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JST Press Release

February 8, 2018
Japan Science and Technology Agency (JST)
5-3, Yonbancho, Chiyoda-ku, Tokyo 102-8666

The detailed picture of Sirtuins deacylation on nucleosomale histones

New insight for the drug development for cancer or age-associated diseases based on the chromatin regulation mechanism

Chromatin structure and gene expression are dynamically regulated by post-translational modifications of histone proteins which constitute the chromosome. Histone acetylation is one of the most prominent regulatory post-translational modifications and is often a key in activating gene expression. The histone deacetylases called sirtuin are known to regulate important physiologic functions, such as metabolism, cell cycle, genome maintenance, and aging process and their aberration are known to cause cancer or other age-associated diseases. They are thus attractive medical targets for the metabolic and aging-related diseases. However, the details of the type of chemical modification and active site targeted by Sirtuins have not been elucidated. In mass spectrometry-based quantitative analysis, we provide detailed information about the acyl group- and site-selectivity of all human sirtuins on acylated nucleosomes and a useful resource in understanding chromatin regulations by histone acylations.

Program Information

KANAI Life Science Catalysis Project

Journal Information

Kana Tanabe, Jiaan Liu, Daiki Kato, Hitoshi Kurumizaka, Kenzo Yamatsugu, Motomu Kanai and Shigehiro A. Kawashima. “LC–MS/MS-based quantitative study of the acyl group- and site-selectivity of human sirtuins to acylated nucleosomes”. Scientific Reports, published online February 8, 2018, doi: 10.1038/s41598-018-21060-2.


[About Research]
Shigehiro Kawashima
Graduate School of Pharmaceutical Sciences, The University of Tokyo

[About Program]
Takeshi Ohyama
Department of Research Project , JST


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