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.
KANAI Life Science Catalysis Project
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.
Graduate School of Pharmaceutical Sciences, The University of Tokyo
Department of Research Project , JST