Locating the folded domain of H5 histone in chicken erythrocyte higher-order fiber.
The capacity of native chicken erythrocyte chromatin to bind antibodies specific for the folded domain of histone H5 (GH5) was investigated by radioimmunoassay and electron microscopy. We measured the accessibility of GH5 to antibodies as chromatin folds from an extended (10-nm) polynucleosome chain into (30-nm) higher-order fibers, as the solvent salt concentration was increased. Half of the available antibody population reacted with unfolded chromatin. In folded fibers, exposure of antigenic determinants was dependent on prior cross-linking treatment. In the absence of such modification, antigenic sites remained fully exposed in native chromatin. However, after fixation the same material presented a substantial and progressive decrease in antibody binding as the salt concentration was raised. These results indicate an inaccessible location for the folded domain of H5 in chromatin higher-order fiber, and are discussed in this context.
D000818:Animals; D000906:Antibodies / Q000276:immunology; D000918:Antibody Specificity; D002645:Chickens; D002843:Chromatin / Q000032:analysis* / Q000276:immunology; D000939:Epitopes / Q000276:immunology; D004912:Erythrocytes / Q000648:ultrastructure*; D006657:Histones / Q000097:blood* / Q000276:immunology; D008854:Microscopy, Electron; D009994:Osmolar Concentration; D011487:Protein Conformation; D011863:Radioimmunoassay; D012965:Sodium Chloride
D000906:Antibodies; D002843:Chromatin; D000939:Epitopes; D006657:Histones; D012965:Sodium Chloride