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Updated: May 25, 2026

Purification of H3 and H4 Histone Proteins and the Quantification of Acetylated Histone Marks in Cells and Brain Tissue
Published on: November 30, 2018
Dietary restriction increases site-specific histone H3 acetylation in rat liver: possible modulation by sirtuins
Kyojiro Kawakami1, Akihiro Nakamura, Sataro Goto
1Juntendo University Graduate School, Institute of Health and Sports Science & Medicine, Hiragagakuendai 1-1, Inzai-shi, Chiba 270-1695, Japan.
Abstract:
We studied dietary restriction (DR) related changes of site-specific acetylation of histone H3 in rat livers to explore a possible link to histone modifications and sirtuin levels with anti-aging effects of DR. The acetylation at lysine residue 9, 27 and 56 in H3 was 20-30% higher in DR animals compared with ad libitum fed counterparts. SIRT6, one of histone deacetylases, was significantly decreased by DR and thereby may be involved in an increase in the histone acetylation. Our findings suggest that upregulation of chromatin activities through increased histone acetylation is a mechanism of anti-aging effects of DR.
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