CD spectra show the relational style between Zic-, Gli-, Glis-zinc finger protein and DNA

Zic family proteins have five C2H2-type zinc finger motifs. The Zic-zinc finger domains show high homology to the corresponding domains of the Gli and Glis families, which also contain five C2H2-type zinc finger motifs. The zinc finger motifs of the proteins of these three protein families form an α-helix conformation in solution. The addition of oligo DNA that included a Gli-binding sequence increased the α-helix content estimated by using circular dichroism spectroscopy. Comparison of the Zic-, Gli-, and Glis-zinc fingers indicated that the α-helix content after the addition of oligo DNA correlated well with the affinity of each zinc finger for the oligo DNA (correlation coefficient, 0.85). The importance of the zinc ion for protein folding was reflected in a reduction in the α-helix content upon removal of the zinc ion. Owing to the compact globular structure, the α-helix structure of the proteins of these three protein families is extremely thermally stable. These results suggest that the α-helix structure is important for DNA binding and profoundly related to functional and structural diversity among the three families.