Abstract
The structure of the globular domain of chicken histone H1 was compared here with that of the DNA-binding homeodomain in the Drosophila Antp protein, and they were observed to display considerable similarity. Both of them consist of three or four α-helices separated by well-defined turns. Charged residues in the aminoterminal end of α3 are therefore suggested to be responsible for sequence-specific recognition of DNA by the histone. In addition, α2 of H1, with a short leucine zipper in it, may be capable of protein-protein interaction in a similar manner to the other homeodomains.
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