Abstract
The E2 proteins of papillomavirus specifically bind to double-stranded DNA containing the consensus sequence ACCG-N 4-CGGT, where N is any nucleotide. Here, we show the binding and recognition of dissimilar DNA sequences by an 18 amino-acid peptide (α1E2), which corresponds to the DNA-recognition helix, α-helix-1. Isothermal DNA binding assays performed with the DNA consensus sequence show saturable curves with α1E2 peptide, and the α1E2 peptide is converted to an ordered conformation upon complexation. Measurements performed with non-specific DNA sequence fail to saturate, a behavior characteristic of non-specific binding. Binding of the α1E2 peptide to these DNA sequences display a different counter-ion dependence, indicating a dissimilar, sequence-dependent mechanism of interaction. Quantitative stoichiometric measurements revealed the specificity in α1E2 peptide recognition of the ACCG half-site, demonstrating capacity for discrimination of nucleic acid bases sequences without the need of a whole protein architecture.
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