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Updated: Aug 3, 2026

Kinetic Screening of Nuclease Activity using Nucleic Acid Probes
Published on: November 1, 2019
DNase-sensitive sites in nucleosomes. Their relative suspectibilities depend on nuclease used
Abstract:
We have used three endonucleases having different catalytic and physicochemical properties to digest HeLa nucleosomes (chromatin core particles) which had been labeled with 32P at their 5'-DNA termini. Each endonuclease nicks nucleosome DNA at the identical sites, supporting the idea that the conformation of the DNA within a nucleosome is the major factor influencing its nuclease susceptibility and indicating that nucleases can indeed yield important information as to nucleoprotein structure. On the other hand, the relaative susceptibility of a given site can differ for each nuclease, indicating that enzyme-substrate interactions unique for each enzyme influence the course of the reaction; this limits the structural information which can be obtained by using a single nuclease to study nucleoprotein structure.
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