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Nucleic Acids Research, 1981, Vol. 9, No. 10 2335-2349
© 1981

CHEMISTRY

Temperature mediated variation of DNA secondary structure in (A.T) clusters; evidence by use of the oligopeptide antibiotic netropsin as a structural probe

K.E. Reinert+, Dörthe Geller and E. Stutter

Academy of Sciences of the GDR, Central Institute of Microbiology and Experimental Therapy, Department of Biophysical Chemistry DDR-69 Jena, Beutenbergstr. 11, GDR

+To whom correspondence should be addressed

Received March 27, 1981. The titration viscometric investigation of the multi-mode interaction of netropsin (Nt) with (A.T) clusters of NaDNA12 and NH4DNA10 has been extended to different temperatures. The position of two boundaries on the r-scale (r= [NTbound; /[DNA-P]) with increasing temperature steadily (rI/II) or more abruptly (rO/I) shifts to lower values. For the most (A.T) rich Nt-binding sites of modes (O), (I) and (II) this observation suggests the existence of an equilibrium between different DNA seoondary structures with a different translation per base pair. The mode specific changes {delta}L1Nt of DNA contour length as induced by one Nt molecule proved to be almost independent of temperature. Concomitant stiffening effects increase with decreasing temperature, contrary to initial expectation. Conformational variability of (A.T) clusters may represent an essential feature in specific or selective DNA-protein interaction.


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