Age-dependent deamidation of H1 degrees histones in chromatin of mammaliantissues

The composition of the H1 degrees histone subfractions was examined in diff erent rat and mouse tissues. Using reverse-phase HPLC and hydrophilic-inter action liquid chromatography we have found that the relative proportions of all four forms of H1 degrees differ from tissue to tissue and from species to species. In principle, we observed an age-dependent increase in the amo unt of both the N-terminally acetylated (H1 degrees a Asn-3 and H1 degrees a Asp-3) and the deamidated forms of H1 degrees (H1 degrees a Asp-3 and H1 degrees b Asp-3). Compared with the proportion of N-terminally acetylated H 1 degrees forms in liver, kidney and brain of rats and mice 20 days of age, we found an increase in these H1 degrees subfractions of up to 30% in the corresponding organs of 300-day-old animals. The proportion of deamidated H 1 degrees forms was 1.6- to 4-fold higher in the livers and 8- to 12-fold h igher in the brains of 300-day-old mice and rats, respectively, than in 20- day-old animals. The tissue-specific nature of the ratio of H1 degrees subf ractions suggests that the different forms of histone H1 degrees have speci fic individual functions. The possible biological significance of age-relat ed accumulation of N-terminal acetylated and deamidated histone H1 degrees forms is discussed in the light of our results.