Interaction of androgen and glucocorticoid receptor DNA-binding domains with their response elements |
| |
| Authors: | P. De Vos F. Claessens B. Peeters W. Rombauts W. Heyns G. Verhoeven |
| |
| Affiliation: | 1. Departamento de Biodiversidad y Biología Experimental, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires, Argentina;2. Instituto de Biodiversidad y Biología Experimental y Aplicada (IBBEA), CONICET-UBA, Buenos Aires, Argentina;3. Institute of Systematics and Ecology of Animals Siberian Branch, Russian Academy of Sciences, 11 Frunze St., Novosibirsk 630091, Russia;4. Tomsk State University, 36 Lenin Ave., Tomsk 634050, Russia;5. Instituto Tecnológico de Chascomús (CONICET-UNSAM), Chascomús, Argentina;6. Institut de Recerca i Tecnologia Agroalimentaries, Centre de Sant Carles de la Ràpita (IRTA-SCR), Crta. Poble Nou km 5.5, 43540 Sant Carles de la Ràpita, Spain;1. Institute for Marine and Antarctic Studies (IMAS), University of Tasmania, TAS, Australia;2. Inland Fisheries and Services (IFS), TAS, Australia |
| |
| Abstract: | Fusion proteins containing the glucocorticoid and the androgen receptor DNA-binding domain (ARF1 and GRF1) were produced in Escherichia coli. DNAse I footprinting was used to compare the interaction of these proteins with responsive elements (REs) in a typically glucocorticoid-responsive gene (mouse mammary tumour virus (MMTV)) and in an androgen-responsive gene (the C3(l) gene of rat prostatic binding protein). It is demonstrated that response elements which most closely resemble the consensus sequence show identical footprinting patterns for ARF1 and GRF1. The protected regions suggest that these sequences are occupied by two DNA-binding domains (DBDs) forming a dimer. Regions that constitute imperfect RE sequences, however, are apparently recognized by only one DBD, which mainly protects the TGTTCT motif. At these REs, the protection patterns produced by ARF1 and GRF1 are not identical. In the long terminal repeat (LTR) of MMTV but not in C3(1), a mechanism other than classical dimer formation seems to increase the affinity of ARF1 and GFR1 for these imperfect REs. |
| |
| Keywords: | Androgen receptor Glucocorticoid receptor DNA-binding domain Responsive element |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
