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Updated: Aug 10, 2026

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones
Published on: July 25, 2019
Ubiquitin Regulation: The Histone Modifying Enzyme's Story
Jianlin Wang1,2, Zhaoping Qiu3,4, Yadi Wu5,6
1Department of Pharmacology & Nutritional Sciences, University of Kentucky School of Medicine, KY 40506, USA. jianlin.wang@uky.edu.
Abstract:
Histone post-translational modifications influence many fundamental cellular events by regulating chromatin structure and gene transcriptional activity. These modifications are highly dynamic and tightly controlled, with many enzymes devoted to the addition and removal of these modifications. Interestingly, these modifying enzymes are themselves fine-tuned and precisely regulated at the level of protein turnover by ubiquitin-proteasomal processing. Here, we focus on recent progress centered on the mechanisms regulating ubiquitination of histone modifying enzymes, including ubiquitin proteasomal degradation and the reverse process of deubiquitination. We will also discuss the potential pathophysiological significance of these processes.
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