The reassociation with chromatin of H1 fragments bisected with thrombin.
When fragments of H1 histone formed by bisection of H1 histone with thrombin were allowed to reassociate with H1 histone-depleted chromatin, the carboxyl-terminal segment reassociated in such a manner as to protect the micrococcal nuclease-sensitive site(s) of the nucleosome core. On the other hand, the NH2-terminal segment of H1 histone protected 20 base pairs of linker DNA adjacent to the nucleosome core particle. These data provide strong evidence that the NH2-terminal portion and the carboxyl-terminal portion of H1 histone interact with 20 base pairs of linker DNA and the core DNA of the nucleosome, respectively.
D000818:Animals; D001482:Base Composition; D002417:Cattle; D002843:Chromatin / Q000378:metabolism*; D004247:DNA / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D006657:Histones / Q000378:metabolism*; D008970:Molecular Weight; D009707:Nucleosomes / Q000378:metabolism; D010446:Peptide Fragments / Q000378:metabolism*; D013917:Thrombin / Q000378:metabolism*; D013950:Thymus Gland / Q000378:metabolism
D002843:Chromatin; D006657:Histones; D009707:Nucleosomes; D010446:Peptide Fragments; D004247:DNA; D013917:Thrombin