Nuclear localization and DNA binding of ecdysone receptor and ultraspiracle
✍ Scribed by M.V. Cronauer; S. Braun; Ch. Tremmel; K.-D. Kröncke; M. Spindler-Barth
- Publisher
- John Wiley and Sons
- Year
- 2007
- Tongue
- English
- Weight
- 221 KB
- Volume
- 65
- Category
- Article
- ISSN
- 0739-4462
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We have prepared several truncated versions of the Choristoneura fumiferana ecdysone receptor (CfEcR) cDNA to identify domains required for heterodimerization with C. fumiferana ultraspiracle (CfUSP). The CfEcR protein containing all six domains bound to hsp27 EcRE in the presence of CfUSP protein.
The human vitamin D receptor (hVDR) possesses a unique array of five basic amino acids positioned between the two DNA-binding zinc fingers that is similar to well-characterized nuclear localization sequences in other proteins. When residues within this region are mutated to nonbasic amino acids, or