Sites of histone/histone interaction in the H3 - H4 complex.
Sites of interaction between histones H3 and h4 have been probed by investigating complex formation, firstly between histone H4 and three peptides cleaved by chemical means from histone H3 (residues 1-90 and 1-120 using cyanogen bromide and residues 42-135 using N-bromosuccinimide), secondly between histone H3 and two peptides cleaved from histone H4 (residues 1 - 84 using cyanogen bromide and residues 38-102 using chymotrypsin) and thirdly between the H4 peptide (residues 38-102) and the three 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. It is concluded that loss of 37 N-terminal residues from histone H4 and 41 N-terminal residues from histone H3 does not prevent complex formation, whilst the loss of 18 C-terminal residues from H4 and 45 C-terminal residues from H3 does prevent it; that last 15 C-terminal residues of H3 are, however, not required for forming a complex. The regions important for complex formation are therefore defined as residues 42-120 in histone H3 and residues 38-102 in histone H4.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001974:Bromosuccinimide; D002645:Chickens; D004912:Erythrocytes; D006657:Histones / Q000097:blood / Q000302:isolation & purification; D046911:Macromolecular Substances; D009682:Magnetic Resonance Spectroscopy; D010446:Peptide Fragments / Q000032:analysis; D011485:Protein Binding; D011487:Protein Conformation
D000596:Amino Acids; D006657:Histones; D046911:Macromolecular Substances; D010446:Peptide Fragments; D001974:Bromosuccinimide