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

See allHide authors and affiliations

Science  22 Jan 1993:
Vol. 259, Issue 5094, pp. 510-513
DOI: 10.1126/science.8424173


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.