Identification of interacting amino acids at the histone 2A--2B binding site.
Histones 2A and 2B of calf thymus were cross-linked within intact nuclei by UV irradiation. This procedure induces the formation of covalent cross-links between noncovalently interacting residues in the histones of native chromatin. Tryptic peptide and partial sequence analysis of the cross-linked product has shown that the covalent linkage is between tyrosine-37, -40, or -42 (we have not yet determined which) of H2B and proline-26 of H2A. We conclude that these residues constitute part of the hydrophobic H2A--H2B binding domain within the nucleosomes of native chromatin.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D002467:Cell Nucleus / Q000528:radiation effects; D006657:Histones / Q000528:radiation effects; D046911:Macromolecular Substances; D010446:Peptide Fragments / Q000032:analysis; D011485:Protein Binding; D013950:Thymus Gland; D014357:Trypsin; D014466:Ultraviolet Rays
D000596:Amino Acids; D006657:Histones; D046911:Macromolecular Substances; D010446:Peptide Fragments; D014357:Trypsin