Structural transition in chromatin induced by ions in solution.
Structural transition in chromatin was measured as a function of counter ions in solution (NaCl or MgCl(2)) and of histones bound on the DNA. The addition of counter ions to aqueous solutions of chromatin, partially dehistonized chromatin, and DNA caused a drastic reduction in viscosity and a significant increase in sedimentation coefficient. Transitions occurred primarily at about 2 x 10(-3) M NaCl and 1 x 10(-5) M MgCl(2) and are interpreted as a change in structure of chromatin induced by tight binding of cations (Na(+) or Mg(++)) to DNA, either free or bound by histones, and is an intrinsic property of DNA rather than of the type of histone bound. At a given ionic condition, removal of histone H1 from chromatin had only a minor effect on the hydrodynamic properties of chromatin while removal of other histones caused a drastic change in these properties. An increase in the sedimentation coefficient of DNA was observed also for protamine. DNA complexes wherein the bound protein contains only unordered coil rather than the alpha-helices found in histones.
D000818:Animals; D002412:Cations; D002417:Cattle; D002843:Chromatin / Q000187:drug effects / Q000648:ultrastructure*; D004247:DNA; D006657:Histones; D008274:Magnesium; D009690:Nucleic Acid Conformation / Q000187:drug effects; D009994:Osmolar Concentration; D011479:Protamines; D012965:Sodium Chloride / Q000494:pharmacology; D014461:Ultracentrifugation; D014783:Viscosity
D002412:Cations; D002843:Chromatin; D006657:Histones; D011479:Protamines; D012965:Sodium Chloride; D004247:DNA; D008274:Magnesium