Reversible histone glycation is associated with disease-related changes in chromatin architecture View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2019-12

AUTHORS

Qingfei Zheng, Nathaniel D. Omans, Rachel Leicher, Adewola Osunsade, Albert S. Agustinus, Efrat Finkin-Groner, Hannah D’Ambrosio, Bo Liu, Sarat Chandarlapaty, Shixin Liu, Yael David

ABSTRACT

Cellular proteins continuously undergo non-enzymatic covalent modifications (NECMs) that accumulate under normal physiological conditions and are stimulated by changes in the cellular microenvironment. Glycation, the hallmark of diabetes, is a prevalent NECM associated with an array of pathologies. Histone proteins are particularly susceptible to NECMs due to their long half-lives and nucleophilic disordered tails that undergo extensive regulatory modifications; however, histone NECMs remain poorly understood. Here we perform a detailed analysis of histone glycation in vitro and in vivo and find it has global ramifications on histone enzymatic PTMs, the assembly and stability of nucleosomes, and chromatin architecture. Importantly, we identify a physiologic regulation mechanism, the enzyme DJ-1, which functions as a potent histone deglycase. Finally, we detect intense histone glycation and DJ-1 overexpression in breast cancer tumors. Collectively, our results suggest an additional mechanism for cellular metabolic damage through epigenetic perturbation, with implications in pathogenesis. More... »

PAGES

1289

References to SciGraph publications

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/s41467-019-09192-z

    DOI

    http://dx.doi.org/10.1038/s41467-019-09192-z

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1112876522

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/30894531


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