Substitution of Ala564 in the first zinc cluster of the deoxyribonucleic acid (DNA)-binding domain of the androgen receptor by Asp, Asn, or Leu exerts differential effects on DNA binding

Endocrinology
H T BrüggenwirthA O Brinkmann

Abstract

In the androgen receptor of a patient with androgen insensitivity, the alanine residue at position 564 in the first zinc cluster of the DNA-binding domain was substituted by aspartic acid. In other members of the steroid receptor family, either valine or alanine is present at the corresponding position, suggesting the importance of a neutral amino acid residue at this site. The mutant receptor was transcriptionally inactive, which corresponded to the absence of specific DNA binding in gel retardation assays, and its inactivity in a promoter interference assay. Two other receptor mutants with a mutation at this same position were created to study the role of position 564 in the human androgen receptor on DNA binding in more detail. Introduction of asparagine at position 564 resulted in transcription activation of a mouse mammary tumor virus promoter, although at a lower level compared with the wild-type receptor. Transcription activation of an (ARE)2-TATA promoter was low, and binding to different hormone response elements could not be visualized. The receptor with a leucine residue at position 564 was as active as the wild-type receptor on a mouse mammary tumor virus promoter and an (ARE)2-TATA promoter, but interacted differen...Continue Reading

References

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Citations

Apr 15, 2011·The Journal of Biological Chemistry·James Robert Krycer, Andrew John Brown
Mar 19, 2016·Andrology·G C ShuklaS Gupta
Jun 5, 2004·Molecular Endocrinology·Hendrikus J DubbinkJan Trapman
Nov 5, 2013·Modern Pathology : an Official Journal of the United States and Canadian Academy of Pathology, Inc·Jana Kaprova-PleskacovaLeendert H J Looijenga
Apr 12, 2019·International Journal of Environmental Research and Public Health·Lucia LanciottiSusanna Esposito
Sep 6, 2005·Journal of Cell Science·Pascal FarlaAdriaan B Houtsmuller

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