Crosslinked histone octamer as a model of the nucleosome core.
When histones in chromatin core particles were crosslinked with dimethylsuberimidate, the resulting particles had properties closely similar to those of native core particles. A crosslinked octameric histone complex was isolated from these particles under nondenaturing conditions. Upon reaction with DNA, this octameric protein folded the DNA into a structure closely resembling that of native core particles as verified by various techniques; protein denaturants were necessary for reassociation. The histone octamer is useful as a model of the nucleosome protein core and for studying histone-DNA interactions that occur in nucleosomes.
D002843:Chromatin / Q000648:ultrastructure*; D002942:Circular Dichroism; D004247:DNA / Q000378:metabolism*; D004270:DNA, Circular / Q000378:metabolism; D004279:DNA, Viral / Q000378:metabolism; D006657:Histones / Q000378:metabolism*; D008961:Models, Structural; D009690:Nucleic Acid Conformation; D009691:Nucleic Acid Denaturation; D011485:Protein Binding; D011487:Protein Conformation; D013539:Simian virus 40; D013696:Temperature
D002843:Chromatin; D004270:DNA, Circular; D004279:DNA, Viral; D006657:Histones; D004247:DNA