title: A single-stranded DNA-binding protein promotes the binding of the purified oestrogen receptor to its responsive element.
abstract: The purified human oestrogen receptor (hER) does not form a detectable complex with an oestrogen responsive element (ERE) under conditions where hER-ERE complexes are readily formed with crude extracts from Hela or yeast cells expressing the hER. This indicates that other factor(s) are necessary for ER-ERE binding. Such a ER DNA binding stimulatory factor (DBSF) has been purified from the yeast Saccharomyces cerevisiae. It is a 45 kDa single-stranded DNA-binding protein (SSB) which cannot be substituted for by the purified E. coli SSB.
authors.affiliation: Laboratoire de Génétique Moléculaire, CNRS, l'INSERM, Faculté de Médecine, Strasbourg, France.
authors.forename: R
authors.initials: R
authors.lastname: Mukherjee
authors.forename: P
authors.initials: P
authors.lastname: Chambon
mesh_terms: D001483:Base Sequence; D004277:DNA, Single-Stranded / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000378:metabolism*; D006367:HeLa Cells; D006801:Humans; D008969:Molecular Sequence Data; D011960:Receptors, Estrogen / Q000378:metabolism*; D012045:Regulatory Sequences, Nucleic Acid; D012441:Saccharomyces cerevisiae / Q000378:metabolism*
chemical_list: D004277:DNA, Single-Stranded; D004268:DNA-Binding Proteins; D011960:Receptors, Estrogen