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J. Biol. Chem., Vol. 265, Issue 25, 14763-14769, 09, 1990
AP Wright, J Carlstedt-Duke and JA Gustafsson
In this study we have reconstituted transactivation of gene expression by
the human glucocorticoid receptor in the yeast, Saccharomyces cerevisiae.
We have expressed the C-terminal half of the human glucocorticoid receptor
(residues 415-777), the smallest derivative that can be expected to
function as a ligand-dependent activator of transcription, in yeast cells.
The function of the expressed protein has been assayed using a reporter
gene consisting of the beta- galactosidase gene from Escherichia coli fused
to the yeast iso-1- cytochrome c promoter with a glucocorticoid-responsive
element from the rat tyrosine aminotransferase gene upstream.
Transactivation of expression from the reporter gene by the expressed
receptor is seen only in the presence of steroid hormones with
glucocorticoid activity and occurs via specific interaction of receptor
with the glucocorticoid- responsive element upstream of the reporter gene.
This result is different from those obtained for the estrogen receptor in
which a similar derivative was not functional in yeast. This suggests that
the well documented conservation of structure and function between steroid
receptors may not extend to the transactivation domains. Our results also
suggest that the mechanism by which receptors are sequestered in an
inactive, non-DNA binding state in the absence of ligand may be
functionally conserved in yeast. In support of this we show evidence that
the expressed receptor is associated with the yeast molecular weight 90,000
heat shock protein as seen in mammalian cells.
Ligand-specific transactivation of gene expression by a derivative of the human glucocorticoid receptor expressed in yeast
Department of Medical Nutrition, Karolinska Institute, Huddinge University Hospital, Sweden.
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