title: Non-histone chromosomal proteins. Evidence for their role in mediating the binding of histones to deoxyribonucleic acid during the cell cycle.
abstract: By selective dissociation of histones with the ionic detergent sodium deoxycholate, we have demonstrated that these basic chromosomal polypeptides, which are effective inhibitors of transcription, are more tenaciously bound to DNA in mitotic than in S-phase chromatin. Evidence is presented which suggests that cell-cycle-stage-specific non-histone chromosomal proteins can account for such variations in the association of histones with DNA. When chromatin is reconstituted with DNA and histones are pooled from S-phase and mitotic cells and either S-phase or mitotic non-histone chromosomal proteins, a preferential extraction of histones with sodium deoxycholate from chromatin reconstituted with S-phase rather than mitotic non-histone chromosomal proteins is observed. In contrast, the extractability of histones with sodium deoxycholate from nucleohistone complexes reconstituted with DNA pooled from S-phase and mitotic cells and either S-phase or mitotic histones is identical. Since non-histone chromosomal proteins rather than histones are responsible for the differences in chromatin template activity during S-phase and mitosis, we propose that non-histone chromosomal proteins may modify gene expression during the cell cycle by mediating the binding of histones to DNA.
mesh_terms: D001665:Binding Sites; D002455:Cell Division / Q000187:drug effects; D002875:Chromosomes / Q000187:drug effects / Q000378:metabolism*; D004247:DNA / Q000378:metabolism*; D003840:Deoxycholic Acid / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D006367:HeLa Cells / Q000378:metabolism; D006657:Histones / Q000378:metabolism*; D006801:Humans; D046911:Macromolecular Substances; D008938:Mitosis / Q000187:drug effects; D011485:Protein Binding
chemical_list: D006657:Histones; D046911:Macromolecular Substances; D003840:Deoxycholic Acid; D004247:DNA