The N-terminal transactivation domain of rat estrogen receptor is localized in a hydrophobic domain of eighty amino acids.
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.
Department of Biochemistry, Faculty of Medicine, University of Tokyo.
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Imakado
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Koike
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Kondo
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Sakai
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Muramatsu
D000818:Animals; D001483:Base Sequence; D015500:Chloramphenicol O-Acetyltransferase / Q000235:genetics; D002872:Chromosome Deletion; D004247:DNA / Q000235:genetics; D008969:Molecular Sequence Data; D009154:Mutation; D010957:Plasmids; D051381:Rats; D011960:Receptors, Estrogen / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D015533:Transcriptional Activation; D014162:Transfection
D011960:Receptors, Estrogen; D004247:DNA; D015500:Chloramphenicol O-Acetyltransferase