POU domain factors of the Brn-3 class recognize functional DNA elements which are distinctive, symmetrical, and highly conserved in evolution.

@article{Gruber1997POUDF,
  title={POU domain factors of the Brn-3 class recognize functional DNA elements which are distinctive, symmetrical, and highly conserved in evolution.},
  author={Carol A Gruber and Jerry M. Rhee and Anatoli S. Gleiberman and Eric E. Turner},
  journal={Molecular and cellular biology},
  year={1997},
  volume={17 5},
  pages={
          2391-400
        }
}
To better understand the diversity of function within the POU domain class of transcriptional regulators, we have determined the optimal DNA recognition site of several proteins of the POU-IV (Brn-3) subclass by random oligonucleotide selection. The consensus recognition element derived in this study, ATAATTAAT, is clearly distinct from octamer sites described for the POU factor Oct-1. The optimal POU-IV site determined here also binds Brn-3.0 with significantly higher affinity than consensus… CONTINUE READING
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