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Updated: Sep 6, 2025

Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli
Published on: December 26, 2020
Preparation of Site-Specific Succinylated Histone Mimics to Investigate Its Impact on Nucleosome Dynamics
Yihang Jing1, Zheng Liu1, Xiang David Li2
1Department of Chemistry, The University of Hong Kong, Hong Kong, P. R. China.
Abstract:
Posttranslational modifications (PTMs) of histones have been demonstrated to be the key regulating mechanism of nucleosome dynamics and chromatin structure. Lysine succinylation is a recently discovered PTM that plays critical roles in metabolism, epigenetic signaling, and is correlated with several diseases. One significant challenge in studying the effects of this modification on nucleosome dynamics is to obtain site-specifically modified histones. Here, we report the rapid site-specific incorporation of a succinylation mimic into histones, which facilitates the characterization of its impact on nucleosome dynamics with a Förster resonance energy transfer (FRET) approach.
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