Studies on protein organization of nucleosomes using cross-linking.
When chromosomal proteins in chromatin or in mononucleosomes were extensively cross-linked with an imido ester, the H1-containing nonameric histone complex was revealed. In this complex, histone H1 is connected with the octamer of core histones. The cross-linking of H1 of the octamer is realized preferentially through H2a and H3 histones. Some HMG (high mortality group) proteins located presumably in the linker regions of a nucleosome fiber also take part in the formation of dimers, possibly with the histones of a nucleosomal core. The results suggest mutant interactions between some linker-associated proteins and intranucleosomal histones. Experiments involving extensive cross-linking of proteins in the purified mononucleosome subfractions demonstrated differences in the organization of core histones between 'complete' nucleosomes and nucleosomes lacking H1.
D000818:Animals; D002286:Carcinoma, Ehrlich Tumor / Q000032:analysis; D002478:Cells, Cultured; D003432:Cross-Linking Reagents / Q000494:pharmacology; D004119:Dimethyl Adipimidate / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D006657:Histones / Q000378:metabolism*; D007096:Imidoesters / Q000494:pharmacology; D007739:L Cells / Q000032:analysis; D046911:Macromolecular Substances; D051379:Mice; D009707:Nucleosomes / Q000187:drug effects / Q000378:metabolism*
D003432:Cross-Linking Reagents; D006657:Histones; D007096:Imidoesters; D046911:Macromolecular Substances; D009707:Nucleosomes; D004119:Dimethyl Adipimidate; C007471:dimethyl dithiobispropionimidate