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Two Functionally Different Protein Isoforms Are Produced from the Chicken Estrogen Receptor- Gene

European Molecular Biology Laboratory (C.G., G.F., V.S-B., F.G.) D-69117, Heidelberg, Germany
National Diagnostic Centre (C.G.) University College Galway, Ireland

The existence of two forms of the chicken estrogen receptor- protein (ER-) in chicken tissues is demonstrated: the previously reported receptor (cER- form I), which has a size of 66 kDa, and a new form (cER- form II), which lacks the N-terminal 41 amino acids present in form I and thus gives rise to a protein of 61 kDa. Whereas the 66-kDa protein is the translation product of several cER- mRNAs (A1–D), the cER- protein isoform II is encoded by a new cER- mRNA (A2), which is transcribed in vivo from a specific promoter that is located in the region of the previously assigned translation start site of the cER- gene. SI nuclease mapping analysis reveals that cER- mRNA A2 is liver enriched. The resulting cER- forms I and II differ in their ability to modulate estrogen target gene expression in a promoter- and cell type-specific manner. Whereas cER- form I activates or represses in a strictly E₂-dependent manner, the truncated form is characterized by a partial transactivating or repressing activity in the absence of its ligand. Comparison of the N-terminal coding regions of different vertebrate ER- reveal a conservation of the translation start methionine of the protein ER- form II in other oviparous species but not in mammals. The expression of two classes of ER- transcripts encoding the two ER- receptor forms in the liver of Xenopus laevis and rainbow trout is demonstrated. Therefore, the existence of two functionally different protein isoforms produced from the ER- gene is probably a common and specific feature in oviparous species.

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