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Vol. 58, Issue 3, 584-590, September 2000
and 
Department of Medical Nutrition (F.D., K.P.) and Center for
Biotechnology (M.T., J.-Å.G.), NOVUM, Karolinska Institute, Huddinge,
Sweden
Human estrogen receptors 
(ER) and 
(ER) are
ligand-inducible transcription factors that are highly homologous in
their central DNA-binding and carboxyl-terminal ligand-binding domains. In contrast, there is very little conservation between ER and ER
in the amino-terminal domain. Using different human cell lines, we show
that wild-type ER transcriptional activity is lower or similar to
that of ER, depending on the cell type. Deletion of the
amino-terminal domain in both ER subtypes resulted in no or a lower
decrease of transcriptional activity of ER compared with ER,
suggesting that the ER amino-terminal domain contains a weaker
transcriptional activation function-1. Using ER and ER deletion mutants, we showed that the amino-terminal transcriptional activity of ER maps to amino acids 1-31. Interestingly, this domain
contains a six amino-acid motif (amino acids 5-10 in human ER) that
is part of the ER-activation function-1 region (amino acids 49-54
in human ER) and highly conserved among all mammalian ER
amino-terminal domains. Despite this similarity between the two ER
subtypes, no autonomous and ligand-independent activity of the
ER-amino-terminal domain was observed in yeast and mammalian cells
in contrast to ER. This study provides a molecular basis for the
difference in transcriptional activity between ER and ER and
establishes that ER contains a structurally and functionally restricted amino-terminal transcriptional activity.
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