title: Multiple and cooperative trans-activation domains of the human glucocorticoid receptor.
abstract: A 30 amino acid peptide (referred to as tau 2) that functions as an activation domain has been localized in the carboxyl terminus of the human glucocorticoid receptor. This sequence, when fused to yeast GAL4 as part of the ligand binding domain, generates a hormone-inducible activator. Tau 2 functions in a position-independent fashion and leads to a progressive gain of function when multimerized. A similar and independent activity has also been identified in the amino terminus of the receptor. These two sequences, although structurally unrelated, are both acidic in character and thus may have certain properties in common with yeast activator sequences.
authors.affiliation: Howard Hughes Medical Institute, Salk Institute for Biological Studies, La Jolla, California.
authors.forename: S M
authors.initials: SM
authors.lastname: Hollenberg
authors.forename: R M
authors.initials: RM
authors.lastname: Evans
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D003001:Cloning, Molecular; D004247:DNA / Q000378:metabolism; D004252:DNA Mutational Analysis; D004268:DNA-Binding Proteins / Q000502:physiology*; D006801:Humans; D066298:In Vitro Techniques; D008969:Molecular Sequence Data; D011401:Promoter Regions, Genetic; D011965:Receptors, Glucocorticoid / Q000502:physiology*; D014157:Transcription Factors / Q000502:physiology*; D014158:Transcription, Genetic
chemical_list: D004268:DNA-Binding Proteins; D011965:Receptors, Glucocorticoid; D014157:Transcription Factors; D004247:DNA