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.