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J Biol Chem, Vol. 275, Issue 13, 9749-9757, March 31, 2000
From the Departments of Pathology and Internal Medicine, Division
of Laboratory Medicine, Washington University School of Medicine,
St. Louis, Missouri 63110
The EGR1/NGFI-A transcription factor directly
activates the luteinizing hormone
A Novel Activation Function for NAB Proteins in
EGR-dependent Transcription of the Luteinizing Hormone
Gene*
(LH) subunit promoter, and
female mice lacking EGR1 are infertile due to LH deficiency. The
NGFI-A-binding proteins NAB1 and
NAB2 are corepressors of EGR1/NGFI-A and of the related proteins
EGR2/Krox20 and EGR3. Here we report that at certain promoters,
including LH, NAB proteins display a novel ability to stimulate
EGR-directed transcription. NAB coactivation requires the conserved
NCD2 protein domain, previously implicated in NAB corepression, is
strictly dependent upon EGR binding to the LH proximal promoter and
is independent of EGR activation domains. Furthermore, we report that
NAB-activated promoters such as LH contain EGR consensus sites that
are fewer in number and lower in binding affinity than those found at
NAB-repressed promoters such as basic fibroblast growth factor.
Analysis of mutant and synthetic promoters confirms that both the
strength and multiplicity of EGR-binding sites influence the
transcriptional outcome of NAB recruitment. These results suggest a
novel means by which EGR target genes could be differentially regulated
in cells where EGR and NAB proteins are coexpressed.
*
This work was supported by National Institutes of Health
Grant 5 P01 CA49712-08 and grants from The Association for the Cure of
Cancer of the Prostate (CaP CURE) and from the Monsanto Corp.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Depts. of Pathology
and Internal Medicine, Division of Laboratory Medicine, Washington University School of Medicine, 660 South Euclid Ave., St. Louis, MO
63110. Tel.: 314-362-4651Fax number: 314-362-8756; E-mail: jeff@
milbrandt.wustl.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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