학술논문
Histone H2B Deacylation Selectivity: Exploring Chromatin’s Dark Matter with an Engineered Sortase
Document Type
Article
Author
Source
Journal of the American Chemical Society; March 2022, Vol. 144 Issue: 8 p3360-3364, 5p
Subject
Language
ISSN
00027863; 15205126
Abstract
We describe a new method to produce histone H2B by semisynthesis with an engineered sortase transpeptidase. N-Terminal tail site-specifically modified acetylated, lactylated, and β-hydroxybutyrylated histone H2Bs were incorporated into nucleosomes and investigated as substrates of histone deacetylase (HDAC) complexes and sirtuins. A wide range of rates and site-specificities were observed by these enzyme forms suggesting distinct biological roles in regulating chromatin structure and epigenetics.