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Endocrinology Vol. 141, No. 2 571-580
Copyright © 2000 by The Endocrine Society

ARTICLES

Two Estrogen Receptor (ER) Isoforms with Different Estrogen Dependencies Are Generated from the Trout ER Gene1

Farzad Pakdel, Raphaël Métivier, Gilles Flouriot and Yves Valotaire

Equipe d’Endocrinologie Moléculaire de la Reproduction, UPRES-A Centre National de la Recherche Scientifique 6026, Université de Rennes I, 35042 Rennes, France

Address all correspondence and requests for reprints to: Dr. Farzad Pakdel, Equipe d’Endocrinologie Moléculaire de la Reproduction, UPRES-A Centre National de la Recherche Scientifique 6026, Université de Rennes I, 35042 Rennes Cedex, France. E-mail: farzad.pakdel{at}univ-rennes1.fr

A characteristic of all estrogen receptors (ER) cloned from fish to date is the lack of the first 37–42 N-terminal amino acids specific to the A domain. Here we report the isolation and characterization from trout ovary of a full-length complementary DNA (cDNA) clone encoding an N-terminal variant form of the rainbow trout ER (rtER). Sequence analysis of open reading frame of this cDNA predicts a 622-amino acid protein. The C-terminal region of this protein, from amino acid position 45 to the end, was very similar to the previously reported rtER (referred to as the short form, or rtERS). In contrast, this novel rtER cDNA (referred to as the long form, or rtERL) contains an additional in-frame ATG initiator codon that adds 45 residues to the N-terminal region of the protein. This new N-terminal region may represent the A domain of ER found in tetrapod species. The first 227 bp of this new cDNA were similar to the 3'-end intronic sequence of the rtER gene intron 1. These data together with S1 nuclease, primer extension, and RT-PCR experiments demonstrate that the rtERL represents a second isoform of rtER that arises from an alternative promoter within the first intron of the gene. Transcripts encoding both rtER forms were expressed in the liver. In vitro translation of the rtERL cDNA produced 2 proteins with molecular masses of 71 and 65 kDa, whereas rtERS cDNA produced 1 65-kDa protein. Interestingly, Western blot analysis with a specific antibody against the C-terminal region of rtER revealed 2 receptor forms of 65 and 71 kDa in trout liver nuclear extracts, in agreement with the presence of the 2 distinct classes of rtER messenger RNA in this tissue. Functional analysis of both rtER isoforms revealed that although rtERS consistently exhibited a basal (estrogen-independent) trans-activation activity that could be further increased in the presence of estrogens, the novel isoform rtERL is characterized by a strict estrogen-dependent transcriptional activity. These data suggest that the additional 45 residues at the N-terminal region of rtERL clearly modify the hormone-independent trans-activation function of the receptor.




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