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Issue 40, 2018
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A chemical reporter facilitates the detection and identification of lysine HMGylation on histones

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Abstract

Lysine 3-hydroxyl-3-methylglutarylation (HMG-K) is a newly identified PTM that can occur non-enzymatically in mitochondria. However, the substrate scope of this new PTM remains insufficiently explored, which has greatly hindered the progress in interpreting its regulatory mechanisms and cellular functions. Here, we report the development of an alkyne-functionalized chemical reporter (HMGAM-yne), for the detection and identification of cellular HMGylated proteins. HMGAM-yne is cell-permeable and metabolically incorporated into proteins in living cells. Subsequent biorthogonal conjugation enables fluorescence visualization and identification of the protein substrates of HMG-K. Using HMGAM-yne, we also identified Sirt5 as an ‘eraser’ that regulates HMGylation in cells. In addition to the known mitochondrial HMG-K proteins, HMGAM-yne facilitates the discovery of multiple nuclear proteins, including histones, as novel substrates of lysine HMGylation.

Graphical abstract: A chemical reporter facilitates the detection and identification of lysine HMGylation on histones

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Publication details

The article was received on 06 Jun 2018, accepted on 21 Aug 2018 and first published on 28 Aug 2018


Article type: Edge Article
DOI: 10.1039/C8SC02483A
Chem. Sci., 2018,9, 7797-7801
  • Open access: Creative Commons BY license
    All publication charges for this article have been paid for by the Royal Society of Chemistry

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    A chemical reporter facilitates the detection and identification of lysine HMGylation on histones

    X. Bao, Y. Xiong, X. Li and X. D. Li, Chem. Sci., 2018, 9, 7797
    DOI: 10.1039/C8SC02483A

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