title: On mechanisms determining the interrelationships between DNA and histone components of chromatin.
abstract: The relative affinity of histones for DNA was studied by the analysis of competitive histone binding to DNA in whole histone/DNA mixtures at physiological and low ionic strengths as well as in water. Use of polyphosphate in similar experiments, as a model of DNA deprived of hydrophobic functional groups allowed us to reject the hypothesis that hydrophobic DNA-histone interaction plays a decisive role in the determination of the relative affinity of histones for DNA, because the orders of histone preference for DNA and for polyphosphate were the same. The relative histone affinity for DNA does not depend on the secondary structure of DNA or on the ionic strength of salt solutions, though the differences in the histone affinities for DNA decrease on lowering the salt concentration. The binding orders of the first and the last molecules of histone type to DNA, studied at various DNA/histone ratios in the medium of physiological ionic strength, are the following: H3+H4, H2A+H2B, H1 and H3+H4, H2A, H2B, H1. In water the binding orders of the first and the last histone molecules to DNA are identical: H3+H4, H2A, H2B+H1. It is concluded that the relative histone affinity for DNA in water/salt solutions is determined by non-ionic interactions between histones bound to DNA. The folding of DNA induced by histone-histone interaction seems to lead to the increase in the correlation between amino acid residues in the histone regions bound to DNA and the ionic DNA-histone interaction becoming stronger.
mesh_terms: D000818:Animals; D002417:Cattle; D002843:Chromatin / Q000032:analysis*; D004247:DNA / Q000032:analysis*; D006657:Histones / Q000032:analysis*; D008297:Male; D008970:Molecular Weight; D009928:Organ Specificity; D011485:Protein Binding; D011817:Rabbits; D013045:Species Specificity; D013737:Testis; D013950:Thymus Gland; D014337:Trout
chemical_list: D002843:Chromatin; D006657:Histones; D004247:DNA