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Publication : The different activities of the two activation domains of the Brn-3a transcription factor are dependent on the context of the binding site.

First Author  Budhram-Mahadeo V Year  1996
Journal  J Biol Chem Volume  271
Issue  15 Pages  9108-13
PubMed ID  8621561 Mgi Jnum  J:235271
Mgi Id  MGI:5795831 Doi  10.1074/jbc.271.15.9108
Citation  Budhram-Mahadeo V, et al. (1996) The different activities of the two activation domains of the Brn-3a transcription factor are dependent on the context of the binding site. J Biol Chem 271(15):9108-13
abstractText  The POU (Pit-Oct-Unc) family transcription factor Brn-3a contains two distinct activation domains, one at the N terminus of the molecule and one at the C terminus coincident with the DNA binding domain. These different activation domains have been shown previously to differ in their ability to activate an artificial test promoter containing a Brn-3a binding site and the naturally occurring alpha-internexin gene promoter. Here we identify the target site for Brn-3a in the alpha-internexin gene promoter and show that it can confer responsiveness to Brn-3a on a heterologous promoter. One of the single-stranded DNA sequences derived from either this novel Brn-3a binding site or from the previously characterized site in the test promoter are shown to bind Brn-3a preferentially compared with the complementary single strand or the corresponding double-stranded sequence. The pattern of responsiveness of these two sequences when cloned upstream of the same test promoter and co-transfected with constructs encoding various portions of Brn-3a indicates that the activity of the two Brn-3a activation domains is dependent upon differences in the context of the target sequence in each promoter rather than on differences in the target sequence itself.
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