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J. Biol. Chem., Vol. 276, Issue 21, 18146-18152, May 25, 2001
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From the Department of Human Biological Chemistry and Genetics,
University of Texas Medical Branch, Galveston, Texas 77555
The activation domains of many transcription
factors appear to exist naturally in an unfolded or only partially
folded state. This seems to be the case for AF1/tau1, the major
transactivation domain of the human glucocorticoid receptor. We show
here that in buffers containing the natural osmolyte trimethylamine
N-oxide (TMAO), recombinant AF1 folds into more a compact
structure, as evidenced by altered fluorescence emission, circular
dichroism spectra, and ultracentrifugal analysis. This conformational
transition is cooperative, a characteristic of proteins folding to
natural structures. The structure resulting from incubation in TMAO
causes the peptide to resist proteolysis by trypsin, chymotrypsin,
endoproteinase Arg-C and endoproteinase Gluc-C. Ultracentrifugation
studies indicate that AF1/tau1 exists as a monomer in aqueous solution
and that the presence of TMAO does not lead to oligomerization or
aggregation. It has been suggested that recombinant AF1 binds both the
ubiquitous coactivator CBP and the TATA box-binding protein, TBP.
Interactions with both of these are greatly enhanced in the presence of
TMAO. Co-immunoadsorption experiments indicate that in TMAO each of these and the coactivator SRC-1 are found complexed with AF1. These
data indicate that TMAO induces a conformation in AF1/tau1 that is
important for its interaction with certain co-regulatory proteins.
The Conformation of the Glucocorticoid Receptor AF1/tau1 Domain
Induced by Osmolyte Binds Co-regulatory Proteins*
*
This work was supported by NCI Grant 5RO1 CA 41407 and
NIDDKD Grant 1R01 DK58829-01 from the National Institutes of Health (to
E. B. T.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of
Human Biological Chemistry and Genetics, University of Texas Medical Branch, 301 University Blvd., 605 Basic Science Bldg., Galveston, TX
77555-0645. Tel.: 409-772-2271; Fax: 409-772-5159; E-mail: bthompso@utmb.edu.
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