Novel interaction at the Cdx-2 binding sites of the lactase-phlorizin hydrolase promoter.

@article{Wering2002NovelIA,
  title={Novel interaction at the Cdx-2 binding sites of the lactase-phlorizin hydrolase promoter.},
  author={Herbert M. van Wering and Leah Moyer and Richard J. Grand and Stephen D. Krasinski},
  journal={Biochemical and biophysical research communications},
  year={2002},
  volume={299 4},
  pages={587-93}
}
Cdx-2 is an intestine-specific homeodomain-containing transcription factor that activates the promoters of intestinal genes through specific interactions with the consensus, TTTAT/C. Here, we demonstrate that Cdx-2 interacts with the lactase-phlorizin hydrolase (LPH) promoter at cis-element (CE)-LPH1a (-54 to -40 bp) as well as the LPH TATA-box. Affinity comparisons between SIF-1, CE-LPH1a, and the LPH TATA-box revealed that the TATA-box has the lowest affinity for Cdx-2. Characterization of CE… CONTINUE READING

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