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J Biol Chem, Vol. 273, Issue 28, 17756-17762, July 10, 1998
From the Steroid Hormones Section, NIDDK/LMCB, National Institutes
of Health, Bethesda, Maryland 20892
The 21-base pair glucocorticoid modulatory
element (GME) of the rat tyrosine aminotransferase gene is the only
cis-acting element known to modulate the transcriptional
activity of receptors bound to glucocorticoid response elements.
Specifically, the GME increases the activity of complexes bound both by
physiological concentrations of glucocorticoids, due to a left shift in
the dose-response curve, and by saturating concentrations of
anti-glucocorticoids. For this reason, the nuclear protein(s) that has
been demonstrated to bind to the GME is of major interest as a possible
transcription factor with hitherto undescribed properties. Subsequent
studies indicated that not one but two proteins of 88 and 67 kDa (=
GMEB-1 and -2, respectively) formed a heteromeric complex with
double-stranded GME oligonucleotides in gel shift assays and
participated in the expression of GME activity (Oshima, H., Szapary,
D., and Simons, S. S., Jr. (1995) J. Biol. Chem.
270, 21893-21910). Here, we report the use of polymerase chain
reaction of degenerate oligonucleotides and 5'- and 3'-rapid
amplification of cDNA ends to clone two cDNAs of 2.0 and 1.9 kilobase pairs that probably result from alternative splicing. Both
cDNAs encoded open reading frames containing all four previously
sequenced peptides. The longer 2.0-kilobase pair cDNA encoded an
open reading frame for an acidic, 529-amino acid protein and afforded a
major 67-kDa and a minor 58-kDa protein after in vitro
transcription/translation. Both proteins were recognized by a
mono-epitopic antibody raised against a peptide of GMEB-2. The in
vitro translated protein bound to GME DNA in gel shift assays.
However, the binding to GME DNA increased markedly after mixing with
authentic GMEB-1 to give a gel-shifted complex that was similar to that
derived from HTC cell cytosol. GMEB-2 shares a unique domain (KDWKR)
with proteins derived from diverse organisms as follows:
Drosophila (DEAF-I), rat (Suppressin), and
Caenorhabditis elegans (three unknown open reading frames).
Collectively, these data suggest that the 67-kDa GMEB-2 not only is an
important factor for the modulation of glucocorticoid receptor bound to
glucocorticoid response elements but also may belong to a novel family
of transcription factors.
Cloning and Characterization of a Novel Binding Factor (GMEB-2)
of the Glucocorticoid Modulatory Element
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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