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J Biol Chem, Vol. 274, Issue 27, 19281-19285, July 2, 1999

Binding Studies with Mutants of Zif268
CONTRIBUTION OF INDIVIDUAL SIDE CHAINS TO BINDING AFFINITY AND SPECIFICITY IN THE Zif268 ZINC FINGER-DNA COMPLEX

Monicia Elrod-Erickson and Carl O. Pabo^¶

From the  Department of Biology and the ^¶ Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139

The Zif268 zinc finger-DNA complex has served as a model system for understanding how Cys₂His₂ type zinc fingers recognize DNA. Structural studies of the Zif268-DNA complex revealed that residues at four positions in the  helix of each zinc finger play key roles in recognition, but there has been no information about the precise contributions of individual residues. Here we report the results of binding studies involving five mutants of Zif268 that have changes in the base-contacting residues of finger one. These studies let us evaluate the contributions that Arg¹⁸ (position 1 of the  helix), Asp²⁰ (position 2), Glu²¹ (position 3), and Arg²⁴ (position 6) make to the overall energy of DNA binding. Our results confirm the important role played by these arginines. By comparing the affinities of the wild type and mutant peptides for various sites, we also prove that Asp²⁰ and Glu²¹ play important roles in determining binding site specificity.

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