Amino acid contacts between histones are the same for plants and mammals. Binding-site studies using ultraviolet light and tetranitromethane.
Leek chromatin has been cross-linked by UV light and tetranitromethane. The same major H2A--H2B and H2B--H4 cross-linked dimers are formed as in mammalian chromatin. CNBr peptide mapping shows that the cross-links occur in the same regions of the histone sequence for both plants and mammals. Interspecies complexes formed between leek and calf H2A and H2B can be cross-linked by UV light with the same specificity as intraspecies H2A--H2B complexes. We conclude that certain geometric features of histone-histone binding sites are conserved precisely during evolution despite large changes in the overall histone sequence. Moreover, our data show that identification of cross-linked amino acids using binding-site probes such as UV light and tetranitromethane can yield significant information about thermodynamically important contacts within histone-histone binding sites.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D002843:Chromatin / Q000032:analysis; D006657:Histones / Q000528:radiation effects; D046911:Macromolecular Substances; D008697:Methane / Q000031:analogs & derivatives; D010446:Peptide Fragments / Q000032:analysis; D010944:Plants / Q000032:analysis*; D011485:Protein Binding; D013045:Species Specificity; D013774:Tetranitromethane; D014466:Ultraviolet Rays
D000596:Amino Acids; D002843:Chromatin; D006657:Histones; D046911:Macromolecular Substances; D010446:Peptide Fragments; D013774:Tetranitromethane; D008697:Methane