H3.H4 tetramer directs DNA and core histone octamer assembly in the nucleosome core particle.
The way in which histones interact with DNA during in vitro assembly of nucleohistone has been examined. Chicken erythrocyte core histones H2A, H2B, H3, and H4 and lambdaDNA in 2 M NaCl were allowed to interact by stepwise decrease in the salt concentration. Binding, although weak, was first observed at 1.4 M NaCl and was essentially completed at 0.6 M NaCl. Analysis of the DNA-bound histones revealed that each of the histones in the pairs H2A,H2B and H3,H4 was always present in equimolar amounts and that the relative proportion of each pair was constant between 1.4 and 0.8 M NaCl. Evidence is presented suggesting that binding occurred via complexes of the four histones, the nature of which is likely to reflect the equilibrium among the octamer and its products of dissociation (Ruiz-Carrillo, A., & Jorcano, J.L. (1979) Biochemistry (preceding paper in this issue)). The presence of complexes of the four core histones is, however not required for the correct assembly of the nucleosome core particle. Nucleohistones obtained by adding at progressively lower ionic strengths the dimer H2A.H2B to the H3.H4-DNA complex (split reconstitutions) had the same characteristics as those assembled with the core histone complexes.
D000818:Animals; D002417:Cattle; D002645:Chickens; D003090:Coliphages; D004247:DNA / Q000378:metabolism*; D004264:DNA Topoisomerases, Type I; D004279:DNA, Viral / Q000378:metabolism*; D003851:Deoxyribonucleases; D004912:Erythrocytes; D006657:Histones / Q000097:blood / Q000378:metabolism*; D046911:Macromolecular Substances; D008836:Micrococcal Nuclease; D009698:Nucleoproteins / Q000378:metabolism*; D009994:Osmolar Concentration; D011485:Protein Binding; D012965:Sodium Chloride; D013950:Thymus Gland
D004279:DNA, Viral; D006657:Histones; D046911:Macromolecular Substances; D009698:Nucleoproteins; D012965:Sodium Chloride; D004247:DNA; D003851:Deoxyribonucleases; D008836:Micrococcal Nuclease; D004264:DNA Topoisomerases, Type I