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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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SKN-1 domain folding and basic region monomer stabilization upon DNA binding.
A. S. Carroll, D. E. Gilbert, X. Liu, J. W. Cheung, J. E. Michnowicz, G. Wagner, T. E. Ellenberger, and T. K. Blackwell (1997)
Genes & Dev. 11, 2227-2238
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Assembly of an active enzyme by the linkage of two protein modules.
A. E. Nixon, M. S. Warren, and S. J. Benkovic (1997)
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Cooperative dimerization of paired class homeo domains on DNA..
D Wilson, G Sheng, T Lecuit, N Dostatni, and C Desplan (1993)
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