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National Institute of Environmental Health Sciences

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Publication Detail

Title: Chemical Labeling and Enrichment of Histone Glyoxal Adducts.

Authors: Ray, Devin M; Jennings, Erin Q; Maksimovic, Igor; Chai, Xander; Galligan, James J; David, Yael; Zheng, Qingfei

Published In ACS Chem Biol, (2022 Apr 15)

Abstract: Because of their long half-lives and highly nucleophilic tails, histones are particularly susceptible to accumulating nonenzymatic covalent modifications, such as glycation. The resulting modifications can have profound effects on cellular physiology due to the regulatory role histones play in all DNA-templated processes; however, the complexity of Maillard chemistry on proteins makes tracking and enriching for glycated proteins a challenging task. Here, we characterize glyoxal (GO) modifications on histones using quantitative proteomics and an aniline-derived GO-reactive probe. In addition, we leverage this chemistry to demonstrate that the glycation regulatory proteins DJ-1 and GLO1 reduce levels of histone GO adducts. Finally, we employ a two-round pull-down method to enrich histone H3 GO glycation and map these adducts to specific chromatin regions.

PubMed ID: 35294181 Exiting the NIEHS site

MeSH Terms: No MeSH terms associated with this publication

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