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J. Biol. Chem., Vol. 276, Issue 24, 20858-20865, June 15, 2001
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From the 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. By 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 an StRE sequence from
the ho-1 gene. CdCl2, a potent inducer of HO-1,
increased expression of ATF4 in mouse hepatoma cells, and detectable
induction of ATF4 protein preceded that of HO-1 (30 min
versus 2 h). A dominant-negative mutant of ATF4
inhibited basal and CdCl2-stimulated expression of a
StRE-dependent/luciferase fusion construct (pE1-luc) in hepatoma 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.
Section of Pulmonary and Critical Care
Medicine, Yale University School of Medicine,
New Haven, Connecticut 06520, Renal
Electrolyte Division and § Division of Pulmonary, Allergy,
and Critical Care Medicine, Department of Medicine, University of
Pittsburgh, Pittsburgh, Pennsylvania 15231, Department of
Molecular Genetics, Alton Ochsner Medical Foundation, New
Orleans, Louisiana 70121, and the ** Department of Biochemistry and
Molecular Biology, Louisiana State University Health Sciences Center,
New Orleans, Louisiana 70112
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