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J Biol Chem, Vol. 273, Issue 33, 20820-20827, August 14, 1998

cAMP Response Element-binding Protein Monomers Cooperatively Assemble to Form Dimers on DNA

Xiling WuDagger , Craig SpiroDagger , Whyte G. Owen§, and Cynthia T. McMurrayDagger §

From the Dagger  Department of Pharmacology and § Department of Biochemistry and Molecular Biology, Mayo Foundation and Graduate School, Rochester, Minnesota 55905

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.

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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