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Originally published In Press as doi:10.1074/jbc.M201003200 on March 14, 2002

J. Biol. Chem., Vol. 277, Issue 22, 20079-20086, May 31, 2002
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Conformational Analysis of the Androgen Receptor Amino-terminal Domain Involved in Transactivation
INFLUENCE OF STRUCTURE-STABILIZING SOLUTES AND PROTEIN-PROTEIN INTERACTIONS*

James ReidDagger §, Sharon M. Kelly, Kate WattDagger , Nicholas C. Price, and Iain J. McEwanDagger ||

From the Dagger  Department of Molecular and Cell Biology, Institute of Medical Sciences, University of Aberdeen, Foresterhill, Aberdeen AB25 2ZD, Scotland, United Kingdom and  IBLS Division of Biochemistry and Molecular Biology, Joseph Black Building, University of Glasgow, Glasgow G12 8QQ, Scotland, United Kingdom

The androgen receptor (AR) is a member of the nuclear receptor superfamily. Sequences within the large amino-terminal domain of the receptor have been shown to be important for transactivation and protein-protein interactions; however, little is known about the structure and folding of this region. In the present study we show that a 344-amino acid polypeptide representing the main determinants for transactivation has the propensity to form alpha -helical structure and that mutations which disrupt putative helical regions alter conformation. Folding of the AR was observed in the presence of the helix-stabilizing solvent trifluoroethanol and the natural osmolyte trimethylamine N-oxide (TMAO). TMAO resulted in the movement of two tryptophan residues to a less solvent-exposed environment and the formation of secondary/tertiary structure resistant to protease cleavage. Critically, binding to the RAP74 subunit of the general transcription factor TFIIF resulted in extensive protease resistance, consistent with induced folding of the receptor transactivation domain. These data indicate that this region of the AR is structurally flexible and folds into a stable conformation upon interactions with a component of the general transcription machinery.

* This work was supported in part by Biotechnology and Biological Sciences Research Council Grant 1/C10407.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.

§ Supported by a three-year Biotechnology and Biological Sciences Research Council Ph.D. studentship.

|| To whom correspondence should be addressed. Tel.: 44-1224-273107; Fax: 44-1224-273144; E-mail: iain.mcewan@abdn.ac.uk.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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