Studies of biochemical crosstalk in chromatin with semisynthetic histones

Current Opinion in Chemical Biology
Calvin Jon Antolin LeonenChampak Chatterjee

Abstract

Reversible post-translational modifications of histone proteins in eukaryotic chromatin are closely tied to gene function and cellular development. Specific combinations of histone modifications, or marks, are implicated in distinct DNA-templated processes mediated by a range of chromatin-associated enzymes that install, erase and interpret the histone code. Mechanistic studies of the precise biochemical relationship between sets of marks and their effects on chromatin function are significantly complicated by the dynamic nature and heterogeneity of marks in cellular chromatin. Protein semisynthesis is a chemical technique that enables the piecewise assembly of uniformly and site-specifically modified histones in quantities sufficient for biophysical and biochemical analyses. Recent pioneering efforts in semisynthesis have yielded access to histones site-specifically modified by entire proteins, such as ubiquitin (Ub) and the small ubiquitin-like modifier (SUMO). Herein, we highlight key studies of biochemical crosstalk involving Ub and SUMO in chromatin that were enabled by histone semisynthesis.

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Citations

Dec 6, 2019·BioEssays : News and Reviews in Molecular, Cellular and Developmental Biology·Wladyslaw A Krajewski
Nov 28, 2019·Chemical Reviews·Robert E Thompson, Tom W Muir
Nov 17, 2020·The Journal of Organic Chemistry·Guo-Chao ChuYi-Ming Li
Nov 24, 2021·Journal of Peptide Science : an Official Publication of the European Peptide Society·Huasong AiJia-Bin Li

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