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Volume 270, Number 50, Issue of December 15, 1995 pp. 29983-29990
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Evidence for an Anti-parallel Orientation of the Ligand-activated Human Androgen Receptor Dimer

(Received for publication, June 8, 1995; and in revised form, September 20, 1995)

Elizabeth Langley , ,  Zhoug-xun Zhou , ,  Elizabeth M. Wilson

Domain interactions of the human androgen receptor (AR) dimer were investigated using a protein-protein interaction assay in which the NH(2)- and carboxyl-terminal regions of human AR were fused to the Saccharomyces cerevisiae GAL4 DNA-binding domain and herpes simplex virus VP16 transactivation domain to produce chimeric proteins. Transcriptional activation of a GAL4 luciferase reporter vector up to 100-fold was greater than Fos/Jun leucine zipper binding, indicating stable AR interaction between AR NH(2)-terminal residues 1-503 and steroid-binding domain residues 624-919 that was specific for and dependent on androgen binding to the steroid-binding domain and was inhibited by anti-androgen binding. Deletion mutagenesis within the NH(2)-terminal region indicated transactivation domain residues 142-337 were not required for dimerization, whereas deletions near the NH(2) terminus (Delta14-150) or NH(2)-terminal to the DNA-binding domain (Delta339-499) reduced or eliminated the AR interaction, respectively. An NH(2)-/NH(2)-terminal interaction was also observed, but no interaction was detected between ligand-free or bound steroid-binding domains. The results indicate that high affinity androgen binding promotes interactions between the NH(2)-terminal and steroid-binding domains of human AR, raising the possibility of an androgen-induced anti-parallel AR dimer.



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