Reference : Multiple domains of the glucocorticoid receptor involved in synergism with the CACCC ...
Scientific journals : Article
Life sciences : Genetics & genetic processes
Multiple domains of the glucocorticoid receptor involved in synergism with the CACCC box factor(s).
Muller, Marc mailto [Université de Liège - ULiège > Département des sciences de la vie > GIGA-R : Biologie et génétique moléculaire >]
Baniahmad, C. [> > > >]
Kaltschmidt, C. [> > > >]
Renkawitz, R. [> > > >]
Molecular Endocrinology
Endocrine Society
Yes (verified by ORBi)
Chevy Chase
[en] Animals ; Base Sequence ; Binding Sites ; Cell Line ; Chromosome Deletion ; DNA-Binding Proteins/metabolism ; Fungal Proteins/genetics/metabolism ; Genetic Vectors ; Kinetics ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Plasmids ; Receptors, Glucocorticoid/genetics/metabolism ; Recombinant Fusion Proteins/metabolism ; Regulatory Sequences, Nucleic Acid ; Saccharomyces cerevisiae Proteins ; Transcription Factors/metabolism
[en] Steroid induction of responsive genes functions through the synergistic activity of steroid receptor-binding sequences with adjacent transcription factor-binding sites. To analyze the mechanism of synergy we tested different human glucocorticoid receptor mutants for synergistic function with another transcription factor in comparison with intrinsic trans-activation obtained with a single receptor binding site (glucocorticoid response element). Multiple domains were found to be involved in synergistic activity of the glucocorticoid receptor with the CACCC box factor. Deletions within the N-terminal receptor half affected simultaneously intrinsic trans-activation and synergism. However, deletion of the hormone-binding domain mainly impaired synergism rather than intrinsic trans-activation, clearly showing that this domain synergizes by a mechanism independent of intrinsic activation. A chimeric protein where the DNA-binding domain of the glucocorticoid receptor was replaced by that of the yeast GAL4 protein also showed functional synergism. These data suggest that some of the receptor domains outside the DNA-binding domain synergize by their intrinsic trans-activating property, but the hormone-binding domain contributes to synergism by a different mechanism.

File(s) associated to this reference

Fulltext file(s):

Open access
MullerSynSubdomainsMolEndo.pdfPublisher postprint736.12 kBView/Open

Bookmark and Share SFX Query

All documents in ORBi are protected by a user license.