Characterization of the histone core complex.
A stable histone core complex containing equimolar ratios of H2A, H2B, H3, and H4 has been isolated from chicken erythrocyte chromatin in high salt. This complex has been characterized by sedimentation and chemical cross-linking studies. In velocity ultracentrifugation, only one single sharp sedimentation boundary has been observed with sedimentation coefficient S020,w = 3.8 +/- 0.1. The molecular weight of the histone core complex has been investigated by low-speed sedimentation equilibrium studies over a wide range of protein concentration. Analysis of the apparent weight-average molecular weight as a function of concentration indicates that the histone core complex in 2 M NaCl, pH 9.0, is in equilibrium between a tetramer (H2A)(H2B)(H3)(H4) and an octamer [(H2A)(H2B)(H3)(H4)]2 species with a tetramer molecular weight of 55,000. The equilibrium constant K is approximately 1.2 X 10(-5) liter per mol at 10 degrees. Evidence of such a tetramer-octamer equilibrium in solution is also supported by the results of our chemical crosslinking experiments on the histone core complex.
D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002843:Chromatin / Q000648:ultrastructure*; D006657:Histones; D046911:Macromolecular Substances; D008970:Molecular Weight; D009994:Osmolar Concentration; D011485:Protein Binding; D011487:Protein Conformation; D014461:Ultracentrifugation
D002843:Chromatin; D006657:Histones; D046911:Macromolecular Substances
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