Multiple and cooperative trans-activation domains of the human glucocorticoid receptor

Cell. 1988 Dec 2;55(5):899-906. doi: 10.1016/0092-8674(88)90145-6.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Cloning, Molecular
  • DNA / metabolism
  • DNA Mutational Analysis
  • DNA-Binding Proteins / physiology*
  • Humans
  • In Vitro Techniques
  • Molecular Sequence Data
  • Promoter Regions, Genetic
  • Receptors, Glucocorticoid / physiology*
  • Transcription Factors / physiology*
  • Transcription, Genetic


  • DNA-Binding Proteins
  • Receptors, Glucocorticoid
  • Transcription Factors
  • DNA