A Conditional Version of the Ets Transcription Factor Erm by Fusion to the Ligand Binding Domain of the Oestrogen Receptor

The fusion of a wide range of proteins to the ligand-binding domain of nuclear receptors has been shown to impart ligand-dependent inducible activity of the resulting chimera. Transcriptional regulators of the ETS family are involved in both normal and oncogenic processes. In order to address the ro...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 1997-10, Vol.239 (1), p.252-256
Main Authors: Pelczar, Hélène, Albagli, Olivier, Chotteau-Lelievre, Anne, Damour, Isabelle, de Launoit, Yvan
Format: Article
Language:English
Subjects:
Binding Sites
Chimera
DNA-Binding Proteins - genetics
DNA-Binding Proteins - metabolism
EM-139
Erm
Ets
HeLa Cells
Humans
Ligands
oestrogen receptor
Receptors, Estrogen - genetics
Receptors, Estrogen - metabolism
Recombinant Fusion Proteins - metabolism
transcription factor
Transcription Factors - genetics
Transcription Factors - metabolism
Transcription, Genetic
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Summary:The fusion of a wide range of proteins to the ligand-binding domain of nuclear receptors has been shown to impart ligand-dependent inducible activity of the resulting chimera. Transcriptional regulators of the ETS family are involved in both normal and oncogenic processes. In order to address the role of Erm, a “PEA3subgroup” member of this family, we generated a chimera between Erm and the widely used ligand-binding domain of the oestrogen receptor (ER). The chimera, ErmER, consists of Erm protein fused at its C-terminal end to the ER domain. We show that ErmER displays a ligand-dependent transcriptional activity onetsresponsive elements. The efficiency of ErmER mediated transactivation is modulated by the hormone concentration while its weak leakiness is reduced by using the steroidal anti-oestrogen EM-139. Our results define ErmER as the first conditional version of an Ets transcription factor, providing a useful tool to decipher Erm biological role and to identify potential Erm target genes.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.1997.7363