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(Received for publication, December 29,
1995; and in revised form, January 31, 1996) The aryl hydrocarbon receptor (AHR) and the aryl hydrocarbon
receptor nuclear translocator (ARNT) belong to a novel subclass of
basic helix-loop-helix transcription factors. The AHR
Volume 271,
Number 15,
Issue of April 12, 1996 pp. 8843-8850
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
ARNT
heterodimer binds to the xenobiotic responsive element (XRE).
Substitution of each of four amino acids in the basic region of ARNT
with alanine severely diminishes or abolishes XRE binding, intimating
that these amino acids contact DNA bases. Three of these amino acids
are conserved among basic helix-loop-helix proteins, and the
corresponding amino acids of Max and USF are known to contact DNA
bases. Alanine scanning mutagenesis of the basic domain of AHR and
substitution with conservative amino acids at particular positions in
this domain and in a more amino-proximal AHR segment previously shown
to be required for XRE binding (Fukunaga, B. N., and Hankinson, O.
(1996) J. Biol. Chem. 271, 3743-3749) demonstrate that
the most carboxyl-proximal amino acid position of the basic domain and
a position within the amino-proximal segment are intolerant to amino
acid substitution with regard to XRE binding, suggesting that these two
amino acids make base contacts. Amino acid positions in these AHR
regions and in the ARNT basic region less adversely affected by
substitution are also identified. The amino acids at these positions
may contact the phosphodiester backbone. The apparent bipartite nature
of the DNA binding region of AHR and the identity of those of its amino
acids that apparently make DNA contacts impute a novel protein-DNA
binding behavior for AHR.
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