The conformation of the chromatin core particle is ionic strength-dependent.
We have examined the susceptibilities of the histones within the HeLa chromatin core particle to covalent modification by a diol-epoxide derivative of the carcinogenic polycyclic aromatic hydrocarbon benzo(a)-pyrene. Core-particle histones exhibit substantial variation in their relative susceptibilities to modification, depending upon the ionic strength of the environment. In contrast, the relative susceptibilities of either purified histones or histones in urea-denatured core particles are insensitive to changes in ionic strength. The variations in the pattern of modification of core particle histones occur primarily at ionic strengths at which the histones remain associated with core-particle DNA (0 to 0.6 M NaCl). Non-histone proteins influence the ionic strength-dependent variations in histone modification. The results imply that the ionic strength of the environment affects the conformation of the core particle and that the nucleoprotein has a flexible structure.
D001580:Benzopyrenes; D002843:Chromatin / Q000648:ultrastructure*; D002868:Chromosomal Proteins, Non-Histone; D004273:DNA, Neoplasm; D006367:HeLa Cells / Q000648:ultrastructure*; D006657:Histones; D006801:Humans; D009690:Nucleic Acid Conformation; D009994:Osmolar Concentration; D011487:Protein Conformation; D014508:Urea
D001580:Benzopyrenes; D002843:Chromatin; D002868:Chromosomal Proteins, Non-Histone; D004273:DNA, Neoplasm; D006657:Histones; D014508:Urea