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We investigated the molecular mechanisms underlying the
transcriptional silencing and the hormone-induced activation of target
genes by thyroid hormone receptor
Volume 270,
Number 18,
Issue of May 5, pp. 10601-10611, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
with the
Basal Transcription Machinery
(TR-). We developed a
cell-free transcription system containing HeLa cell nuclear extracts in
which unliganded human TR- represses basal transcription from a
promoter bearing thyroid hormone response elements. Binding of hormonal
ligand to the receptor reverses this transcriptional silencing.
Specific binding of TR- to the thyroid hormone response element at
the target promoter is crucial for silencing. Studies employing
TR- mutants indicate that the silencing activity is located within
the C-terminal rather than the N-terminal domain of the receptor. Our
studies reveal further that unliganded TR- inhibits the assembly
of a functional transcription preinitiation complex (PIC) at the target
promoter. We postulate that interaction with TR- impairs the
function(s) of one or more assembling transcriptional complexes during
the multistep assembly of a PIC. Consistent with this hypothesis, we
observe that, in the absence of thyroid hormone, TR- or a
heterodimer of TR- and retinoid-X-receptor undergoes direct
protein-protein interactions with the transcription factor IIB-TATA
binding protein complex, an early intermediate during PIC assembly.
Binding of hormone to TR- dramatically reduces the interaction
between the receptor and the transcription factor IIB-TATA binding
protein complex. We propose that the role of ligand is to facilitate
the assembly of functional PICs at the target promoter by reducing
nonproductive interactions between TR- and the initiation factors.
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