The N-terminal transactivation domain of rat estrogen receptor is localized in a hydrophobic domain of eighty amino acids |
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Authors: | S Imakado S Koike S Kondo M Sakai M Muramatsu |
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Affiliation: | Department of Biochemistry, Faculty of Medicine, University of Tokyo. |
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Abstract: | In order to determine the transactivation domain(s) of the rat estrogen receptor (rat ER), we made a number of rat ER deletion mutants and transfected the mutant plasmids into COS7 cells together with an estrogen-responsive reporter plasmid, ERE-tk(197)-CAT, which contained the estrogen response element of Xenopus vitellogenin A2 gene. We have identified and localized the N-terminal transactivation domain of the rat ER to a hydrophobic region extending from Ala 59 to Glu 140. |
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