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The amino acid sequences of histones are highly conserved throughout evolution; however, the variations in their primary structures exhibit different properties between each species. This is particularly true for the C-terminal tail, which has been well characterized for the structure-function relationships of the human core histone proteins. Here, we found that the C-terminal region of histone H3 is more divergent in the C-terminal tails of amphibians than in those of mammals. Because of this difference, we examined the isolation and characterization of the C-terminal tail region of human histone H3. To achieve these goals, we prepared the core histones and the C-terminal tail peptides of human nucleosomal H3 by in vitro reconstitution with the complete core histones of Xenopus laevis, and analyzed these core histones and core histone peptides by peptide mapping and mass spectrometry. Although these peptides are the same in size to the corresponding regions of human histones, we found for the first time that the human C-terminal tail peptides were truncated during tryptic digestion. Thus, we prepared human core histone peptides and the corresponding human C-terminal tail peptides by mass spectrometry, and observed that the C-terminal tails of human histone H3 have longer tails than those of Xenopus laevis. These results show that the C-terminal tail of human histone H3 has a two-amino acid variation between amphibians and mammals,

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