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Nucleic Acids Research, 1975, Vol. 2, No. 1 11-20
© 1975

Articles

The interaction of rlbonuclease T1 with DNA

Frederick G. Walz, Sandra Blddlecome and Lois Hcoverman

Department of Biological Sciences, State University of New York at Albany Albany, New York 12222, USA

Received October 18, 1974. The interaction of RNase T1 with calf thymus DNA was studied using uv difference spectroscopy and the effect of the enzyme on DNA melting. There was no indication of RNase T1 binding with native DNA. A prominent difference spectrum for RNase T1 binding with denatured DNA (d-DNA) was observed at pH 5, 25° and low ionic strength (µ = .01 M) which was depressed at higher ionic strength and pH. The normalized difference spectrum at µ = .01 M, pH 5 and 25° can be interpreted as indicating an interaction of an exposed guanine residue directly with the enzyme and a coupling of this process with the "melting" of short folded segments of d-DNA. The apparent association constant calculated per M guanine residues was 2.4 x 104 M–1 under these conditions. The results are discussed in reference to comparable studies on the interaction of RNase T1 with RNA and small guanine ligands.


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