Contact site of histones 2A and 2B in chromatin and in solution

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Abstract
Irradiation of isolated nuclei or of a complex of histones 2A (H2A) and 2B (H2B) with UV light produces a covalent cross-link between H2A and H2B. Sequence analysis of the peptides isolated from the H2A-H2B dimer formed in solution and in nuclei demonstrated that both dimers are produced through the covalent linage of Tyr-40 and H2B and Pro-26 of H2A. Tyrosyl residues proximal to Tyr-40 did not produce a cross-link with H2A, thereby indicating that strict conformational parameters are required for production of the H2A-H2B cross-link. The precise juxtaposition of Tyr-40 of H2B and Pro-26 of H2A in this region of the H2A/H2B contact site evidently is not altered upon interaction of these histones with H3 and H4 (tetramer), DNA or other chromosomal components during nucleosome assembly.