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(Received for publication, April 1, 1996, and in revised form, December 3, 1996)
From the In an effort to better understand the mechanism
of toxicity of 2,3,7,8-tetrachlorodibenzo-p-dioxin, we
employed an iterative search of human expressed sequence tags to
identify novel basic-helix-loop-helix-PAS (bHLH-PAS) proteins that
interact with either the Ah receptor (AHR) or the Ah receptor nuclear
translocator (ARNT). We characterized five new "embers
f the AS superfamily," or MOPs 1-5, that
are similar in size and structural organization to the AHR and ARNT. MOPs 1-4 have N-terminal bHLH and PAS domains and C-terminal variable regions. MOP5 contained the characteristic PAS domain and a variable C
terminus; it is possible that the cDNA contains a bHLH domain, but the
entire open reading frame has yet to be completed.
Coimmunoprecipitation studies, yeast two-hybrid analysis, and transient
transfection experiments demonstrated that MOP1 and MOP2 dimerize with
ARNT and that these complexes are transcriptionally active at defined DNA enhancer sequences in vivo. MOP3 was found to associate
with the AHR in vitro but not in vivo. This
observation, coupled with the fact that MOP3 formed tighter
associations with the 90-kDa heat shock protein than the human AHR,
suggests that MOP3 may be a conditionally active bHLH-PAS protein that
requires activation by an unknown ligand. The expression profiles of
the AHR, MOP1, and MOP2 mRNAs, coupled with the observation that
they all share ARNT as a common dimeric partner, suggests that the
cellular pathways mediated by MOP1 and MOP2 may influence or respond to
the dioxin signaling pathway.
Volume 272, Number 13,
Issue of March 28, 1997
pp. 8581-8593
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
§
,
,
,
,
Department of Molecular Pharmacology and
Biological Chemistry, Northwestern University Medical School, Chicago,
Illinois 60611, the § McArdle Laboratory for Cancer
Research, University of Wisconsin Medical School, Madison,
Wisconsin 53706, and the ¶ Department of Veterinary Science,
Pennsylvania State University, State College, Pennsylvania 16802
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