| Abstract: | Earlier experiments with the use of nucleoprotein-celite chromatography revealed that DNA is bound to a replicative complex localized in the nuclear matrix by a topologically tight bond. Induction of site-specific DNA breaks by restriction nucleases in isolated nuclei of proliferating cells causes a gradual concentration-dependent liberation of DNA from the tight binding to the nuclear matrix. The DNA involved in the tight interaction with matrix proteins is especially sensitive to digestion by Sau 3A1, EcoRI, PstI, BCNI and Bam HI restrictases. One-strand DNA-specific nuclease Bal 31 also destroys the tight DNA-matrix bond. The tightness of DNA-protein bonds in chromatin particles formed after the digestion of nuclei with restrictases is dependent on the particle size. The data are summarized in a model of a topological DNA-matrix bond. |
