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Papers In Press, published online ahead of print March 26, 2001
J. Biol. Chem, 10.1074/jbc.M101198200
Submitted on February 7, 2001
Revised on March 23, 2001
Accepted on March 26, 2001
Department of Molecular Genetics, Alton Ochsner Medical Foundation, New Orleans, Louisiana 70121
Corresponding Author: jalam{at}ochsner.org
Nrf2 regulates expression of genes encoding enzymes with antioxidant (e.g., heme oxygenase-1 (HO-1)) or xenobiotic detoxification (e.g., NAD(P)H:quinone oxidoreductase, glutathione S-transferase) functions via the stress- or antioxidant- response elements (StRE/ARE). Nrf2 heterodimerizes with small Maf proteins but the role of such dimers in gene induction is controversial and other partners may exist. Using the yeast two-hybrid assay, we identified activating transcription factor (ATF) 4 as a potential Nrf2 interacting protein. Association between Nrf2 and ATF4 in mammalian cells was confirmed by co-immunoprecipitation and mammalian two hybrid assays. Furthermore, Nrf2•ATF4 dimers bound to a StRE sequence from the ho-1 gene. CdCl2, a potent inducer of HO-1, increased expression of ATF4 in mouse hepatoma (Hepa) cells and detectable induction of ATF4 protein preceded that of HO-1 (30 min vs. 2 h). A dominant-negative mutant of ATF4 inhibited basal and CdCl2-stimulated expression of a StRE-dependent /luciferase fusion construct (pE1-luc) in Hepa cells but only basal expression in mammary epithelial MCF-7 cells. A dominant mutant of Nrf2 was equally inhibitory in both cell types in the presence or absence of CdCl2. These results indicate that ATF4 regulates basal and CdCl2-induced expression of the ho-1 gene in a cell-specific manner and possibly in a complex with Nrf2.
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