Relaxation of chromatin structure upon removal of histones H2A and H2B.
Modification of chromatin from chicken erythrocytes with dimethylmaleic anhydride is accompanied by its solubilization and the dissociation of histones H1, H5, H2A and H2B. Histone H1 is the first to dissociate and H5 the last. After regeneration of the modified amino groups, residual chromatin preparations with different histone composition were studied by circular dichroism and thermal denaturation. In addition to the effects produced by the lack of histones H1 and H5, both techniques show a substantial relaxation of chromatin structure induced by the loss of histones H2A and H2B, which appear to play an important role in the superhelical folding of DNA.
D000818:Animals; D002645:Chickens; D002843:Chromatin / Q000648:ultrastructure*; D002942:Circular Dichroism; D004247:DNA / Q000032:analysis; D004912:Erythrocytes / Q000648:ultrastructure; D006657:Histones / Q000032:analysis*; D006358:Hot Temperature; D008299:Maleic Anhydrides; D009690:Nucleic Acid Conformation; D012995:Solubility
D002843:Chromatin; D006657:Histones; D008299:Maleic Anhydrides; C007474:2,3-dimethylmaleic anhydride; D004247:DNA