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Unlike nuclear receptors that form heterodimers with RXR to bind to their response element, LRH-1 regulates target genes by binding as a monomer to DNA response elements with consensus sequence 5'PyCAAGGPyCPu3' [ 7], which is similar to a "half-site" recognized by dimeric receptors.
During transcriptional activation, gene specific activators bind to their response elements and recruit the regulatory factors needed to initiate efficient RNA synthesis.
Interestingly, NFκB transcription factors bind to their response elements even if they are packaged in a nucleosome [ 53].
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Once bound to their response elements, NFκB transcription factors can recruit chromatin remodeling complexes to expose other response elements and allow the formation of the initiation complex [ 54].
NRs bind to their DNA response elements either as monomers, dimers, or heterodimers.
In the presence of retinoids, nuclear receptors bind to their respective response elements RAREs and RXREs in regulatory regions of target genes and modulate gene transcription [ 7].
These steroids bind to their receptor, activating hormone response elements and gene transcription; this subsequently activates hormone response proteins that influence cell function and differentiation (Clark et al 2002).
That is, organic chemicals typically bind to their receptor to elicit a response [41, 57].
The TR-RXRs and RAR-RXRs are also normally bound to their cognate response elements (TRE and RARE, respectively) in hormone-responsive promoters in the absence of ligand, unlike the SRs, which normally reside as quiescent monomers in the cytoplasm (GR, MR, PR, AR) or nucleus (ER) and then migrate to their respective HREs following hormone activation and dimerization.
For the steroid receptors GR and ERα, DBDs are monomers in solution and form dimers when bound to their respective response elements.
It is thus conceivable that chromatin changes associated with S phase can provide a window of opportunity for the ectopic TFs to bind their response elements.
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