Interaction of two LAC repressor protein segments with polynucleotides.

The interaction of the oligopeptides Ala-Gln-GIn-Leu-Ala-Gly-OH and Gln-Leu- Ala-Gly-OMe corresponding, respectively, to the sequence 53–58 and 55–58 of lac repressor protein with four polynucleotides was studied. The two peptides did not interact with poly dA. poly dT, poly d(A-T).poly d(A-T) or poly d(A-G).poly d(C-T). But they interacted in a characteristic way with poly d(A-C). poly d (G-T), the sequences of which are in abundance in the lac operator region. Both the peptides stabilised the melting of poly d (A-C). poly d (G-T) at a peptide to nucleotide ratio (P/N) of 4; at lower ratios, they destabilised the DNA slightly. The circular dichroism of the alternating polynucleotide with CAC/GTG sequences was perturbed by both the oligopeptides. The hexapeptide at a P/N of 4 caused the transformation of the Bform circular dichroism spectrum to a new state, characterised by strong 220 and 240 nm bands, and a rather weak long wavelength spectrum.