Chemical Labeling and Enrichment of Histone Glyoxal Adducts

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

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish (US)
JournalACS Chemical Biology
DOIs
StateAccepted/In press - 2021
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine

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