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Studies on a Nuclease from Ustilago maydis

II. SUBSTRATE SPECIFICITY AND MODE OF ACTION OF THE ENZYME

From the ¹ From the National Institute for Medical Research, Mill Hill, London NW7 1AA, England

The nuclease from Ustilago maydis liberates oligonucleotides from heat-denatured DNA with a preferential attack at deoxyguanosine residues during the early course of hydrolysis. However, after exhaustive digestion, a large proportion of mononucleotides are found to accumulate. Examination of partial digests of denatured T7 DNA by sucrose gradient centrifugation indicates that the DNA is reduced progressively to smaller fragments. Single stranded circular DNA from phage X174 is refractory to hydrolysis by the enzyme. This finding suggests that the enzyme requires DNA ends for activity. When DNA radioactively labeled specifically at either the 3' end or the 5' end is digested with the nuclease, the label is liberated at a faster rate than the total nucleotide. The enzyme introduces single strand breaks into linear duplex DNA, but will not degrade circular duplex DNA.

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