Spin-label study of histone H1-DNA interaction. Comparative properties of the central part of the molecule and the N and C-amino tails.
Covalent spin labelling of lysine and arginine residues in histone H1 under specified conditions allows the study of histone-DNA interaction. When the labelled histone is free in solution, the electron spin resonance spectrum is characteristic of a label moving in a viscous medium while the label becomes fully immobilized upon the interaction of histone and DNA. This property is used to study histone-DNA interactions under various conditions of ionic strength and thermal denaturation. On the other hand, spin label probes in the globular part of the molecule shows no strong immobilization upon binding to linear DNA, suggesting a special mechanism for the binding of histone H1 to chromatin.
D000818:Animals; D001120:Arginine; D002417:Cattle; D004247:DNA; D004578:Electron Spin Resonance Spectroscopy; D006657:Histones; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008239:Lysine; D011485:Protein Binding; D011489:Protein Denaturation; D013113:Spin Labels; D013696:Temperature
D006657:Histones; D013113:Spin Labels; D004247:DNA; D001120:Arginine; D008239:Lysine