Histon-histone interactions within chromatin. Preliminary location of multiple contact sites between histones 2A, 2B, and 4.
The contact-site cross-linkers tetranitromethane, UV light, formaldehyde, and a monofunctional imido ester have been used to generate a collection of histone-histone dimers and trimers from nuclei and chromatin. Four different H2B-H4 dimers have been isolated. Preliminary CNBr peptide mapping has shown that all are cross-linked at different positions that are apparently clustered within the C-terminal regions of these histones. Similarily, two different H2A-H2B dimers and two different H2A-H2B-H4 trimers have been partially characterized. The data suggest a functional map for H2B in which the N-terminal third interacts with DNA, the middle third interacts with H2A, and the C-terminal third interacts with H4. We hope, by pursuing this type of analysis, to develop a detailed understanding of each histone-histone binding interaction through saturation cross-linking of the binding sites.
D000818:Animals; D002417:Cattle; D002467:Cell Nucleus / Q000648:ultrastructure; D055598:Chemical Phenomena; D002621:Chemistry; D002843:Chromatin / Q000648:ultrastructure*; D006657:Histones / Q000528:radiation effects; D046911:Macromolecular Substances; D008970:Molecular Weight; D010446:Peptide Fragments / Q000032:analysis; D013774:Tetranitromethane; D013950:Thymus Gland; D014466:Ultraviolet Rays
D002843:Chromatin; D006657:Histones; D046911:Macromolecular Substances; D010446:Peptide Fragments; D013774:Tetranitromethane