Conformational changes in the H3 . H4 histone complex. Serological and circular dichroism studies.
The H3.H4 complex has been extracted from calf thymus chromatin in either 0.05 M NaOAc, pH 5.0, or in 2.0 M KCl, 0.1 M KPO4, pH 6.7, and both forms have been shown to consist solely of histones H3 and H4 when examined on sodium dodecyl sulfate-polyacrylamide gels. Serological and circular dichroism analyses indicate the existence of structural differences between the two forms. Dilution of the high salt form of the complex into low salt produces a time-dependent conformational change which is related to reduction in the alpha helix content of the complex and which exposes antigenic sites on the complex. The existence of multiple forms of the H3.H4 complex may be related to the dynamic equilibrium of nucleosome structure in vivo.
D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D003168:Complement Fixation Tests; D004591:Electrophoresis, Polyacrylamide Gel; D006657:Histones / Q000276:immunology; D046911:Macromolecular Substances; D011487:Protein Conformation; D013950:Thymus Gland / Q000032:analysis
D006657:Histones; D046911:Macromolecular Substances