| Autor: |
Wu, Xiling, Spiro, Craig, Owen, Whyte G., McMurray, Cynthia T. |
| Zdroj: |
Journal of Biological Chemistry; August 1998, Vol. 273 Issue: 33 p20820-20827, 8p |
| Abstrakt: |
We have analyzed the properties of cAMP response element-binding protein (CREB) in solution with emphasis on dimerization and effects of phosphorylation. Using a purified CREB fusion protein, a novel dye-label technique, and sedimentation equilibrium analysis, we directly and conclusively demonstrate that, unlike Jun and Fos, CREB dimerization is DNA-dependent. CREB exists primarily as a monomer in solution and cooperatively assembles on DNA to form dimers. Sedimentation equilibrium analysis also indicates that dimerization is unaffected by cAMP-dependent protein kinase-phosphorylation or by the symmetry of the cAMP-responsive element binding site. Filter binding assays reveal that CREB binding is unaffected by phosphorylation regardless of the symmetry of the cAMP-responsive element binding site. Our results suggest that structurally similar members of the same bZIP superfamily may differ significantly in their regulation at the level of dimerization. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
|
