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J. Biol. Chem., Vol. 282, Issue 47, 34365-34371, November 23, 2007

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Bach1 Repression of Ferritin and Thioredoxin Reductase1 Is Heme-sensitive in Cells and in Vitro and Coordinates Expression with Heme Oxygenase1, -Globin, and NADP(H) Quinone (Oxido) Reductase1^*

Korry J. Hintze¹, Yasutake Katoh, Kazuhiko Igarashi, and Elizabeth C. Theil^¶2

From the Council for BioIron at CHORI, Children's Hospital Oakland Research Institute, Oakland, California 94609, Department of Biochemistry, Tohoku University School of Medicine, Sendai 980-8575, Japan, and ^¶Department of Nutritional Sciences and Toxicology, University of California, Berkeley, Berkeley, California 94720

Ferritin gene transcription is regulated by heme as is ferritin mRNA translation, which is mediated by the well studied mRNA·IRE/IRP protein complex. The heme-sensitive DNA sequence in ferritin genes is the maf recognition/antioxidant response element present in several other genes that are induced by heme and repressed by Bach1. We now report that chromatin immunoprecipitated with Bach1 antiserum contains ferritin DNA sequences. In addition, overexpression of Bach1 protein in the transfected cells decreased ferritin expression, indicating insufficient endogenous Bach1 for full repression; decreasing Bach1 with antisense RNA increased ferritin expression. Thioredoxin reductase1, a gene that also contains a maf recognition/antioxidant response element but is less studied, responded similarly to ferritin, as did the positive controls heme oxygenase1 and NADP(H) quinone (oxido) reductase1. Bach1-DNA promoter interactions in cells were confirmed in vitro with soluble, recombinant Bach1 protein and revealed a quantitative range of Bach1/DNA stabilities: ferritin L ferritin H -globin, -globin 2-fold >heme oxygenase1 = quinone reductase -globin 4-fold >thioredoxin reductase1. Such results indicate the possibility that modulation of cellular Bach1 concentrations will have variable effects among the genes coordinately regulated by maf recognition/antioxidant response elements in iron/oxygen/antioxidant metabolism.

Received for publication, January 10, 2007 , and in revised form, September 10, 2007.

^* This work was supported by funds from the National Institutes of Health (DK20251) (to E. C. T. and K. J. H.), The CHORI Foundation (to E. C. T.), and grants-in-aid from the Ministry of Education, Science, Sport, and Culture of Japan (to K. I.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Fig. S1.

¹ Present address: Dept. of Nutrition and Food Sciences, Utah State University, Logan, UT 84322-1400.

² To whom correspondence should be addressed: Children's Hospital Oakland Research Inst., 5700 Martin Luther King Jr. Way, Oakland, CA 94609. Tel.: 510-450-7670; Fax: 510-597-7131; E-mail: etheil{at}chori.org.

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