Sites of Histone/Histone Interaction in the H3 · H4 Complex

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Abstract
Sites of interaction between histones [chicken erythrocyte] H3 and H4 were probed by investigating complex formation, between histone H4 and 3 peptides cleaved by chemical means from histone H3 (residues 1-90 and 1-120 using cyanogen bromide and residues 42-135 using N-bromosuccinimide), between histone and 2 peptides cleaved from histone H4 (residues 1-84 using cyanogen bromide and residues 38-102 using chymotrypsin) and between the H4 peptide (residues 38-102) and the 3 H3 peptides (residues 1-90, 1-120 and 42-135). The criterion for complex formation is the appearance of characteristic perturbed resonances in the aromatic region of the 270 MHz proton resonance spectrum of the peptide mixture. Loss of 37 N-terminal residues from histone H4 and 41 N-terminal residues from histone H3 does not prevent complex formation, while the loss of 18 C-terminal residues from H4 and 45 C-terminal residues from H3 does prevent it; the last 15 C-terminal residues of H3 are not required for forming a complex. The regions important for complex formation are defined as residues 42-120 in histone H3 and residues 38-102 in histone H4.