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(Received for publication, May 6, 1996)
From the Department of Pathology, Washington University School of
Medicine, St. Louis, Missouri 63110
We have identified a novel steroid hormone
response element in the avian
Volume 271, Number 34,
Issue of August 23, 1996
pp. 20650-20654
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
3 integrin promoter. This
sequence, comprising three hexameric direct repeat half-sites separated
by nine and three nucleotides binds vitamin D receptor (VDR)-retinoid X
receptor (RXR) and retinoic acid receptor (RAR)-RXR heterodimers.
VDR-RXR binds direct repeats separated by three base pairs, and RAR-RXR
recognizes half-sites separated by nine bases, whereas the central
half-site interacts with both heterodimers. Retinoic acid and
1,25-dihydroxyvitamin D3 activate both a genomic fragment
including the transcriptional start site and an oligonucleotide
containing the three repeats, linked to a heterologous promoter.
Co-addition of the steroids produces neither synergy nor an additive
effect; rather the result equals that for retinoic acid alone.
Scatchard analysis demonstrates that RAR-RXR has greater affinity than
VDR-RXR for the composite element. Based on these findings we propose a
model in which there is specific, polarity-defined binding of VDR-RXR
and RAR-RXR to three half-sites, which form two overlapping steroid
response elements, with the central half-site common to both. Our
results identify a novel mechanism by which one steroid hormone can
modulate the activity of a second, by competing for a shared half-site
in a composite response element.
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