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J. Biol. Chem., Vol. 269, Issue 6, 4438-4449, 02, 1994
GG Mason, AM Witte, ML Whitelaw, C Antonsson, J McGuire, A Wilhelmsson, L Poellinger and JA Gustafsson
The basic region/helix-loop-helix dioxin receptor mediates signal
transduction by dioxin (2,3,7,8-tetrachlorodibenzo-p-dioxin). Upon ligand
binding the dioxin receptor is converted from a latent, non-DNA binding
form to a form that directly interacts with target genes by binding to
dioxin-responsive transcriptional control elements. We have purified by
conventional and DNA affinity chromatographic procedures the
ligand-activated, DNA binding form of dioxin receptor to examine its
architecture and functional properties. We observed that the DNA binding
activity of the receptor was labile. Most notably, this activity was lost
following DNA affinity purification. In complementation experiments we have
identified an auxiliary factor(s) that exhibited very poor, if any,
intrinsic affinity for the DNA target sequence in vitro but strongly
increased the DNA binding activity of the purified receptor-containing
material identified by immunoblot analysis. In a similar fashion the in
vitro expressed basic region/helix-loop-helix factor Arnt (that has been
postulated to modulate the nuclear translocation function of the receptor)
reconstituted the DNA binding function of the purified receptor, and the
purified auxiliary factor reconstituted receptor activity upon addition to
an extract from mutant, Arnt-deficient hepatoma cells. Conversely, purified
dioxin receptor reconstituted DNA binding activity in extracts from
receptor-deficient hepatoma cells which express bona fide levels of Arnt.
Interestingly, UV cross-linking studies using a BrdU-substituted DNA target
sequence indicated that primarily the receptor protein was bound to DNA.
Moreover, we demonstrate that purified receptor or Arnt exhibited virtually
no detectable affinity for the target sequence individually but, in the
presence of one another, showed a strong synergy in DNA binding activity in
vitro. Importantly, simultaneous expression of the receptor and Arnt
resulted in synergistic induction of gene expression in vivo. These data
demonstrate that Arnt plays a central role in control of dioxin receptor
function by cooperatively modulating the DNA binding activity of the
receptor in vitro and dioxin-dependent transactivation in vivo.
Purification of the DNA binding form of dioxin receptor. Role of the Arnt cofactor in regulation of dioxin receptor function
Department of Medical Nutrition, Karolinska Institute, Huddinge Hospital, Sweden.
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