Binding of polylysine to chromatin subunits and cleavage by micrococcal nuclease. A comparison of accessible sites.
Native chromatin and chromatin subunits (nucleosomes) were titrated with polylysine and digested with micrococcal nuclease and deoxyribonuclease I at individual lysine/nucleotide ratios. In contrast to earlier reports, which had been obtained using mechanically sheared chromatin, a comparison of the sites accessible for micrococcal nuclease and polylysine reveals that polylysine does not preferentially protect the micrococcal-nuclease-susceptible sites in chromatin. Similar results were obtained in digestion experiments with DNase I. From the experimental data presented we conclude that polylysine does not preferentially bind to the internucleosomal DNA, which is the prime target site for micrococcal nuclease, but rather to the total nucleosomal DNA moiety.
D000818:Animals; D002467:Cell Nucleus; D002843:Chromatin / Q000378:metabolism / Q000648:ultrastructure; D004591:Electrophoresis, Polyacrylamide Gel; D007700:Kinetics; D008099:Liver; D046911:Macromolecular Substances; D008836:Micrococcal Nuclease; D010455:Peptides / Q000378:metabolism; D011107:Polylysine / Q000378:metabolism; D011485:Protein Binding; D051381:Rats
D002843:Chromatin; D046911:Macromolecular Substances; D010455:Peptides; D011107:Polylysine; D008836:Micrococcal Nuclease