title: Transcriptional regulation by competition between ELP isoforms and nuclear receptors.
abstract: ELP is a transcription factor belonging to the nuclear receptor superfamily. The consensus binding sequence for ELP contains a half site of the nuclear receptor recognition element. We demonstrated previously that ELP1, the repressor type isoform of ELP, competes for binding with the retinoic acid receptor and represses retinoic acid-induced transactivation. In this study, competitive repression by ELP1 was investigated for several other nuclear receptors. As in the case of the retinoic acid receptor, binding of vitamin D receptor, thyroid hormone receptor, and estrogen receptor could be competed by ELP1, resulting in repression of their ligand-dependent transactivation. Interestingly, the activator-type ELP isoforms were capable of repressing retinoic acid-induced transactivation through binding to the retinoic acid receptor binding element. These data suggest that competition for target DNA binding is a general mechanism of transcriptional repression by ELP isoforms.
authors.affiliation: Department of Molecular Pathology, Research Institute for Radiation Biology and Medicine, Hiroshima University, Kasumi, Mimami-ku, Japan.
authors.forename: N
authors.initials: N
authors.lastname: Kotomura
authors.forename: Y
authors.initials: Y
authors.lastname: Ninomiya
authors.forename: K
authors.initials: K
authors.lastname: Umesono
authors.forename: O
authors.initials: O
authors.lastname: Niwa
mesh_terms: D016475:3T3 Cells; D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D001667:Binding, Competitive; D019556:COS Cells; D015500:Chloramphenicol O-Acetyltransferase / Q000096:biosynthesis; D004268:DNA-Binding Proteins / Q000096:biosynthesis / Q000378:metabolism*; D005786:Gene Expression Regulation; D018398:Homeodomain Proteins; D006801:Humans; D008156:Luciferases / Q000096:biosynthesis; D051379:Mice; D009838:Oligodeoxyribonucleotides; D018167:Receptors, Calcitriol / Q000378:metabolism; D018160:Receptors, Cytoplasmic and Nuclear / Q000096:biosynthesis / Q000378:metabolism*; D011960:Receptors, Estrogen / Q000378:metabolism; D018168:Receptors, Retinoic Acid / Q000378:metabolism; D011988:Receptors, Thyroid Hormone / Q000378:metabolism; D011994:Recombinant Proteins / Q000096:biosynthesis; D012097:Repressor Proteins / Q000096:biosynthesis / Q000378:metabolism*; D054339:Steroidogenic Factor 1; D014157:Transcription Factors / Q000378:metabolism*; D014158:Transcription, Genetic; D014162:Transfection
chemical_list: D004268:DNA-Binding Proteins; D018398:Homeodomain Proteins; D009838:Oligodeoxyribonucleotides; D018167:Receptors, Calcitriol; D018160:Receptors, Cytoplasmic and Nuclear; D011960:Receptors, Estrogen; D018168:Receptors, Retinoic Acid; D011988:Receptors, Thyroid Hormone; D011994:Recombinant Proteins; D012097:Repressor Proteins; D054339:Steroidogenic Factor 1; D014157:Transcription Factors; D008156:Luciferases; D015500:Chloramphenicol O-Acetyltransferase