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Departments of Medicine (R.J.G.H.) and Biochemistry (M.B., J.G.A.S, R.J.G.H.) University of Ottawa Ottawa Civic Hospital Loeb Research Institute Ottawa, Ontario, Canada K1Y 4E9
We report glucocorticoid-dependent induction of
transcription from the herpes simplex virus thymidine kinase gene
promoter proximal regulatory region in the absence of glucocorticoid
response elements and independent of the ability of
glucocorticoid receptor (GR) to bind DNA. Examination of the thymidine
kinase promoter localized glucocorticoid responsiveness to a binding
site for CCAAT enhancer-binding proteins (C/EBPs). Further analysis
indicated that GR specifically potentiated the induction of
transcription by C/EBPß, but not C/EBP
or 
, and that full
induction could be obtained by the ligand-binding domain (LBD) of GR
alone. C/EBPß, but not C/EBP or , reciprocally potentiated
transcriptional activation by DNA-bound GR LBD. However, C/EBPß was
unable to increase activation by a GR LBD with a short C-terminal
truncation, indicating that the functional interaction between the two
factors was dependent upon the GR AF-2. Surprisingly, despite the
specificity in functional effects, all three C/EBPs bound
indistinguishably to GR in GST pull-down and immunoprecipitation
assays. Indeed, several nuclear receptors, including the estrogen
(ER), progesterone, retinoic acid (RAR), and androgen receptors,
displayed a similar potential to bind C/EBPs. Previous reports have
demonstrated that ER and RARs repress transcriptional activation by
C/EBPß in ways that were dependent on their related AF-2 functions.
Therefore, the GR AF-2 may encode functional features that distinguish
the transcriptional regulatory potential of GR from that of ER and RAR.
Finally, C/EBP binding mapped to the GR DNA-binding domain, which was
not required for functional interaction with C/EBPß. Thus, the
potentiation of C/EBPß-mediated transcription by GR would appear to
require the presence of an intermediary factor.
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