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Originally published In Press as doi:10.1074/jbc.M204232200 on July 10, 2002

J. Biol. Chem., Vol. 277, Issue 38, 34997-35006, September 20, 2002
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c-Myc Represses and Miz-1 Activates the Murine Natural Resistance-associated Protein 1 Promoter*

Holly BowenDagger §, Thelma E. BiggsDagger , Emma PhillipsDagger , Stephen T. BakerDagger , V. Hugh Perry||, Derek A. Mann**, and C. Howard BartonDagger Dagger Dagger

From the Dagger  Biochemistry and Molecular Biology, || CNS Inflammation Group, University of Southampton, Bassett Crescent East, Southampton SO16 7PX and the ** Liver Group, Division of Infection, Inflammation, Allergy, and Repair, Level D South Block, University of Southampton, Southampton General Hospital, Tremona Rd., Southampton SO16 6YD, United Kingdom

Iron is essential for growth, and impaired iron homoeostasis through a non-conserved mutation within murine Nramp1, also termed Slc11a1, contributes to susceptibility to infection. Nramp1 depletes the macrophage cytosol of iron, with effects on iron-regulated gene expression and iron-dependent processes. Wu and colleagues (Wu, K.-J., Polack, A., and Dalla-Favera, R. (1999) Science 283, 676-679) showed converse control of iron regulatory protein expression (IRP2) and H-ferritin by c-Myc, suggesting a role for c-Myc in enhancing cytoplasmic iron levels for growth. We investigated if c-Myc also regulates Nramp1 expression. We show an inverse correlation with cell growth, and in co-transfection experiments c-Myc represses the Nramp1 promoter. Within the Nramp1 promoter we identified six non-canonical E boxes, which are not important for c-Myc repression. By deletion analysis the repressor site maps to one or more initiator elements flanking the transcriptional initiation site. Co-transfections with the c-Myc interacting zinc finger protein (Miz-1) show that Miz-1 can overcome c-Myc repression of Nramp1, and, from a deletion construct lacking E box sites, Miz-1 activates the Nramp1 promoter. These studies reinforce the link between c-Myc and iron regulation and provide further evidence that c-Myc negatively regulates genes that decrease the iron content of the cytosol. The results provide further support for a divalent cation antiporter function for Nramp1.

* This work was supported in part by grants from the Wessex Medical (HOPE) and Wellcome Trusts.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.

§ A recipient of a University of Southampton Inter-Schools Biomedical Research Initiative studentship.

The recipient of a Biotechnology and Biological Sciences and Research Council studentship.

Dagger Dagger To whom correspondence should be addressed. Tel.: 44-23-8059-2907; Fax: 44-23-8059-4459; E-mail: CHB@soton.ac.uk.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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