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(Received for publication, September 13,
1995; and in revised form, November 7, 1995) The aryl hydrocarbon receptor (AHR) is a ligand-activated
transcription factor that binds DNA in the form of a heterodimer with
the AHR nuclear translocator protein (ARNT). Both proteins possess
basic helix-loop-helix motifs. ARNT binds to the side of the xenobiotic
responsive element (XRE) that resembles an E-box (the sequence
recognized by the majority of other basic helix-loop-helix proteins),
whereas AHR binds to the side of the XRE that does not conform to the
E-box sequence. The basic region of ARNT closely resembles those of
other E-box-binding proteins, whereas the ``nominal basic
region'' of AHR (amino acids 27-39), although required for
XRE binding, deviates from this consensus. By extensive mutational
analysis it is shown here that an additional block of amino acids of
AHR (from tyrosine 9 to lysine 20) that contains a highly basic segment
is required for XRE binding and transcriptional activation. Deletion of
the first nine amino acids negates XRE binding. Substitution of either
tyrosine 9 or arginine 14 with alanine eliminates XRE binding, whereas
alanine substitutions at certain other sites within the block reduce
but do not eliminate binding. The reported absence of the first nine
amino acids in the purified protein may therefore be artifactual. These
results suggest that the amino acids of AHR involved in binding to the
XRE constitute a novel DNA-binding domain, comprising amino acids
located within and amino-terminal to the nominal basic region.
Volume 271,
Number 7,
Issue of February 16, 1996 pp. 3743-3749
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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