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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Molecular interactions of steroid hormone receptor with its enhancer element: evidence for receptor dimer formation.

A steroid hormone responsive element (GRE/PRE), sufficient to confer glucocorticoid and progesterone inducibility when linked to a reporter gene, was used in band-shift assays to examine its molecular interactions with steroid hormone receptors. Both progesterone and glucocorticoid receptors bound directly and specifically to the GRE/PRE. The purine contact sites for both form A and form B chicken progesterone receptor, as well as those for rat glucocorticoid receptor, are identical. A peptide fragment produced in bacteria that primarily contain the DNA binding domain of the glucocorticoid receptor binds first to the TGTTCT half-site of the GRE/PRE, and a second molecule binds subsequently to the TGTACA (half-site) of the GRE/PRE in a cooperative manner. Utilizing the peptide fragment and the protein A-linked fragment, we demonstrated that the receptor interacts with its cognate enhancer as a dimer.[1]

References

  1. Molecular interactions of steroid hormone receptor with its enhancer element: evidence for receptor dimer formation. Tsai, S.Y., Carlstedt-Duke, J., Weigel, N.L., Dahlman, K., Gustafsson, J.A., Tsai, M.J., O'Malley, B.W. Cell (1988) [Pubmed]
 
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