Abstract
The homology of N-termini of histones, H2A and H4, was examined. It was proposed that the N-terminus common to both histones, “Ser1-Gly2-Arg3-Gly4-Lys5-(X)6-Gly7-Gly8-Lys9-X10-(X) 11-(X)12-Lys13-X14-X15-Ala16-Lys17”has fundamental importance to gene regulation. The acetylation of Lys residues has a significance for gene regulation in view of the location of four molecules of H2A and H4 in the nucleosome. The possibility of folding the pseudo-βαβ-structure by N-terminus of H2A was discussed.
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