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J Biol Chem, Vol. 274, Issue 5, 3182-3188, January 29, 1999
From the Second Department of Internal Medicine, The glucocorticoid receptor (GR) is considered to
belong to a class of transcription factors, the functions of which are
exposed to redox regulation. We have recently demonstrated that
thioredoxin (TRX), a cellular reducing catalyst, plays an important
role in restoration of GR function in vivo under oxidative
conditions. Although both the ligand binding domain and other domains
of the GR have been suggested to be modulated by TRX, the molecular
mechanism of the interaction is largely unknown. In the present study,
we hypothesized that the DNA binding domain (DBD) of the GR, which is
highly conserved among the nuclear receptors, is also responsible for
communication with TRX in vivo. Mammalian two-hybrid assay and glutathione S-transferase pull-down assay revealed the
direct association between TRX and the GR DBD. Moreover, analysis of subcellular localization of TRX and the chimeric protein harboring herpes simplex viral protein 16 transactivation domain and the GR DBD
indicated that the interaction might take place in the nucleus under
oxidative conditions. Together these observations indicate that TRX,
via a direct association with the conserved DBD motif, may represent a
key mediator operating in interplay between cellular redox signaling
and nuclear receptor-mediated signal transduction.
Direct Association with Thioredoxin Allows Redox Regulation of
Glucocorticoid Receptor Function
, Department of Anesthesia,
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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