Aspects of specific DNA-protein interaction; local bending of DNA molecules by in-register binding of the oligopeptide antibiotic distamycin.

Distamycin A binds strongly/moderately to DNA below/above r = 0.08 molecules bound per DNA phosphate. Titration viscometric measurements for high and low molecular weight DNA yielded the relative changes of DNA persistence length, delta alpha/alpha 0, and contour length, delta L/L0 (Nucl. Acids Res. 7 (1979) 1375). delta L/L0 is negligible/positive in the range below/above r = 0.09 at 0.2 M Na+! A two-line covering of the small groove by ligand molecules explains the increase of contour length. The characteristic delta alpha/alpha 0 drop is quantitatively interpreted by local DNA bending (kinking). The underlying theoretical basis is presented in two appendices and applied, in a third one, to literature data for the DNA-actinomycin system. The angle gamma of local DNA bending as induced by complex formation with different distamycin derivatives is presented for DNA species of different base composition. By means of appropriate model, a length mismatch per dinucleotide of (0.03(2) +/- 0.01)nm [or (0.04(3) +/- 0.01)nm] was derived from the experimentally obtained bending angle per dinucleotide of (1.6 +/- 0.4)0 [or (2.1 +/- 0.05)0], independent of DNA base composition and distamycin chain length.