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Abstract
eukaryote nucleus, DNA exists as a highly ordered nucleoprotein complex, chromatin, whose organization regulates ultimately various functional states of the cell. To better understand this organiza- tion, it is of interest to know the subchromatin locali- zation of proteins which influence functional activity of chromatin. Poly(ADP-ribose) polymerase, which is a ubiquitous nuclear enzyme, provides a suitable probe for this purpose, because it is firmly integrated in eukaryotic chromatin structure [l] . A chromatin fractionation technique, which yielded a fraction greatly enriched in nascent RNA and in DNA sequences transcriptionally active in vivo was developed [2,3] . The technique involves selective shearing of chromatin with DNAase II followed by differential precipitation. The nucleolytic cleavage of chromatin DNA is a mild treatment and does not lead to detectable level of chromosomal protein rearrangement relative to specific DNA sequences, which is observed during mechanical shearing of chromatin [4,5]. In this report, using this procedure, we studied the distribution of poly(ADP-ribose) polymerase activity in transcriptionally active and inactive chromatin regions. It was shown that the enzyme is not preferen- tially localized in transcriptionally active chromatin region. 2. Materials and methods 2.1.
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