Differential DNA binding by calf uterine estrogen and progesterone receptors results from differences in oligomeric states

Biochemistry ◽  
1991 ◽  
Vol 30 (25) ◽  
pp. 6148-6154 ◽  
Author(s):  
D. F. Skafar
2005 ◽  
Vol 34 (3) ◽  
pp. 603-615 ◽  
Author(s):  
Jacqueline Brodie ◽  
Iain J McEwan

The androgen receptor (AR) is a ligand-activated transcription factor that recognises and binds to specific DNA response elements upon activation by the steroids testosterone or dihydrotestosterone. In vitro, two types of response element have been characterised - non-selective elements that bind the androgen, glucocorticoid and progesterone receptors, and androgen receptor-selective sequences. In the present study, the allosteric effects of DNA binding on the receptor amino-terminal domain (NTD) were studied. Binding to both types of DNA response element resulted in changes in the intrinsic fluorescence emission spectrum for four tryptophan residues within the AR-NTD and resulted in a more protease-resistant conformation. In binding experiments, it was observed that the presence of the AR-NTD reduced the affinity of receptor polypeptides for binding to both selective and non-selective DNA elements derived from the probasin, PEM and prostatin C3 genes respectively, without significantly altering the protein–base pair contacts. Taken together, these results highlight the role of intra-domain communications between the AR-NTD and the DNA binding domain in receptor structure and function.


2002 ◽  
Vol 441 (4) ◽  
pp. 328-334 ◽  
Author(s):  
Peter Regitnig ◽  
Angelika Reiner ◽  
Hans-Peter Dinges ◽  
Gerald Höfler ◽  
Elisabeth Müller-Holzner ◽  
...  

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