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Science 22 January 1993:
Vol. 259. no. 5094, pp. 510 - 513
DOI: 10.1126/science.8424173
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Articles

Science, Vol 259, Issue 5094, 510-513
Copyright © 1993 by American Association for the Advancement of Science

articles

Altered specificity of DNA-binding proteins with transition metal dimerization domains

B Cuenoud and A Schepartz

Department of Chemistry, Yale University, New Haven, CT 06511-8118.

The bZIP motif is characterized by a leucine zipper domain that mediates dimerization and a basic domain that contacts DNA. A series of transition metal dimerization domains were used to alter systematically the relative orientation of basic domain peptides. Both the affinity and the specificity of the peptide-DNA interaction depend on domain orientation. These results indicate that the precise configuration linking the domains is important; dimerization is not always sufficient for DNA binding. This approach to studying the effect of orientation on protein function complements mutagenesis and could be used in many systems.


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