Histone 1 is proximal to histone 2A and to A24.
Water-soluble carbodiimide crosslinks histones 1A and 1B to histone 2A and to semi-histone A24 in chromatin from mouse cells. The identities of the histone species present in the crosslinked dimers were determined by fingerprinting. The molar ratio of H1--A24 to H2A is the same as the molar ratio of A24 to H2A in these cells. The H1-H2A crosslinks form equally well in whole nuclei, lysed nuclei, and H1-containing mononucleosomes isolated from a sucrose gradient. These results suggest that there exist major H1 interactions within the nucleosome.
D000818:Animals; D001665:Binding Sites; D002234:Carbodiimides; D002467:Cell Nucleus / Q000648:ultrastructure; D002645:Chickens; D002843:Chromatin / Q000648:ultrastructure*; D002868:Chromosomal Proteins, Non-Histone / Q000378:metabolism; D004247:DNA / Q000378:metabolism; D004912:Erythrocytes / Q000648:ultrastructure; D006657:Histones / Q000378:metabolism*; D007939:Leukemia L1210; D051379:Mice; D011485:Protein Binding; D011487:Protein Conformation
D002234:Carbodiimides; D002843:Chromatin; D002868:Chromosomal Proteins, Non-Histone; D006657:Histones; D004247:DNA