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Attachment of origins of replicons and replication forks to the nuclear matrix. Cell 12:805–816Īelen JMA, Opstelten RJG, Wanka F (1983) Organization of DNA replication in Physarum polycephalum. A few polypeptides with the same or very similar electrophoretic mobilities were found in the residual structures of both the nuclei and the chromosomes.Īdolph KW, Cheng SM, Laemmli UK (1977) Role of nonhistone proteins in metaphase chromosome structure. On the other hand, the residual chromosome structures contained two major polypeptides of 37 and 83 kilodalton relative molecular weights that were absent from the nuclear matrix preparations. The major nuclear matrix proteins, i.e., the lamins A, B, and C, were not found in the chromosomes and chromosome scaffolds. Residual protein structures were prepared from isolated nuclei by the same procedures. Protein compositions of both structures as obtained by SDS-polyacrylamide gel electrophoresis were essentially the same. Residual protein structures were also obtained by digesting isolated chromosomes with staphylococcal nuclease. Chromosomes with minimal cytoplasmic contamination were obtained by a simple procedure using a pH 8 isolation medium containing Triton X-100 and polyamines, and residual protein-DNA complexes were prepared by extraction with 2 M NaCl. Residual protein structures were prepared from isolated chromosomes and interphase nuclei of in vitro cultured bovine liver cells and the protein compositions were analysed.
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