The superstructure of chromatin and its condensation mechanism. III: Effect of monovalent and divalent cations X-ray solution scattering and hydrodynamic studies.
Solutions of rat liver and chicken erythrocyte chromatin at different ionic strengths were characterized by synchrotron X-ray solution scattering, ultracentrifugation, density and viscosity measurements. Previous observations on nuclei were extended to rat liver, calf thymus and yeast nuclei. It is shown that with monovalent cations condensation is independent of the nature of the cation whereas with divalent cations there are significant differences related to the preference of base binding over phosphate binding. The consistency of hydrodynamic and scattering results confirm the view that chromatin in solution at low ionic strength has a helix-like superstructure. A survey of X-ray and neutron scattering results in the literature shows that previous interpretations, e.g. in terms of a 10 nm filament, are incompatible with the experimental data at low resolution.
D000818:Animals; D002413:Cations, Divalent; D002414:Cations, Monovalent; D002417:Cattle; D002645:Chickens; D002843:Chromatin / Q000648:ultrastructure*; D004912:Erythrocytes / Q000648:ultrastructure; D008099:Liver / Q000648:ultrastructure; D008274:Magnesium; D015636:Magnesium Chloride; D051381:Rats; D012542:Scattering, Radiation; D013950:Thymus Gland / Q000648:ultrastructure; D014783:Viscosity; D014965:X-Rays
D002413:Cations, Divalent; D002414:Cations, Monovalent; D002843:Chromatin; D015636:Magnesium Chloride; D008274:Magnesium