Short Isoform of POU Factor Brn-3b Can Form a Heterodimer with Brn-3a That Is Inactive for Octamer Motif Binding

作者: Thomas Theil , Bernd Rödel , Frank Spiegelhalter , Tarik Möröy

DOI: 10.1074/JBC.270.52.30958

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摘要: Abstract The POU proteins Brn-3a and Brn-3b belong to a family of DNA binding transcription factors that share stretches extensive homology. Both are expressed as shorter longer isoforms. long form is able oncogenically transform primary fibroblasts. By contrast, the short (Brn-3b(s)) cannot fibroblasts but specifically inhibit transforming activity Brn-3a(l). Moreover, Brn-3a(l) can act transcriptional transactivator, while Brn-3b(s) not only unable do so in addition inhibits transactivating Here, we show opposite antagonistic activities due their different properties; stable complexes with several octamer-related target sequences. presence completely by preventing formation Brn-3a(l)-DNA well disrupting preformed complexes. Experiments GST fusion vitro studies suggest inhibition occurs via direct interaction two solution. Therefore, hypothesize antagonist inhibiting its through an inactive hetero-oligomeric complex.

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