Molecular cloning and characterization of reptilian estrogen receptor cDNAs

• Published in: Molecular and cellular endocrinology Vol. 183; no. 1; pp. 33 - 39
• Main Authors: Sumida, Kayo, Ooe, Norihisa, Saito, Koichi, Kaneko, Hideo
• Format: Journal Article
• Language: English
• Published: Ireland Elsevier Ireland Ltd 25.10.2001
• Subjects: Alligator (caiman); Alligators and Crocodiles - genetics; Amino Acid Sequence; Animals; Base Sequence; Caiman crocodilus; Cloning, Molecular; Cnemidophorus uniparens; DNA, Complementary; Estrogen receptor; Genes, Reporter; HeLa Cells; Humans; Lizards - genetics; Male; Molecular Sequence Data; Receptors, Estrogen - chemistry; Receptors, Estrogen - genetics; Reporter gene assay; Reptilian Proteins - chemistry; Reptilian Proteins - genetics; Reverse Transcriptase Polymerase Chain Reaction; Transfection; Whiptail lizard; Reporter gene assay; Estrogen receptor; Alligator (caiman); Whiptail lizard
• ISSN: 0303-7207; 1872-8057
• DOI: 10.1016/S0303-7207(01)00613-X

cDNAs encoding alligator (caiman), Caiman crocodilus and whiptail lizard, Cnemidophorus uniparens estrogen receptors (ERs) were cloned and sequenced. This is the first report of full-length cDNA sequences for reptilian ERs, to our knowledge. The full-length alligator (caiman) ER cDNA (1764 bp, 587 amino acid residues) shows 68% amino acid homology with the full-length whiptail lizard ER cDNA (1746 bp, 581 amino acid residues). The respective ligand binding E domains have 87 and 83% amino acid homology with human ER while the DNA binding C domains show 100% amino acid homology with the human, rat and chicken forms. When the cDNAs were inserted into the pRc/RSV vector and transfected into HeLa cells with a reporter plasmid, the encoding proteins were confirmed to be functional through the interaction of the receptor–ligand complex with the estrogen responsive element (ERE).