title: Molecular cloning, structure, and expression of mouse estrogen-responsive finger protein Efp. Co-localization with estrogen receptor mRNA in target organs.
abstract: We have previously identified a human estrogen-responsive gene, efp (estrogen-responsive finger protein), which encodes a putative transcription regulator (Inoue, S., Orimo, A., Hosoi, T., Kondo, S., Toyoshima, H., Kondo, T., Ikegami, A., Ouchi, Y., Orimo, H., and Muramatsu, M. (1993) Proc. Natl. Acad. Sci. U.S.A. 90, 11117-11121). Here, we report isolation of mouse Efp cDNA and its structure containing three cysteine-rich domains (RING finger and B1 and B2 boxes), a coiled-coil domain, and a C-terminal domain. High levels of Efp mRNA were detected in uterus, ovary, and placenta by RNase protection assay. By in situ hybridization histochemistry the transcripts of efp were also detected in uterus, mammary gland, ovary, and brain, and the co-localization of Efp and estrogen receptor mRNA was particularly demonstrated in these female organs. Moreover, the level of Efp mRNA in uterus and brain, which are known as target organs for estrogen, was up-regulated in vivo by 17 beta-estradiol. Furthermore, both the Efp and estrogen receptor mRNA were stained in the brain vesicles of 11.5-day embryos by whole mount in situ hybridization. These findings raise the possibility that efp is an estrogen-responsive gene that mediates estrogen action in various target organs.
authors.affiliation: Department of Biochemistry, Saitama Medical School, Japan.
authors.forename: A
authors.initials: A
authors.lastname: Orimo
authors.forename: S
authors.initials: S
authors.lastname: Inoue
authors.forename: K
authors.initials: K
authors.lastname: Ikeda
authors.forename: S
authors.initials: S
authors.lastname: Noji
authors.forename: M
authors.initials: M
authors.lastname: Muramatsu
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001921:Brain / Q000378:metabolism; D003001:Cloning, Molecular; D003545:Cysteine; D004268:DNA-Binding Proteins / Q000096:biosynthesis* / Q000737:chemistry* / Q000235:genetics; D004622:Embryo, Mammalian; D005314:Embryonic and Fetal Development; D005260:Female; D015723:Gene Library; D006801:Humans; D017403:In Situ Hybridization; D008321:Mammary Glands, Animal / Q000378:metabolism; D051379:Mice; D008813:Mice, Inbred ICR; D008969:Molecular Sequence Data; D009928:Organ Specificity; D010053:Ovary / Q000378:metabolism; D010920:Placenta / Q000378:metabolism; D011247:Pregnancy; D017433:Protein Structure, Secondary; D015347:RNA Probes; D012333:RNA, Messenger / Q000032:analysis / Q000096:biosynthesis*; D011960:Receptors, Estrogen / Q000096:biosynthesis*; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry; D014157:Transcription Factors / Q000096:biosynthesis* / Q000737:chemistry* / Q000235:genetics; D014158:Transcription, Genetic; D000070584:Tripartite Motif Proteins; D044767:Ubiquitin-Protein Ligases; D014599:Uterus / Q000378:metabolism; D016335:Zinc Fingers
chemical_list: D004268:DNA-Binding Proteins; D015347:RNA Probes; D012333:RNA, Messenger; D011960:Receptors, Estrogen; D011994:Recombinant Proteins; D014157:Transcription Factors; C490034:Trim25 protein, mouse; D000070584:Tripartite Motif Proteins; C084523:TRIM25 protein, human; D044767:Ubiquitin-Protein Ligases; D003545:Cysteine