence and reprint requests should be addressed: Dept. de Bioquímica y Biología Molecular, Campus de Rabanales, edificio C-6, planta 2a, Carretera Madrid-Cádiz Km 396-a, Universidad de Córdoba, 14071-Córdoba, España. Tel.: 34-957-218695; Fax: 34-957-218688; E-mail: bb1pucuc@uco.es.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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