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A 161-base pair fragment (AB1)
Volume 270,
Number 20,
Issue of May 19, pp. 11977-11984, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
10 kilobase pairs upstream
of the transcription start site of the mouse heme oxygenase-1 gene
functions as a basal level and inducer-dependent enhancer.
AB1/chloramphenicol acetyltransferase fusion genes stably transfected
into mouse hepatoma (Hepa) cells or L929 fibroblasts were activated
7-8- or 17-22-fold, respectively, after treatment of the
cells with either CdCl
or heme. The AB1 fragment is
composed largely of three tandem repeats containing two conserved core
elements, A and B. Part of core element A (TCCGGAGCTGTG) resembles the
consensus-binding site for transcription factor AP-4, whereas core
element B (GCTGAGTCANGG) includes the consensus-binding site (TGAGTCA)
for the AP-1 family of transcription factors. Nuclear proteins from
Hepa cells did not bind to any of the core A elements, but bound to all
three copies of the core B element. AB1 derivatives with one or two
mutant AP-1-binding elements exhibited reduced but measurable
inducer-dependent enhancer activity, but mutation of all three
AP-1-binding sites abolished activation by CdCl and heme
and also by mercury chloride, zinc chloride,
HO, sodium arsenate, and
12-O-tetradecanoylphorbol-13-acetate. Pretreatment of stably
transfected L929 cells with protein kinase C inhibitors, but not with
tyrosine kinase inhibitors or N-acetylcysteine, abrogated
12-O-tetradecanoylphorbol-13-acetate-dependent activation of
the AB1/chloramphenicol acetyltransferase fusion gene. Induction by
HO was unaffected by the kinase inhibitors, but
completely abolished by N-acetylcysteine. Heme-dependent
induction was not significantly affected by any of these chemicals.
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