Effect of spermine on cleavage of plasmid DNA by nucleases S1 and Bal 31.
S1, a single-strand-specific nuclease, cleaves both strands of supercoiled DNA mostly once at unpaired sites. However, all the sites are not cleaved with the same frequency by the enzyme, there being sites of preferential cleavage and infrequent ones. Spermine was found to reduce this cleavage specificity of S1 with supercoiled plasmid DNA. A similar effect of spermine was observed with Bal 31 nuclease. Bal 31 contains in addition to S1-like activity a quasi-processive exonuclease activity that simultaneously degrades both 3'- and 5'-termini of linearized duplex DNA. Spermine stimulated the exonuclease activity. The above results were obtained within the concentration range of spermine that did not induce DNA aggregation.
D004269:DNA, Bacterial / Q000378:metabolism*; D004278:DNA, Superhelical / Q000378:metabolism*; D004587:Electrophoresis, Agar Gel; D004706:Endodeoxyribonucleases / Q000378:metabolism*; D004720:Endonucleases / Q000378:metabolism*; D009690:Nucleic Acid Conformation; D010957:Plasmids; D015719:Single-Strand Specific DNA and RNA Endonucleases; D013096:Spermine / Q000494:pharmacology*; D013379:Substrate Specificity
D004269:DNA, Bacterial; D004278:DNA, Superhelical; D013096:Spermine; D004706:Endodeoxyribonucleases; D004720:Endonucleases; C038407:exonuclease Bal 31; D015719:Single-Strand Specific DNA and RNA Endonucleases