The Complete Primary Structure of Human Estrogen Receptor β (hERβ) and Its Heterodimerization with ER αin Vivoandin Vitro

Abstract

Human estrogen receptor β (hERβ) cDNA that encodes the full-length amino acid sequence has been isolated from testis poly(A)+RNA with the combination of cDNA screening and reverse transcription-PCR. It is composed of a 1590-bp open reading frame and a segment of the 5′- and 3′-untranslated region (UTR) and encodes an additional 53 amino acids in the N-terminal region compared with the previously reported one. Protein interaction between ERα and ERβ was demonstratedin vitroby GST pull-down assay andin vivoby immunoprecipitation. Thus, this study indicates that ERα and ERβ can interactin vivo,cross-signaling each other.